Datasets:
Synthyra
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SwissProt

Dataset card Data Studio Files Community
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Entry
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Entry Name
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Sequence
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35.2k
EC number
stringlengths
7
118
⌀
Cofactor
stringlengths
38
1.77k
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Gene Ontology (biological process)
stringlengths
18
11.3k
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Gene Ontology (cellular component)
stringlengths
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1.75k
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Gene Ontology (molecular function)
stringlengths
24
2.09k
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Pfam
stringlengths
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232
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Gene3D
stringlengths
10
250
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Protein families
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9
237
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Post-translational modification
stringlengths
16
8.52k
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Subcellular location [CC]
stringlengths
29
6.18k
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Catalytic activity
stringlengths
64
35.7k
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Kinetics
stringlengths
69
11.7k
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Pathway
stringlengths
27
908
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pH dependence
stringlengths
64
955
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Temperature dependence
stringlengths
70
1.16k
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Function [CC]
stringlengths
17
15.3k
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Organism
stringlengths
8
196
I6LNY0
BSR_PSEPU
MPFRRTLLAASLVLLITGQAPLYAAPPLSMDNGTNALTVQNSNAWVEVSASALQHNIRTLQAELAGKSRLCAVLKADAYGHGIGLVMPSIIAQGVPCVAVASNEEARVVRASGFTGQLVRVRAASLSELEDALQYDMEELVGSAEFARQADAIAARHGKTLRIHLAFNSSGMSRNGVEMATWSGRGEALQITDQKHLELVALMTHFAVEDKDDVRKGLAAFNEQTDWLIKHARLDRSKLTLHAANSFATLEVPEARLDMVRTGGALFGDTVPGRTEYKRAMQFKSRVAAVHSYPAGNTVGYDRTFTLARDSRLANITVGYSDGYRRVFTNKGHVLINGHRVPVVGKVSMNTLMVDVTDFPDVKGGNEVVLFGKQAGGEITQAEMEEINGALLADLYTVWGSSNPKILVD
5.1.1.10
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975};
peptidoglycan biosynthetic process [GO:0009252]
cytosol [GO:0005829]; periplasmic space [GO:0042597]
alanine racemase activity [GO:0008784]; arginine racemase activity [GO:0047679]; lysine racemase activity [GO:0018113]; pyridoxal phosphate binding [GO:0030170]
PF00842;PF01168;
3.20.20.10;
Alanine racemase family, Bsr subfamily
null
SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q88GJ9, ECO:0000255|HAMAP-Rule:MF_02212}.
CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid = a D-alpha-amino acid; Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975}; CATALYTIC ACTIVITY: Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975}; CATALYTIC ACTIVITY: Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069, ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975}; CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.34 mM for L-alanine {ECO:0000269|PubMed:22806802}; KM=25.4 mM for L-lysine {ECO:0000269|PubMed:23118975}; KM=14.5 mM for L-arginine {ECO:0000269|PubMed:23118975}; Vmax=18.73 mmol/min/mg enzyme with L-alanine as substrate {ECO:0000269|PubMed:22806802}; Note=kcat is 4238 min(-1) with L-alanine as substrate (PubMed:22806802). kcat is 3545 min(-1) with L-lysine as substrate. kcat is 2228 min(-1) with L-arginine as substrate (PubMed:23118975). {ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:22806802};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:22806802};
FUNCTION: Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine, and L-arginine and D-arginine (PubMed:23118975). To a lesser extent, is also able to interconvert alanine and isoleucine enantiomers (PubMed:22806802, PubMed:23118975). {ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975}.
Pseudomonas putida (Arthrobacter siderocapsulatus)
I6PL68
HEI10_ORYSJ
MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT
2.3.2.27
null
chiasma assembly [GO:0051026]; homologous chromosome pairing at meiosis [GO:0007129]; protein ubiquitination [GO:0016567]; reciprocal meiotic recombination [GO:0007131]
chiasma [GO:0005712]; chromosome [GO:0005694]
metal ion binding [GO:0046872]; transferase activity [GO:0016740]
PF14634;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22792078}. Chromosome {ECO:0000269|PubMed:22792078}. Note=Dynamic localization on the meiotic chromosomes. Initially appears as distinct foci. Later observed along the chromosomes and finally restrict to prominent foci that specially localize to chiasma sites. Extends along the chromosome in the wake of synapsis. {ECO:0000269|PubMed:22792078}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
null
null
FUNCTION: Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis. {ECO:0000269|PubMed:22792078}.
Oryza sativa subsp. japonica (Rice)
I6VSD2
TM147_CAPHI
MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTYRPAVLLLMFLSVYKAFVMETFVHLCSLGSWTALLARALVTGLLALSTLALYVAVVNVHS
null
null
multi-pass transmembrane protein insertion into ER membrane [GO:0160063]; protein localization to nuclear inner membrane [GO:0036228]; regulation of apoptotic process [GO:0042981]; regulation of cytokine production [GO:0001817]; regulation of mononuclear cell proliferation [GO:0032944]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of phagocytosis [GO:0050764]
endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]
ribosome binding [GO:0043022]
PF09767;
null
TMEM147 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27337943}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Also acts as a negative regulator of CHRM3 function, most likely by interfering with its trafficking to the cell membrane. Negatively regulates CHRM3-mediated calcium mobilization and activation of RPS6KA1/p90RSK activity. Regulates LBR localization to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9BVK8}.; FUNCTION: (Microbial infection) Involved in the immunomodulatory effects exerted by H.contortus GAL-1 on host peripheral blood mononuclear cells to down-regulate host immune response. {ECO:0000269|PubMed:27337943}.
Capra hircus (Goat)
I6WU39
OLIAC_CANSA
MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK
4.4.1.26
null
cannabinoid biosynthetic process [GO:1901696]; olivetolic acid biosynthetic process [GO:1901697]; pollen tube adhesion [GO:0009865]; terpenoid biosynthetic process [GO:0016114]
cytoplasm [GO:0005737]
cyclase activity [GO:0009975]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]
PF07876;
3.30.70.100;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22802619}.
CATALYTIC ACTIVITY: Reaction=3,5,7-trioxododecanoyl-CoA = CoA + H(+) + olivetolate; Xref=Rhea:RHEA:34123, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:66950, ChEBI:CHEBI:66957; EC=4.4.1.26; Evidence={ECO:0000269|PubMed:22802619, ECO:0000269|PubMed:26783002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34124; Evidence={ECO:0000269|PubMed:22802619, ECO:0000269|PubMed:26783002};
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:22802619). Polyketide cyclase which functions in concert with OLS/TKS to form olivetolic acid (PubMed:22802619, PubMed:26783002). Has no intrinsic polyketide synthase activity and requires the presence of OLS to produce olivetolic acid (PubMed:22802619). {ECO:0000269|PubMed:22802619, ECO:0000269|PubMed:26783002}.
Cannabis sativa (Hemp) (Marijuana)
I6WXK4
PTPB_MYCTU
MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
3.1.3.-; 3.1.3.16; 3.1.3.48
null
dephosphorylation [GO:0016311]; symbiont-mediated suppression of host defense-related programmed cell death [GO:0034054]; symbiont-mediated suppression of host inflammatory response [GO:0052036]
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; phosphatidylinositol-4,5-bisphosphate phosphatase activity [GO:0106019]; phosphatidylinositol-4-phosphate phosphatase activity [GO:0043812]; protein tyrosine phosphatase activity [GO:0004725]; ubiquitin binding [GO:0043130]
PF13350;
3.90.190.10;
Protein-tyrosine phosphatase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10986245}. Host cytoplasm {ECO:0000269|PubMed:36227980}. Host cell membrane {ECO:0000269|PubMed:36227980}. Note=Further investigation is required to determine whether PtpB is direct substrate for SecA2, the ESX/type VII secretion system, or an alternate mechanism. {ECO:0000305|PubMed:23084287}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:16271885, ECO:0000269|PubMed:17584180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:16271885, ECO:0000269|PubMed:17584180}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:17584180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000269|PubMed:17584180}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:17584180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence={ECO:0000269|PubMed:17584180}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; Evidence={ECO:0000269|PubMed:17584180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42329; Evidence={ECO:0000269|PubMed:17584180}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-4-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:45836, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:85468; Evidence={ECO:0000269|PubMed:17584180, ECO:0000269|PubMed:36227980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45837; Evidence={ECO:0000269|PubMed:17584180, ECO:0000269|PubMed:36227980}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911; Evidence={ECO:0000269|PubMed:17584180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309; Evidence={ECO:0000269|PubMed:17584180};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.291 mM for P-tyr {ECO:0000269|PubMed:17584180}; KM=0.44 mM for P-Ser {ECO:0000269|PubMed:17584180}; KM=0.253 mM for P-Thr {ECO:0000269|PubMed:17584180}; KM=0.217 mM for P-Tyr insulin {ECO:0000269|PubMed:17584180}; KM=0.327 mM for P-Tyr EGFR {ECO:0000269|PubMed:17584180}; KM=0.078 mM for P-Ser peptide {ECO:0000269|PubMed:17584180}; KM=0.076 mM for P-Thr peptide {ECO:0000269|PubMed:17584180}; KM=1.749 mM for 5'AMP {ECO:0000269|PubMed:17584180}; KM=1.196 mM for 5'IMP {ECO:0000269|PubMed:17584180}; KM=0.17 mM for pNPP {ECO:0000269|PubMed:17584180}; KM=10 mM for pNPP {ECO:0000269|PubMed:16271885}; KM=0.018 mM for PtdIns3P {ECO:0000269|PubMed:17584180}; KM=0.074 mM for PtdIns4P {ECO:0000269|PubMed:17584180}; KM=0.064 mM for PtdIns5P {ECO:0000269|PubMed:17584180}; Note=kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32 sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate. kcat is 158.31 sec(-1) with P-Tyr EGFR as substrate. kcat is 18.08 sec(-1) with P-Ser peptide as substrate. kcat is 9.12 sec(-1) with P-Thr peptide as substrate. kcat is 60.97 sec(-1) with 5'AMP as substrate. kcat is 88.40 sec(-1) with 5'IMP as substrate. kcat is 134.70 sec(-1) with pNPP as substrate. kcat is 38.5 sec(-1) with PtdIns3P as substrate. kcat is 100.3 sec(-1) with PtdIns4P as substrate. kcat is 80.5 sec(-1) with PtdIns5P as substrate. {ECO:0000269|PubMed:17584180};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is near 5.5. {ECO:0000269|PubMed:16271885};
null
FUNCTION: Essential virulence factor that promotes mycobacterial survival within host macrophages (PubMed:14617138, PubMed:16256440, PubMed:20167798, PubMed:29888212, PubMed:36227980). Acts as a phosphatase that possesses triple substrate specificity toward phosphotyrosine, phosphoserine/threonine and phosphoinositides (PubMed:10986245, PubMed:16271885, PubMed:17584180, PubMed:36227980). Supports mycobacteria survival during infection by modulating the normal host signaling pathways, attenuating the bactericidal immune responses and promoting the host cell survival (PubMed:20167798, PubMed:29888212). Inhibits host pyroptosis by disrupting the membrane localization of host gasdermin-D (GSDMD): acts by catalyzing dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of GSDMD and subsequent cytokine release and pyroptosis (PubMed:36227980). Inhibits host inflammatory responses and apoptosis through impeding the NF-kappa-B and MAPK signal pathways and TP53/p53 expression in the macrophage (PubMed:29888212). Blocks the IL6/IL-6 production by down-regulating ERK1/2, p38 and p65 activity (PubMed:20167798, PubMed:29888212). Prevents macrophage cell death by activating the Akt pathway and blocking caspase 3 activity (PubMed:20167798, PubMed:29888212). Reduces the expression of iNOS in activated macrophages and inhibits the generation of destroying reactive nitrogen intermediate NO (PubMed:29888212). {ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:14617138, ECO:0000269|PubMed:16256440, ECO:0000269|PubMed:16271885, ECO:0000269|PubMed:17584180, ECO:0000269|PubMed:20167798, ECO:0000269|PubMed:29888212, ECO:0000269|PubMed:36227980}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6WZG6
ENCAP_MYCTU
MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH
null
null
null
encapsulin nanocompartment [GO:0140737]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
null
PF04454;
3.30.2400.30;3.30.2320.10;
Encapsulin family, Family 1 subfamily
PTM: The initiator methionine is partially removed. When isolated from culture filtrate isoelectric focusing gives 3 bands, none of which are glycosylated. {ECO:0000269|PubMed:9596740}.
SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Secreted {ECO:0000269|PubMed:9596740}. Cell membrane {ECO:0000269|PubMed:9596740}; Peripheral membrane protein {ECO:0000269|PubMed:9596740}. Note=Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751132). Detected at low levels in short-term culture filtrate, the nanocompartment is very stable and may survive cell lysis, explaining its apparent secretion (Probable) (PubMed:9596740). Detected in infected host (mouse J774 cell line) exosomes (PubMed:20662102). {ECO:0000269|PubMed:20662102, ECO:0000269|PubMed:34751132, ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:34751132}.
null
null
null
null
null
FUNCTION: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:24855650, PubMed:34751132). Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo (PubMed:24855650). Probably involved in protection against oxidative damage from the host immune response (Probable) (PubMed:34751132). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity (PubMed:9596740). {ECO:0000269|PubMed:24855650, ECO:0000269|PubMed:34751132, ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:24855650}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6X235
ADPP_MYCTU
MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER
3.6.1.13; 3.6.1.58
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12906832, ECO:0000269|PubMed:27683242}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27683242}; Note=Binds 3 Mg(2+) ions per subunit (PubMed:12906832). Activity is highest with Mn(2+). Can also use Zn(2+) or Co(2+), with lower efficiency (PubMed:27683242). {ECO:0000269|PubMed:12906832, ECO:0000269|PubMed:27683242};
DNA repair [GO:0006281]; DNA replication [GO:0006260]; nucleoside phosphate metabolic process [GO:0006753]; ribose phosphate metabolic process [GO:0019693]
cytosol [GO:0005829]
8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; ADP-ribose diphosphatase activity [GO:0047631]; ADP-sugar diphosphatase activity [GO:0019144]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; metal ion binding [GO:0046872]; UDP-sugar diphosphatase activity [GO:0008768]
PF00293;
3.90.79.10;
Nudix hydrolase family
null
null
CATALYTIC ACTIVITY: Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+); Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.6.1.13; Evidence={ECO:0000269|PubMed:27683242}; CATALYTIC ACTIVITY: Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate; Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58; Evidence={ECO:0000269|PubMed:23463507}; CATALYTIC ACTIVITY: Reaction=8-oxo-GDP + H2O = 8-oxo-GMP + H(+) + phosphate; Xref=Rhea:RHEA:62356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:143554, ChEBI:CHEBI:145694; EC=3.6.1.58; Evidence={ECO:0000269|PubMed:23463507};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for ADPR (in the presence of Mg(2+) ions) {ECO:0000269|PubMed:27683242}; KM=554 uM for ADPR (in the presence of Mn(2+) ions) {ECO:0000269|PubMed:27683242}; KM=9.5 uM for 8-oxo-dGDP {ECO:0000269|PubMed:23463507}; Vmax=0.04 pmol/min/ng enzyme with 8-oxo-dGDP as substrate {ECO:0000269|PubMed:23463507}; Note=kcat is 14.4 sec(-1) with ADPR as substrate (in the presence of Mg(2+) ions). kcat is 28.9 sec(-1) with ADPR as substrate (in the presence of Mn(2+) ions) (PubMed:27683242). kcat is 0.0164 sec(-1) with 8-oxo-dGDP as substrate (PubMed:23463507). {ECO:0000269|PubMed:23463507, ECO:0000269|PubMed:27683242};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:27683242};
null
FUNCTION: Catalyzes the hydrolysis of ADP-ribose (ADPR) to AMP and ribose-5-phosphate. Can also hydrolyze ADP-mannose and ADP-glucose, with lower efficiency. Has weaker activity with NAD, GDP-sugars and UDP-sugars (PubMed:27683242). Also catalyzes the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP. Functions in concert with MutT1 to detoxify 8-oxo-dGTP to 8-oxo-dGMP and may play an important role in supporting cellular growth under oxidative stress (PubMed:23463507). The catalytic efficiency is much higher for the hydrolysis of ADPR than 8-oxo-dGTP, suggesting a more relevant biological role in hydrolysis of ADPR (PubMed:27683242). {ECO:0000269|PubMed:23463507, ECO:0000269|PubMed:27683242}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6X8D2
PKS13_MYCTU
MADVAESQENAPAERAELTVPEMRQWLRNWVGKAVGKAPDSIDESVPMVELGLSSRDAVAMAADIEDLTGVTLSVAVAFAHPTIESLATRIIEGEPETDLAGDDAEDWSRTGPAERVDIAIVGLSTRFPGEMNTPEQTWQALLEGRDGITDLPDGRWSEFLEEPRLAARVAGARTRGGYLKDIKGFDSEFFAVAKTEADNIDPQQRMALELTWEALEHARIPASSLRGQAVGVYIGSSTNDYSFLAVSDPTVAHPYAITGTSSSIIANRVSYFYDFHGPSVTIDTACSSSLVAIHQGVQALRNGEADVVVAGGVNALITPMVTLGFDEIGAVLAPDGRIKSFSADADGYTRSEGGGMLVLKRVDDARRDGDAILAVIAGSAVNHDGRSNGLIAPNQDAQADVLRRAYKDAGIDPRTVDYIEAHGTGTILGDPIEAEALGRVVGRGRPADRPALLGAVKTNVGHLESAAGAASMAKVVLALQHDKLPPSINFAGPSPYIDFDAMRLKMITTPTDWPRYGGYALAGVSSFGFGGANAHVVVREVLPRDVVEKEPEPEPEPKAAAEPAEAPTLAGHALRFDEFGNIITDSAVAEEPEPELPGVTEEALRLKEAALEELAAQEVTAPLVPLAVSAFLTSRKKAAAAELADWMQSPEGQASSLESIGRSLSRRNHGRSRAVVLAHDHDEAIKGLRAVAAGKQAPNVFSVDGPVTTGPVWVLAGFGAQHRKMGKSLYLRNEVFAAWIEKVDALVQDELGYSVLELILDDAQDYGIETTQVTIFAIQIALGELLRHHGAKPAAVIGQSLGEAASAYFAGGLSLRDATRAICSRSHLMGEGEAMLFGEYIRLMALVEYSADEIREVFSDFPDLEVCVYAAPTQTVIGGPPEQVDAILARAEAEGKFARKFATKGASHTSQMDPLLGELTAELQGIKPTSPTCGIFSTVHEGRYIKPGGEPIHDVEYWKKGLRHSVYFTHGIRNAVDSGHTTFLELAPNPVALMQVALTTADAGLHDAQLIPTLARKQDEVSSMVSTMAQLYVYGHDLDIRTLFSRASGPQDYANIPPTRFKRKEHWLPAHFSGDGSTYMPGTHVALPDGRHVWEYAPRDGNVDLAALVRAAAAHVLPDAQLTAAEQRAVPGDGARLVTTMTRHPGGASVQVHARIDESFTLVYDALVSRAGSESVLPTAVGAATAIAVADGAPVAPETPAEDADAETLSDSLTTRYMPSGMTRWSPDSGETIAERLGLIVGSAMGYEPEDLPWEVPLIELGLDSLMAVRIKNRVEYDFDLPPIQLTAVRDANLYNVEKLIEYAVEHRDEVQQLHEHQKTQTAEEIARAQAELLHGKVGKTEPVDSEAGVALPSPQNGEQPNPTGPALNVDVPPRDAAERVTFATWAIVTGKSPGGIFNELPRLDDEAAAKIAQRLSERAEGPITAEDVLTSSNIEALADKVRTYLEAGQIDGFVRTLRARPEAGGKVPVFVFHPAGGSTVVYEPLLGRLPADTPMYGFERVEGSIEERAQQYVPKLIEMQGDGPYVLVGWSLGGVLAYACAIGLRRLGKDVRFVGLIDAVRAGEEIPQTKEEIRKRWDRYAAFAEKTFNVTIPAIPYEQLEELDDEGQVRFVLDAVSQSGVQIPAGIIEHQRTSYLDNRAIDTAQIQPYDGHVTLYMADRYHDDAIMFEPRYAVRQPDGGWGEYVSDLEVVPIGGEHIQAIDEPIIAKVGEHMSRALGQIEADRTSEVGKQ
2.3.1.-
null
DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]
PF00698;PF16197;PF00109;PF02801;PF00550;PF00975;
3.40.47.10;1.10.1200.10;3.40.50.1820;3.30.70.250;3.40.366.10;
null
PTM: 4'-phosphopantetheine is transferred from CoA to specific serines of apo-Pks13 by PptT. {ECO:0000269|PubMed:16709676, ECO:0000269|PubMed:19436070}.
null
null
null
PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:23770708, ECO:0000269|PubMed:25467124}.
null
null
FUNCTION: Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:23770708, PubMed:25467124). Forms, with FadD32, the initiation module of the mycolic condensation system (PubMed:19436070, PubMed:19477415, PubMed:25467124). Synthesizes, in coupled reaction with FadD32, the biosynthetic precursors of mycolic acids, alpha-alkyl beta-ketoacids, via the condensation of two long chain fatty acid derivatives, a very long meromycoloyl-AMP and a shorter 2-carboxyacyl-CoA (PubMed:19436070, PubMed:25467124). The acyl chain of the acyl-AMP produced by FadD32 is specifically transferred onto the N-terminal ACP domain of Pks13, and then transferred onto the KS domain. The extender unit carboxyacyl-CoA is specifically loaded onto the AT domain, which catalyzes the covalent attachment of the carboxyacyl chain to its active site, and its subsequent transfer onto the P-pant arm of the C-terminal ACP domain. The KS domain catalyzes the condensation between the two loaded fatty acyl chains to produce an alpha-alkyl beta-ketothioester linked to the C-ACP domain (PubMed:19436070). Then, the thioesterase-like domain acts as a transacylase and is responsible for both the release and the transfer of the alpha-alkyl beta-ketoacyl chain onto a polyol acceptor molecule, particularly trehalose, leading to the formation of the trehalose monomycolate precursor (PubMed:25467124). {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:23770708, ECO:0000269|PubMed:25467124}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6XD65
PNCA_MYCTU
MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS
3.5.1.-; 3.5.1.19
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18201201}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:18201201, ECO:0000269|PubMed:21283666}; Note=PncA contains Mn(2+) and Fe(2+) in a molecular ratio of 1:1. PncA has only one metal center. It is believed that PncA binds iron in the natural state, although both metals can support enzymatic activity. {ECO:0000269|PubMed:18201201};
nicotinamide metabolic process [GO:0006769]; pyridine nucleotide biosynthetic process [GO:0019363]; response to antibiotic [GO:0046677]; xenobiotic metabolic process [GO:0006805]
null
ferrous iron binding [GO:0008198]; manganese ion binding [GO:0030145]; nicotinamidase activity [GO:0008936]
PF00857;
3.40.50.850;
Isochorismatase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + nicotinamide = NH4(+) + nicotinate; Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19; Evidence={ECO:0000269|PubMed:18201201}; CATALYTIC ACTIVITY: Reaction=H2O + pyrazinamide = NH4(+) + pyrazine-2-carboxylate; Xref=Rhea:RHEA:35063, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:45285, ChEBI:CHEBI:71266; Evidence={ECO:0000269|PubMed:18201201};
null
PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate from nicotinamide: step 1/1. {ECO:0000250|UniProtKB:P21369}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for the hydrolysis of nicotinamide. The enzyme activity decreases rapidly below pH 6.0 or above pH 8.0. {ECO:0000269|PubMed:18201201};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for the hydrolysis of nicotinamide. Below 25 or above 70 degrees Celsius, the enzyme loses its activity rapidly. {ECO:0000269|PubMed:18201201};
FUNCTION: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate (PubMed:18201201). Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (By similarity). {ECO:0000250|UniProtKB:P21369, ECO:0000269|PubMed:18201201}.; FUNCTION: Is involved in the activation of the first-line antituberculous drug pyrazinamide (PZA) by converting it into the active form, pyrazinoic acid. {ECO:0000269|PubMed:18201201}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6XD69
PKS12_MYCTU
MVDQLQHATEALRKALVQVERLKRTNRALLERSSEPIAIVGMSCRFPGGVDSPEGLWQMVADARDVMSEFPTDRGWDLAGLFDPDPDVRHKSYARTGGFVDGVADFDPAFFGISPSEALAMDPQHRMLLELSWEALERAGIDPTGLRGSATGVFAGLIVGGYGMLAEEIEGYRLTGMTSSVASGRVAYVLGLEGPAVSVDTACSSSLVALHMAVGSLRSGECDLALAGGVTVNATPTVFVEFSRHRGLAPDGRCKPYAGRADGVGWSEGGGMLVLQRLSDARRLGHPVLAVVVGSAVNQDGASNGLTAPNGPSQQRVVRAALANAGLSAAEVDVVEGHGTGTTLGDPIEAQALLATYGQDRGEPGEPLWLGSVKSNMGHTQAAAGVAGVIKMVLAMRHELLPATLHVDVPSPHVDWSAGAVELLTAPRVWPAGARTRRAGVSSFGISGTNAHVIIEAVPVVPRREAGWAGPVVPWVVSAKSESALRGQAARLAAYVRGDDGLDVADVGWSLAGRSVFEHRAVVVGGDRDRLLAGLDELAGDQLGGSVVRGTATAAGKTVFVFPGQGSQWLGMGIELLDTAPAFAQQIDACAEAFAEFVDWSLVDVLRGAPGAPGLDRVDVVQPVLFAVMVSLAELWKSVAVHPDAVIGHSQGEIAAAYVAGALSLRDAARVVTLRSKLLAGLAGPGGMVSIACGADQARDLLAPFGDRVSIAVVNGPSAVVVSGEVGALEELIAVCSTKELRTRRIEVDYASHSVEVEAIRGPLAEALSGIEPRSTRTVFFSTVTGNRLDTAGLDADYWYRNVRQTVLFDQAVRNACEQGYRTFIESSPHPALITGVEETFAACTDGDSEAIVVPTLGRGDGGLHRFLLSAASAFVAGVAVNWRGTLDGAGYVELPTYAFDKRRFWLSAEGSGADVSGLGLGASEHPLLGAVVDLPASGGVVLTGRLSPNVQPWLADHAVSDVVLFPGTGFVELAIRAGDEVGCSVLDELTLAAPLLLPATGSVAVQVVVDAGRDSNSRGVSIFSRADAQAGWLLHAEGILRPGSVEPGADLSVWPPAGAVTVDVADGYERLATRGYRYGPAFRGLTAMWARGEEIFAEVRLPEAAGGVGGFGVHPALLDAVLHAVVIAGDPDELALPFAWQGVSLHATGASAVRARIAPAGPSAVSVELADGLGLPVLSVASMVARPVTERQLLAAVSGSGPDRLFEVIWSPASAATSPGPTPAYQIFESVAADQDPVAGSYVRSHQALAAVQSWLTDHESGVLVVATRGAMALPREDVADLAGAAVWGLVRSAQTEHPGRIVLVDSDAATDDAAIAMALATGEPQVVLRGGQVYTARVRGSRAADAILVPPGDGPWRLGLGSAGTFENLRLEPVPNADAPLGPGQVRVAMRAIAANFRDIMITLGMFTHDALLGGEGAGVVVEVGPGVTEFSVGDSVFGFFPDGSGTLVAGDVRLLLPMPADWSYAEAAAISAVFTTAYYAFIHLADVQPGQRVLIHAGTGGVGMAAVQLARHLGLEVFATASKGKWDTLRAMGFDDDHISDSRSLEFEDKFRAATGGRGFDVVLDSLAGEFVDASLRLVAPGGVFLEMGKTDIRDPGVIAQQYPGVRYRAFDLFEPGRPRMHQYMLELATLFGDGVLRPLPVTTFDVRRAPAALRYLSQARHTGKVVMLMPGSWAAGTVLITGGTGMAGSAVARHVVARHGVRNLVLVSRRGPDAPGAAELVAELAAAGAQVQVVACDAADRAALAKVIADIPVQHPLSGVIHTAGALDDAVVMSLTPDRVDVVLRSKVDAAWHLHELTRDLDVSAFVMFSSMAGLVGSSGQANYAAANSFLDALAAHRRAHGLPAISLGWGLWDQASAMTGGLDAADLARLGREGVLALSTAEALELFDTAMIVDEPFLAPARIDLTALRAHAVAVPPMFSDLASAPTRRQVDDSVAAAKSKSALAHRLHGLPEAEQHAVLLGLVRLHIATVLGNITPEAIDPDKAFQDLGFDSLTAVEMRNRLKSATGLSLSPTLIFDYPTPNRLASYIRTELAGLPQEIKHTPAVRTTSEDPIAIVGMACRYPGGVNSPDDMWDMLIQGRDVLSEFPADRGWDLAGLYNPDPDAAGACYTRTGGFVDGVGDFDPAFFGVGPSEALAMDPQHRMLLELSWEALERAGIDPTGLRGSATGVFAGVMTQGYGMFAAEPVEGFRLTGQLSSVASGRVAYVLGLEGPAVSVDTACSSSLVALHMAVGSLRSGECDLALAGGVTVNATPDIFVEFSRWRGLSPDGRCKAFAAAADGTGFSEGGGMLVLQRLSDARRLGHPVLAVVVGSAVNQDGASNGLTAPNGPSQQRVVRAALANAGLSAAEVDVVEGHGTGTTLGDPIEAQALLATYGQDRGEPGEPLWLGSVKSNMGHTQAAAGVAGVIKMVLAMRHELLPATLHVDVPSPHVDWSAGAVELLTAPRVWPAGARTRRAGVSSFGISGTNAHVIIEAVPVVPRREAGWAGPVVPWVVSAKSESALRGQAARLAAYVRGDDGLDVADVGWSLAGRSVFEHRAVVVGGDRDRLLAGLDELAGDQLGGSVVRGTATAAGKTVFVFPGQGSQWLGMGMGLHAGYPVFAEAFNTVVGELDRHLLRPLREVMWGHDENLLNSTEFAQPALFAVEVALFRLLGSWGVRPDFVMGHSIGELSAAHVAGVLSLENAAVLVAARGRLMQALPAGGAMVAVQAAEEEVRPLLSAEVDIAAVNGPASLVISGAQNAVAAVADQLRADGRRVHQLAVSHAFHSPLMDPMIDEFAAVAAGIAIGRPTIGVISNVTGQLAGDDFGSAAYWRRHIRQAVRFADSVRFAQAAGGSRFLEVGPSGGLVASIEESLPDVAVTTMSALRKDRPEPATLTNAVAQGFVTGMDLDWRAVVGEAQFVELPTYAFQRRRFWLSGDGVAADAAGLGLAASEHALLGAVIDLPASGGVVLTGRLSPSVQGWLADHSVAGVTIFPGAGFVELAIRAGDEVGCGVVDELTLAAPLVLPASGSVAVQVVVNGPDESGVRGVSVYSRGDVGTGWVLHAEGALRAGSAEPTADLAMWPPAGAVPVEVADGYQQLAERGYGYGPAFRGLTAMWRRGDEVFAEVALPADAGVSVTGFGVHPVLLDAALHAVVLSAESAERGQGSVLVPFSWQGVSLHAAGASAVRARIAPVGPSAVSIELADGLGLPVLSVASMLARPVTDQQLRAAVSSSGPDRLFEVTWSPQPSAAVEPLPVCAWGTTEDSAAVVFESVPLAGDVVAGVYAATSSVLDVLQSWLTRDGAGVLVVMTRGAVALPGEDVTDLAGAAVWGLVRSAQTEHPGRIVLVDSDAPLDDSALAAVVTTGEPQVLWRRGEVYTARVHGSRAVGGLLVPPSDRPWRLAMSTAGTFENLRLELIPDADAPLGPGQVRVAVSAIAANFRDVMIALGLYPDPDAVMGVEACGVVIETSLNKGSFAVGDRVMGLFPEGTGTVASTDQRLLVKVPAGWSHTAAATTSVVFATAHYALVDLAAARSGQRVLIHAGTGGVGMAAVQLARHLGLEVFATASKGKWDTLRAMGFDDDHISDSRSLEFEDKFRAATGGRGFDVVLDSLAGEFVDASLRLVAPGGVFLEMGKTDIRDPGVIAQQYPGVRYRAFDLFEPGPDRIAQILAELATLFGDGVLRPLPVTTFDVRCAPAALRYLSQARHTGKVVMLMPGSWAAGTVLITGGTGMAGSAVARHVVARHGVRNLVLVSRRGPDAPGAAELVAELAAAGAQVQVVACDAADRAALAKVIADIPVQHPLSGVIHTAGALDDAVVMSLTPDRVDVVLRSKVDAAWHLHELTRDLDVSAFVMFSSMAGLVGSSGQANYAAANSFLDALAAHRRAHGLPAISLGWGLWDQASAMTGGLATVDFKRFARDGIVAMSSADALQLFDTAMIVDEPFMLPAHIDFAALKVKFDGGTLPPMFVDLINAPTRRQVDDSLAAAKSKSALLQRLEGLPEDEQHAVLLDLVRSHIATVLGSASPEAIDPDRAFQELGFDSLTAVEMRNRLKSATGLALSPTLIFDYPNSAALAGYMRRELLGSSPQDTSAVAAGEAELQRIVASIPVKRLRQAGVLDLLLALANETETSGQDPALAPTAEQEIADMDLDDLVNAAFRNDDE
2.3.1.295
null
DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; identical protein binding [GO:0042802]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;
3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;
null
null
null
CATALYTIC ACTIVITY: Reaction=5 (S)-methylmalonyl-CoA + a medium-chain fatty acyl-CoA + 32 H(+) + 5 malonyl-CoA + 22 NADPH = a mycoketide-CoA + 10 CO2 + 10 CoA + 11 H2O + 22 NADP(+); Xref=Rhea:RHEA:58028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90546, ChEBI:CHEBI:142474; EC=2.3.1.295; Evidence={ECO:0000269|PubMed:15611286, ECO:0000269|PubMed:18613748};
null
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}.
null
null
FUNCTION: Involved in the synthesis of beta-D-mannosyl phosphomycoketide (MPM), an antigenic mycobacterial polyketide (PubMed:15611286, PubMed:18613748). Binds a fatty acyl-CoA as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths (PubMed:15611286, PubMed:18613748). Shows preference for small-/medium-chain starter fatty acyl substrates (PubMed:18613748). Uses a hybrid modularly iterative mechanism, by forming a supramolecular assembly to perform repetitive cycles of iterations (PubMed:18613748). {ECO:0000269|PubMed:15611286, ECO:0000269|PubMed:18613748}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6XFS7
RDMTR_MYCTU
MTRIIGGVAGGRRIAVPPRGTRPTTDRVRESLFNIVTARRDLTGLAVLDLYAGSGALGLEALSRGAASVLFVESDQRSAAVIARNIEALGLSGATLRRGAVAAVVAAGTTSPVDLVLADPPYNVDSADVDAILAALGTNGWTREGTVAVVERATTCAPLTWPEGWRRWPQRVYGDTRLELAERLFANV
2.1.1.-; 2.1.1.171
null
rRNA methylation [GO:0031167]
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
methyltransferase activity [GO:0008168]; nucleic acid binding [GO:0003676]
PF03602;
3.40.50.150;
Methyltransferase superfamily
PTM: Glycosylated. {ECO:0000269|PubMed:25824946}.; PTM: Phosphorylated (PubMed:25824946). In vitro, is phosphorylated by multiple mycobacterial kinases (PknA, PknB, PknD, PknH, PknJ and PknL) and by mammalian kinases (PubMed:25824946). {ECO:0000269|PubMed:25824946}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25824946}. Host cytoplasm {ECO:0000269|PubMed:25824946}. Host nucleus {ECO:0000269|PubMed:25824946}. Host nucleus, host nucleolus {ECO:0000269|PubMed:25824946}. Note=Secreted into the host cell upon mycobacterial infection (PubMed:25824946). Localizes to the nucleus in addition to the cytoplasm inside the host cell (PubMed:25824946). {ECO:0000269|PubMed:25824946}.
CATALYTIC ACTIVITY: Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.171; Evidence={ECO:0000269|PubMed:21474448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23549; Evidence={ECO:0000269|PubMed:21474448};
null
null
null
null
FUNCTION: SAM-dependent methyltransferase that binds both to RNA and DNA (PubMed:21474448). Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle (PubMed:21474448). In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery (PubMed:25824946). Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context (PubMed:25824946). {ECO:0000269|PubMed:21474448, ECO:0000269|PubMed:25824946}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6XHI4
FADA5_MYCTU
MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI
2.3.1.16
null
cholesterol catabolic process [GO:0006707]; fatty acid beta-oxidation [GO:0006635]; phenylacetate catabolic process [GO:0010124]
null
acetyl-CoA C-acyltransferase activity [GO:0003988]; identical protein binding [GO:0042802]
PF02803;PF00108;
3.40.47.10;
Thiolase-like superfamily, Thiolase family
null
null
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000269|PubMed:19822655, ECO:0000269|PubMed:25482540}; CATALYTIC ACTIVITY: Reaction=3-oxochol-4-en-22-oyl-CoA + acetyl-CoA = 3,22-dioxochol-4-en-24-oyl-CoA + CoA; Xref=Rhea:RHEA:46312, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83792, ChEBI:CHEBI:86014; Evidence={ECO:0000269|PubMed:19822655, ECO:0000269|PubMed:25482540};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for CoA {ECO:0000269|PubMed:25482540}; KM=15 uM for CoA {ECO:0000269|PubMed:19822655}; KM=11.8 uM for 3,22-dioxochol-4-en-24-oyl-CoA {ECO:0000269|PubMed:25482540}; KM=464 uM for AcAcCoA {ECO:0000269|PubMed:19822655}; Note=kcat is 0.725 sec(-1) for 3,22-dioxochol-4-en-24-oyl-CoA substrate (PubMed:25482540). kcat is 0.076 sec(-1) for AcAcCoA substrate (PubMed:19822655). kcat is 0.018 sec(-1) for CoA substrate (PubMed:19822655). {ECO:0000269|PubMed:19822655, ECO:0000269|PubMed:25482540};
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:19822655}.
null
null
FUNCTION: Involved in the beta-oxidation of the cholesterol side chain (PubMed:19822655). It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection (PubMed:19822655). Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) and acetyl-CoA (PubMed:25482540). Also able to use acetoacetyl-CoA (AcAcCoA) as substrate (PubMed:19822655). {ECO:0000269|PubMed:19822655, ECO:0000269|PubMed:25482540}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6XU97
EST45_MYCTU
MLSDDELTGLDEFALLAENAEQAGVNGPLPEVERVQAGAISALRWGGSAPRVIFLHGGGQNAHTWDTVIVGLGEPALAVDLPGHGHSAWREDGNYSPQLNSETLAPVLRELAPGAEFVVGMSLGGLTAIRLAAMAPDLVGELVLVDVTPSALQRHAELTAEQRGTVALMHGEREFPSFQAMLDLTIAAAPHRDVKSLRRGVFHNSRRLDNGNWVWRYDAIRTFGDFAGLWDDVDALSAPITLVRGGSSGFVTDQDTAELHRRATHFRGVHIVEKSGHSVQSDQPRALIEIVRGVLDTR
3.1.1.1
null
metabolic process [GO:0008152]
null
carboxylesterase activity [GO:0106435]; hydrolase activity [GO:0016787]
PF12697;
3.40.50.1820;
AB hydrolase superfamily
null
null
CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:20957207, ECO:0000269|PubMed:25354081}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:25354081}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:20957207}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:20957207}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:20957207};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl hexanoate. {ECO:0000269|PubMed:20957207};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 39 degrees Celsius for the hydrolysis of p-nitrophenyl hexanoate. {ECO:0000269|PubMed:20957207};
FUNCTION: Esterase likely involved in ester/lipid metabolism. Shows strong substrate selectivity toward short, straight chain alkyl esters with the highest activity toward four atom chains. The physiological substrate is unknown (PubMed:25354081). Is able to hydrolyze ester bonds within a wide range of p-nitrophenyl derivatives (C2-C14) in vitro (PubMed:20957207). {ECO:0000269|PubMed:20957207, ECO:0000269|PubMed:25354081}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y0R5
FOLC_MYCTU
MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGERFGPDRVRTAENLRDAIDVATSLVDDAAADPDVAGDAFSRTGIVITGSVVTAGAARTLFGRDPQ
6.3.2.12; 6.3.2.17
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P08192}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305|PubMed:18566510};
folic acid biosynthetic process [GO:0046656]; folic acid-containing compound biosynthetic process [GO:0009396]; response to antibiotic [GO:0046677]; tetrahydrofolate biosynthetic process [GO:0046654]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
ATP binding [GO:0005524]; dihydrofolate synthase activity [GO:0008841]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326]
PF02875;PF08245;
3.90.190.20;3.40.1190.10;
Folylpolyglutamate synthase family
null
null
CATALYTIC ACTIVITY: Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216; EC=6.3.2.12; Evidence={ECO:0000269|PubMed:23118010, ECO:0000269|PubMed:24366731}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738, Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005, ChEBI:CHEBI:456216; EC=6.3.2.17; Evidence={ECO:0000250|UniProtKB:P08192};
null
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. {ECO:0000305|PubMed:23118010}.; PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. {ECO:0000250|UniProtKB:P08192}.
null
null
FUNCTION: Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu) (PubMed:23118010). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives (By similarity). {ECO:0000250|UniProtKB:P08192, ECO:0000269|PubMed:23118010}.; FUNCTION: Is involved in the bioactivation of the antituberculous drug para-aminosalicylic acid (PAS). Is able to use hydroxy-dihydropteroate (H2PtePAS) as substrate, which is the product formed by the action of DHPS (FolP1) on PAS, leading to hydroxy-dihydrofolate (H2PtePAS-Glu). This compound inhibits dihydrofolate reductase DHFR (DfrA), the next enzyme in the folate pathway, and thus disrupts the folate-dependent metabolic pathways. {ECO:0000269|PubMed:23118010, ECO:0000305|PubMed:23779105}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y2J4
LIPY_MYCTU
MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA
3.1.1.3
null
lipid catabolic process [GO:0016042]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]
acetylesterase activity [GO:0008126]; triglyceride lipase activity [GO:0004806]
PF07859;PF00934;
3.40.50.1820;1.10.287.850;
Mycobacterial PE family, PGRS subfamily; 'GDXG' lipolytic enzyme family
PTM: Upon export, the PE domain is removed by proteolytic cleavage (PubMed:21471225, PubMed:31662454). Cleavage occurs at the cell surface and is not required for secretion (PubMed:31662454). Cleaved after Gly-149 by the aspartic protease PecA. May also be cleaved before Leu-98 and after Ala-136 (PubMed:31662454). {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:31662454}.
SUBCELLULAR LOCATION: [Cytosolic triacylglycerol lipase]: Cytoplasm {ECO:0000269|PubMed:29986895}.; SUBCELLULAR LOCATION: [Extracellular triacylglycerol lipase]: Secreted {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Secreted, cell wall {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693}. Cell surface {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Note=Exported to the cell surface via the ESX-5 / type VII secretion system (T7SS). {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}.
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:16354661}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:31034693}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) + octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:23684389, ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=1-butyrylglycerol + H2O = butanoate + glycerol + H(+); Xref=Rhea:RHEA:44324, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:17968, ChEBI:CHEBI:76503; Evidence={ECO:0000269|PubMed:29986895}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.57 mM for triolein (glyceryl trioleate) {ECO:0000269|PubMed:16354661}; Vmax=653.3 nmol/min/mg enzyme with triolein (glyceryl trioleate) as substrate {ECO:0000269|PubMed:16354661};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:16354661};
null
FUNCTION: Catalyzes the hydrolysis of both intracellular and extracellular triacylglycerol (TAG) (PubMed:16354661, PubMed:17938218, PubMed:21471225, PubMed:29986895, PubMed:31034693). In vitro, can also hydrolyze p-nitrophenyl (pNP) esters with various chain lengths, including pNP-acetate (C2), pNP-butyrate (C4), pNP-caproate (C6), pNP-caprylate (C8), pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16) and pNP-stearate (C18) (PubMed:23684389, PubMed:26398213). Also hydrolyzes monobutyrin, tributyrin and trioctanoin (PubMed:29986895). Overexpression results in increase of virulence characterized by reduced survival of infected mouse and increased burden of bacilli in the lungs (PubMed:24631199). Hydrolyzes internal or host-derived TAG depending on its localization (PubMed:29986895). {ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:23684389, ECO:0000269|PubMed:24631199, ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693}.; FUNCTION: [Cytosolic triacylglycerol lipase]: Hydrolyzes TAG that accumulates within mycobacterial intracytosolic lipid inclusions (ILI) (PubMed:29986895). Probably responsible for the utilization of stored long-chain TAG during the dormancy and reactivation stages of the pathogen (PubMed:16354661). {ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:29986895}.; FUNCTION: [Extracellular triacylglycerol lipase]: Hydrolyzes host-derived TAG. {ECO:0000269|PubMed:29986895}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y3Q0
CHSE5_MYCTU
MDFTTTEAAQDLGGLVDTIVDAVCTPEHQRELDKLEQRFDRELWRKLIDAGILSSAAPESLGGDGFGVLEQVAVLVALGHQLAAVPYLESVVLAAGALARFGSPELQQGWGVSAVSGDRILTVALDGEMGEGPVQAAGTGHGYRLTGTRTQVGYGPVADAFLVPAETDSGAAVFLVAAGDPGVAVTALATTGLGSVGHLELNGAKVDAARRVGGTDVAVWLGTLSTLSRTAFQLGVLERGLQMTAEYARTREQFDRPIGSFQAVGQRLADGYIDVKGLRLTLTQAAWRVAEDSLASRECPQPADIDVATAGFWAAEAGHRVAHTIVHVHGGVGVDTDHPVHRYFLAAKQTEFALGGATGQLRRIGRELAETPA
1.3.99.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26161441}; Note=Binds 1 FAD per heterodimer. {ECO:0000269|PubMed:26161441};
cholesterol catabolic process [GO:0006707]
null
acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660]
PF00441;PF02771;
1.10.540.10;2.40.110.10;1.20.140.10;
Acyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(25S)-3-oxocholest-4-en-26-oyl-CoA + A = 3-oxo-cholest-4,24-dien-26-oyl-CoA + AH2; Xref=Rhea:RHEA:46688, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:83819, ChEBI:CHEBI:86414; Evidence={ECO:0000269|PubMed:26161441};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.3 uM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.4 uM for 3-OCS-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=4.1 uM for octanoyl-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; Note=kcat is 2.7 sec(-1) for 3-OCS-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 1.5 sec(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 0.48 sec(-1) for 3-OCO-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 0.042 sec(-1) for octanoyl-CoA as substrate (at pH 8.5 and 25 degrees Celsius). {ECO:0000269|PubMed:26161441};
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:26161441}.
null
null
FUNCTION: Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA (PubMed:26161441, PubMed:26348625). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) (PubMed:26161441). It dehydrogenates only (25S)-OCS-CoA diastereomer (PubMed:26161441, PubMed:26348625). {ECO:0000269|PubMed:26161441, ECO:0000269|PubMed:26348625}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y4D2
PEPAM_MYCTU
MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR
3.5.1.28
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595};
cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; cytokinesis [GO:0000910]; peptidoglycan catabolic process [GO:0009253]
outer membrane-bounded periplasmic space [GO:0030288]
metal ion binding [GO:0046872]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]
PF01520;
3.40.630.40;
N-acetylmuramoyl-L-alanine amidase 3 family
null
SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:24019530}.
CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595};
null
PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}.
null
null
FUNCTION: Cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides (PubMed:24019530, PubMed:24311595). Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity (PubMed:24311595). May have a role in peptidoglycan fragment recycling (PubMed:24019530). {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y4U9
DYP_MYCTU
MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTLAAGSLSIGSLKGSPR
1.11.1.7
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:24855650}; Note=Tetramer binds heme in a 1:1 ratio (PubMed:24855650). Addition of hemin to purified protein yields a tetrameric protein (Probable). {ECO:0000269|PubMed:24855650, ECO:0000305|PubMed:9634230};
null
cytosol [GO:0005829]; encapsulin nanocompartment [GO:0140737]
heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]
PF20628;PF04261;
null
DyP-type peroxidase family
null
SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Note=Consistently identified in encapsulin nanocompartments isolated in situ (PubMed:34751132). Located inside the nanocompartment in E.coli (Probable). {ECO:0000269|PubMed:34751132, ECO:0000305|PubMed:24855650}.
CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:24855650, ECO:0000269|PubMed:34751132};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0 or less. {ECO:0000269|PubMed:34751132};
null
FUNCTION: Cargo of a type 1 encapsulin nanocompartment in situ; this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it is almost as protective as the intact nanocompartment; its encapsulation has a modest yet significant effect on protection against oxidative stress at low pH (PubMed:34751132). A heme-dependent peroxidase, it probably does not have deferrochelatase activity. Converts guaiacol and H2O2 to tetraguaiacol, also acts on 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Retains peroxidase activity when encapsulated but has a reduced set of substrates; acts on ABTS but not guaiacol (PubMed:24855650, PubMed:34751132). {ECO:0000269|PubMed:24855650, ECO:0000269|PubMed:34751132}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y778
FABG4_MYCTU
MAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNLLAPLRLTEGLVGNGSIGEGGRVIGLSSIAGIAGNRGQTNYATTKAGMIGITQALAPGLAAKGITINAVAPGFIETQMTAAIPLATREVGRRLNSLLQGGQPVDVAEAIAYFASPASNAVTGNVIRVCGQAMIGA
1.1.1.212
null
fatty acid elongation [GO:0030497]
null
3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0047025]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
PF13561;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
null
CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NAD(+) = a 3-oxoacyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:19913, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.212; Evidence={ECO:0000305|PubMed:23163771}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19915; Evidence={ECO:0000305|PubMed:23163771}; CATALYTIC ACTIVITY: Reaction=3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:42048, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78611; Evidence={ECO:0000269|PubMed:21081168, ECO:0000269|PubMed:23163771}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42050; Evidence={ECO:0000269|PubMed:21081168, ECO:0000269|PubMed:23163771}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-CoA + NAD(+) = 3-oxohexanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:45828, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62418, ChEBI:CHEBI:74280; Evidence={ECO:0000269|PubMed:19685079}; CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:45832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:74272; Evidence={ECO:0000269|PubMed:19685079};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=141.9 uM for acetoacetyl-CoA {ECO:0000269|PubMed:23163771}; KM=252 uM for 3-hydroxybutanoyl-CoA {ECO:0000269|PubMed:23163771}; KM=24.2 uM for NADH {ECO:0000269|PubMed:23163771}; KM=228.3 uM for NAD(+) {ECO:0000269|PubMed:23163771}; Note=kcat is 454 sec(-1) with acetoacetyl-CoA as substrate. kcat is 169 sec(-1) with 3-hydroxybutanoyl-CoA as substrate. kcat is 319 sec(-1) with NADH as substrate. kcat is 83 sec(-1) with NAD(+) as substrate. {ECO:0000269|PubMed:23163771};
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:23163771}.
null
null
FUNCTION: Catalyzes the NADH-dependent reduction of beta-ketoacyl derivatives (PubMed:19685079, PubMed:21081168, PubMed:23163771). Can accept the beta-oxo fatty acyl group covalently linked with CoA or ACP for catalysis (PubMed:23163771). Highly specific for NADH (PubMed:19685079, PubMed:21081168). Could be involved in fatty acid biosynthesis (Probable). {ECO:0000269|PubMed:19685079, ECO:0000269|PubMed:21081168, ECO:0000269|PubMed:23163771, ECO:0000305|PubMed:19685079, ECO:0000305|PubMed:23163771}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y9J2
LDT2_MYCTU
MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
2.3.2.-
null
cell wall organization [GO:0071555]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360]
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
acyltransferase activity [GO:0016746]; metal ion binding [GO:0046872]; peptidoglycan L,D-transpeptidase activity [GO:0071972]
PF17964;PF03734;
2.60.40.3710;2.60.40.3780;2.40.440.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
null
null
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
null
null
FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. {ECO:0000269|PubMed:24041897}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6Y9Q3
PRPC_MYCTU
MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
2.3.3.16; 2.3.3.5
null
carbohydrate metabolic process [GO:0005975]; propionate metabolic process, methylcitrate cycle [GO:0019679]; tricarboxylic acid cycle [GO:0006099]
cytosol [GO:0005829]
2-methylcitrate synthase activity [GO:0050440]; citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440]
PF00285;
1.10.580.10;1.10.230.10;
Citrate synthase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5; Evidence={ECO:0000250|UniProtKB:H8F0D7}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000250|UniProtKB:H8F0D7};
null
PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:18375549}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305|PubMed:18375549}.
null
null
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA. {ECO:0000269|PubMed:18375549, ECO:0000269|PubMed:22365605}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6YCA3
CHSE4_MYCTU
MRISYTPQQEELRRELRSYFATLMTPERREALSSVQGEYGVGNVYRETIAQMGRDGWLALGWPKEYGGQGRSAMDQLIFTDEAAIAGAPVPFLTINSVAPTIMAYGTDEQKRFFLPRIAAGDLHFSIGYSEPGAGTDLANLRTTAVRDGDDYVVNGQKMWTSLIQYADYVWLAVRTNPESSGAKKHRGISVLIVPTTAEGFSWTPVHTMAGPDTSATYYSDVRVPVANRVGEENAGWKLVTNQLNHERVALVSPAPIFGCLREVREWAQNTKDAGGTRLIDSEWVQLNLARVHAKAEVLKLINWELASSQSGPKDAGPSPADASAAKVFGTELATEAYRLLMEVLGTAATLRQNSPGALLRGRVERMHRACLILTFGGGTNEVQRDIIGMVALGLPRANR
1.3.99.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26161441}; Note=Binds 1 FAD per heterodimer. {ECO:0000269|PubMed:26161441};
cholesterol catabolic process [GO:0006707]
plasma membrane [GO:0005886]
flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627]
PF00441;PF02770;PF02771;
1.10.540.10;2.40.110.10;1.20.140.10;
Acyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(25S)-3-oxocholest-4-en-26-oyl-CoA + A = 3-oxo-cholest-4,24-dien-26-oyl-CoA + AH2; Xref=Rhea:RHEA:46688, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:83819, ChEBI:CHEBI:86414; Evidence={ECO:0000269|PubMed:26161441};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.3 uM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.4 uM for 3-OCS-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=4.1 uM for octanoyl-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; Note=kcat is 2.7 sec(-1) for 3-OCS-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 1.5 sec(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 0.48 sec(-1) for 3-OCO-CoA as substrate (at pH 8.5 and 25 degrees Celsius). kcat is 0.042 sec(-1) for octanoyl-CoA as substrate (at pH 8.5 and 25 degrees Celsius). {ECO:0000269|PubMed:26161441};
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:26161441}.
null
null
FUNCTION: Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA (PubMed:26161441, PubMed:26348625). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) (PubMed:26161441). It dehydrogenates only (25S)-OCS-CoA diastereomer (Probable). {ECO:0000269|PubMed:26161441, ECO:0000269|PubMed:26348625}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6YFP0
BIRA_MYCTU
MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR
6.3.4.15
null
positive regulation of cell population proliferation [GO:0008284]; protein modification process [GO:0036211]
cytoplasm [GO:0005737]; protein-containing complex [GO:0032991]
ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin-[acetyl-CoA-carboxylase] ligase activity [GO:0004077]; protein homodimerization activity [GO:0042803]
PF02237;PF03099;
2.30.30.100;
Biotin--protein ligase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.15; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11757; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; CATALYTIC ACTIVITY: Reaction=ATP + biotin + H(+) = biotinyl-5'-AMP + diphosphate; Xref=Rhea:RHEA:31115, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:62414; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31116; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; CATALYTIC ACTIVITY: Reaction=biotinyl-5'-AMP + L-lysyl-[protein] = AMP + 2 H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:59732, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:62414, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59733; Evidence={ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 uM for biotin {ECO:0000269|PubMed:18509457}; KM=21.08 uM for Mg/ATP {ECO:0000269|PubMed:18509457}; KM=0.2 mM for ATP {ECO:0000269|PubMed:24723382}; KM=5.2 uM for apo-BCCP {ECO:0000269|PubMed:18509457}; Note=kcat is 0.034 sec(-1) with biotin as substrate. kcat is 0.0282 sec(-1) with Mg/ATP as substrate. kcat is 0.030 sec(-1) with apo-BCCP as substrate (PubMed:18509457). kcat is 0.017 sec(-1) with ATP as substrate (PubMed:24723382). {ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:18509457};
null
FUNCTION: Catalyzes the transfer of biotin onto a conserved lysine residue of the biotin carboxyl carrier protein (BCCP) domain of acetyl-CoA carboxylase and converts it to active holo-BCCP (PubMed:18509457, PubMed:24723382). Forms an acyl-adenylate intermediate (PubMed:18509457, PubMed:24723382). Cannot use GTP or desthiobiotin (PubMed:18509457). {ECO:0000269|PubMed:18509457, ECO:0000269|PubMed:24723382}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I6YG32
RIMI_MYCTU
MTADTEPVTIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTMRRDSGDPS
2.3.1.255; 2.3.1.258
null
N-terminal protein amino acid acetylation [GO:0006474]
null
peptide alpha-N-acetyltransferase activity [GO:0004596]; peptide-alanine-alpha-N-acetyltransferase activity [GO:0008999]
PF00583;
3.40.630.30;
Acetyltransferase family, RimI subfamily
null
null
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein]; Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein]; Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein]; Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]; Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]; Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, ChEBI:CHEBI:133371; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, ChEBI:CHEBI:133375; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:27353550};
null
null
null
null
FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues. Able to mediate acetylation of a wide variety of N-terminal residues, with preference for hydrophobic N-termini. Acetylates GroS/GroES and GroEL1. Able to acetylate the ribosomal protein bS18, but it is unclear whether it acetylates its N-terminal alanine residue. {ECO:0000269|PubMed:27353550}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
I7C2V3
SPXN_CARAU
MKDLRTLAAYALALLLLATFVSYSRSAPMGSFQRRNWTPQAMLYLKGTQGRRFVSEDRNEGDLYDTIRLESQSQNTENLSISKAAAFLLNVLQQARDEGEPY
null
null
long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; negative regulation of heart rate [GO:0010459]; negative regulation of renal sodium excretion [GO:0035814]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of sensory perception of pain [GO:0051930]
extracellular space [GO:0005615]; transport vesicle [GO:0030133]
neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766]
PF15171;
null
Spexin family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}.
null
null
null
null
null
FUNCTION: Plays a role in the regulation of food intake and body weight and in reproduction. May also play a role as a central modulator of cardiovascular and renal function and nociception (By similarity). {ECO:0000250}.; FUNCTION: [Spexin-1]: Brain administration of the peptide inhibits food consumption. May function as a satiety factor for feeding control. Involved in the negative regulation of the reproductive axis by inhibiting luteinizing hormone secretion from pituitary cells (PubMed:23623870, PubMed:23715729). {ECO:0000269|PubMed:23623870, ECO:0000269|PubMed:23715729}.
Carassius auratus (Goldfish)
I7CA98
TODT_PSEPT
MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
null
null
phosphorelay signal transduction system [GO:0000160]
cytoplasm [GO:0005737]; protein-DNA complex [GO:0032993]
DNA-binding transcription activator activity [GO:0001216]; transcription cis-regulatory region binding [GO:0000976]
PF00196;PF00072;
3.40.50.2300;1.10.10.10;
null
PTM: Phosphorylated by TodS. {ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to three boxes in the tod promoter region in a cooperative manner. Boxes-1 and -2 are pseudopalindromes and Box-3 is a half-palindrome. {ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:18166197, ECO:0000269|PubMed:18950641, ECO:0000269|PubMed:22212183}.
Pseudomonas putida (strain DOT-T1E)
I7H727
TPS2_TOOSI
MSVPVSQIPSLKAKGVIMRRNANYHPNIWGDRFINYVPVDKMNHTCHLQAIEELKDAVRRELLTATGLSQLNLIDAIQRLGVGYHFERELEEALQHVYHKNHYHDDTEDNLYSISLRFRLLRQHGYYVSCDILNKFKDEKDNFKESLTTDVPGMLSLYEAAHPGVHGEDILDEAIAFTTTHLKSLAIDHLRNPSLASQVIHALRQPLHRGVPRLENRRYISIYQDEVSHNKALVKLFKLDFNLVQSLHKKELSEISRWWKELDLANKLPFARDRLVECYFWIIGVYYEPQYSLARKILTKTIAMGSIIDDIYDVYGTPEELNLFTDAIERWDASCMDQLPEYMQIFYEALLDLYNEIEKEIAKEGWSYRVHYAKEAMKILARGYHDESKWFHNNYIPTMEEYMHVALVTSGYTMLTTSSFLGMDNIVTKETFDWVFSGPKIIRASGTIARLMDDVKSHKFEQERGHAASAVECYMEQHGVSEQEVCKEFYQQVGNAWKDINQDFLKPTDVPMTILMRVLNLARVIDVVYKEGDGYTHVGKVMKENVASLLIDPIPV
4.2.3.-; 4.2.3.104; 4.2.3.198
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};
diterpenoid biosynthetic process [GO:0016102]; sesquiterpene biosynthetic process [GO:0051762]
null
beta-elemene synthase activity [GO:0102889]; magnesium ion binding [GO:0000287]; sesquiterpene synthase activity [GO:0010334]
PF01397;PF03936;
1.10.600.10;1.50.10.130;
Terpene synthase family, Tpsa subfamily
null
null
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate; Xref=Rhea:RHEA:47052, ChEBI:CHEBI:33019, ChEBI:CHEBI:59961, ChEBI:CHEBI:175763; EC=4.2.3.198; Evidence={ECO:0000269|PubMed:23072391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47053; Evidence={ECO:0000269|PubMed:23072391}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate; Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:23072391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557; Evidence={ECO:0000269|PubMed:23072391}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (1S,2S,4R)-beta-elemene + diphosphate; Xref=Rhea:RHEA:68712, ChEBI:CHEBI:33019, ChEBI:CHEBI:62855, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:23072391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68713; Evidence={ECO:0000269|PubMed:23072391};
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}.
null
null
FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds known for their medicinal efficacy for treating enteritis, dysentery, itch and some cancers (PubMed:21818683, PubMed:23072391). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-elemene, alpha-humulene, delta-cadinene and alpha-selinene (PubMed:21818683, PubMed:23072391). {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}.
Toona sinensis (Chinese mahogany) (Cedrela sinensis)
I7HJS4
ZN683_MOUSE
MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHLRVHSGERPFQCALCQKRFTQLAHLQKHHLVHTGERPHQCQVCHKRFSSSSNLKTHLRLHSGAKPSQCGLCPSYLTPNVYPKLHHRLRAPQLRGLTHTHLPLASLTCLAQWHQGALDLVEKKMGWTVDKVSSESKGKQG
null
null
adaptive immune response [GO:0002250]; cell fate commitment [GO:0045165]; innate immune response [GO:0045087]; natural killer cell differentiation [GO:0001779]; NK T cell differentiation [GO:0001865]; regulation of extrathymic T cell differentiation [GO:0033082]; regulation of gene expression [GO:0010468]; regulation of natural killer cell differentiation [GO:0032823]; regulation of natural killer cell differentiation involved in immune response [GO:0032826]; regulation of NK T cell differentiation [GO:0051136]; regulation of transcription by RNA polymerase II [GO:0006357]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T-cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs (PubMed:22885984, PubMed:27102484). Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T-cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (PubMed:22885984, PubMed:27102484). Also plays a role in the differentiation of both thymic and peripheral NKT cells (PubMed:22885984). Negatively regulates the accumulation of interferon-gamma (IFN-gamma) in NKT cells at steady state or after antigenic stimulation (PubMed:22885984). Positively regulates granzyme B production in NKT cells after innate stimulation (PubMed:22885984). Associates with the transcriptional repressor PRDM1/BLIMP1 to chromatin at gene promoter regions (PubMed:27102484). {ECO:0000269|PubMed:22885984, ECO:0000269|PubMed:27102484}.
Mus musculus (Mouse)
J3KML8
GFY_MOUSE
MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPGTKELHVPQNSDPKGPDIPLPSARIAGPPAPLEHPNQVAPAPQRHSRGDTVNTIIVVERVKETGVTLVSRPRGSVGGALCLFFAGTGLLIGIFLLLWCLYRRASRHRSFAHHRLRDSGDEPVLHLDAPKDPLDLYFYAPDAWVPSHIATQPPPSTPPLPPKLPPPPRGPQRLEALSPAALSPNFF
null
null
non-motile cilium assembly [GO:1905515]; protein localization to non-motile cilium [GO:0097499]; response to stimulus [GO:0050896]; sensory perception of smell [GO:0007608]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
null
null
null
null
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23926254}; Single-pass type I membrane protein {ECO:0000269|PubMed:23926254}.
null
null
null
null
null
FUNCTION: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling. {ECO:0000269|PubMed:23926254}.
Mus musculus (Mouse)
J3QMI4
CAHM3_MOUSE
MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAASPRRWGPGLNHRAPIAAPGTKLCHQLNV
null
null
ATP transport [GO:0015867]; protein heterooligomerization [GO:0051291]; response to stimulus [GO:0050896]; sensory perception of taste [GO:0050909]
basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]
monoatomic cation channel activity [GO:0005261]; voltage-gated monoatomic ion channel activity [GO:0005244]
PF14798;
null
CALHM family
PTM: N-glycosylated. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3 and ZDHHC15. Palmitoylation positively regulates CALHM1:CALHM3 channel conductance. {ECO:0000269|PubMed:33788965}.
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:30804437, ECO:0000305|PubMed:29681531}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the basolateral membrane of epithelial cells including taste cells. {ECO:0000269|PubMed:30804437}.
CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:29681531};
null
null
null
null
FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes. With CALHM1 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to membrane depolarization and low extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of small ions including Ca(2+), Na(+), K(+) and Cl(-), as well as larger ions such as ATP(4-). {ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}.
Mus musculus (Mouse)
J3QMK6
AL3B3_MOUSE
MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGVGSSGMGRYHGKFSFDTFSNQRACLLSCPGMEKLNGLRYPPYSPRRQQLLRWAIGSESCTLL
1.2.1.3
null
cellular aldehyde metabolic process [GO:0006081]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]
PF00171;
null
Aldehyde dehydrogenase family
PTM: Geranylgeranylation is important for membrane localization and enzyme activity. {ECO:0000269|PubMed:25286108}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000305|PubMed:25286108}.
CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:25286108}; CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+); Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:25286108};
null
null
null
null
FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty acids. {ECO:0000269|PubMed:25286108}.
Mus musculus (Mouse)
J3QMY9
TO6BL_MOUSE
MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMNAQGPALLLFLFVDFQSDVPVQQAKIWGLHTLLTAHLSAILSESRSTVQQSIQSAVDQVWQLYHHDAKTQQRLQASLSVAVNSIMSVLTGSTRSSFRKTCLQALEAADTQEFGVKLHRIFYDITQHQFLKHCSCDTEQHLTPEKNISAQNTKDQHKNIAQEFPEESIGQAENKRPKRGSPNHGREESRVLGSARDRSPPKSATRDRELTEVSLTARGSQTQAAHGRAQAAEAASPAGGLEDLWLQEVSNLSEWLNPGHRS
null
null
meiotic DNA double-strand break formation [GO:0042138]; reciprocal meiotic recombination [GO:0007131]
chromosome [GO:0005694]
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]
PF15091;
null
TOP6B-like family
null
SUBCELLULAR LOCATION: Chromosome {ECO:0000305}. Note=Localizes to meiotic chromosomes. {ECO:0000305}.
null
null
null
null
null
FUNCTION: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. {ECO:0000269|PubMed:26917764}.
Mus musculus (Mouse)
J3QPC3
ACTMP_MOUSE
MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
3.4.11.-
null
protein processing [GO:0016485]
cytoplasm [GO:0005737]
cysteine-type aminopeptidase activity [GO:0070005]; initiator methionyl aminopeptidase activity [GO:0004239]
PF21646;
null
ACTMAP family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:36173861}.
CATALYTIC ACTIVITY: [Actin maturation protease]: Reaction=H2O + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein] = N(alpha)-acetyl-L-methionine + N-terminal L-aspartyl-[protein]; Xref=Rhea:RHEA:74571, Rhea:RHEA-COMP:12669, Rhea:RHEA-COMP:12693, ChEBI:CHEBI:15377, ChEBI:CHEBI:64720, ChEBI:CHEBI:71670, ChEBI:CHEBI:133063; Evidence={ECO:0000269|PubMed:36173861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74572; Evidence={ECO:0000269|PubMed:36173861}; CATALYTIC ACTIVITY: [Actin maturation protease]: Reaction=H2O + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein] = N(alpha)-acetyl-L-methionine + N-terminal L-glutamyl-[protein]; Xref=Rhea:RHEA:74575, Rhea:RHEA-COMP:12668, Rhea:RHEA-COMP:12697, ChEBI:CHEBI:15377, ChEBI:CHEBI:64721, ChEBI:CHEBI:71670, ChEBI:CHEBI:133360; Evidence={ECO:0000269|PubMed:36173861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74576; Evidence={ECO:0000269|PubMed:36173861}; CATALYTIC ACTIVITY: [Actin maturation protease]: Reaction=H2O + N-terminal N(alpha)-acetyl-L-cysteinyl-L-aspartyl-[protein] = N-acetyl-L-cysteine + N-terminal L-aspartyl-[protein]; Xref=Rhea:RHEA:74579, Rhea:RHEA-COMP:12669, Rhea:RHEA-COMP:18395, ChEBI:CHEBI:15377, ChEBI:CHEBI:64720, ChEBI:CHEBI:78236, ChEBI:CHEBI:193599; Evidence={ECO:0000269|PubMed:36173861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74580; Evidence={ECO:0000269|PubMed:36173861}; CATALYTIC ACTIVITY: [Actin maturation protease]: Reaction=H2O + N-terminal N(alpha)-acetyl-L-cysteinyl-L-glutamyl-[protein] = N-acetyl-L-cysteine + N-terminal L-glutamyl-[protein]; Xref=Rhea:RHEA:74583, Rhea:RHEA-COMP:12668, Rhea:RHEA-COMP:18396, ChEBI:CHEBI:15377, ChEBI:CHEBI:64721, ChEBI:CHEBI:78236, ChEBI:CHEBI:193601; Evidence={ECO:0000269|PubMed:36173861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74584; Evidence={ECO:0000269|PubMed:36173861};
null
null
null
null
FUNCTION: Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation (PubMed:36173861). Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins Actb and Actg1 after translation (PubMed:36173861). Cleaves N-terminal acetylated cysteine of muscle alpha-actins Acta1, Actc1 and Acta2 after canonical removal of N-terminal methionine (PubMed:36173861). {ECO:0000269|PubMed:36173861}.
Mus musculus (Mouse)
J3S6Y1
TSEAR_MOUSE
MSALLMLCAVLLLLGTPSRGARPWEPCTDLRPLDILAEVVPLNGATSGIRMVQVEGVRGLQFSATEPRTTSFPASRIFSSCDFFPEEFSIIVTLRVPNLPPKKNEYLLSLLAEERDTLLLGLRYSPTQLHFLFLSEDLAGAWQTRVSFWSPGLMDSRWHTLILAVSQGSFSLTTDCGLPVDIMADVSFPPTLSVRGARFFIGSRKRTKGLFTGVIRQLVLLPGSDATPQLCPSRNARLAELSIPQVLKRLTGKPDDNEVLNYPYEADMKVTLGSRPPCTKAEGAQFWFDAAQKGLYLCAGSEWVSVLAAKTKLDYVEEHQSLHTNSETLGIEVFSIPGVGLFAAAANRKARSAIYKWTDGKFVSYQNIATHQAQSWRHFTIGKKIFLAVANFGPNERGQEFSVIYKWSPRKLKFTLYQRIATHSARDWEAFEVDGEHFLVVANHREGDNHNIDSMVYRWNPSSQLFEANQSIATSGAYDWEFFTVGPYSFLVVANTFNGTSTQVHSHLYIWLVGAFQLFQSFLTFGAADWEVFHIGERIFLAVANSHSYDVQMQAQNDSYVLSSVIYELNITAQTFVKFQDIPTCSALDWEFFSVGEDHFLVVANSFDGNTFSVNSIIYRWQGYEGFVAVHKLPTFGCRDWEAFNTTAGSYLIYSSAKEPLSRVLKLRTG
null
null
hair cycle process [GO:0022405]; Notch signaling pathway [GO:0007219]; regulation of Notch signaling pathway [GO:0008593]; sensory perception of sound [GO:0007605]; signal transduction [GO:0007165]; tooth mineralization [GO:0034505]
cell surface [GO:0009986]; ciliary membrane [GO:0060170]; extracellular region [GO:0005576]; stereocilium [GO:0032420]
null
PF03736;
2.60.120.200;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22678063}. Cell surface {ECO:0000269|PubMed:22678063}. Cell projection, stereocilium {ECO:0000269|PubMed:22678063}. Note=Secreted protein which may bind to the cell surface via a membrane receptor. {ECO:0000269|PubMed:22678063}.
null
null
null
null
null
FUNCTION: Plays a critical role in tooth and hair follicle morphogenesis through regulation of the Notch signaling pathway. May play a role in development or function of the auditory system. {ECO:0000250|UniProtKB:Q8WU66}.
Mus musculus (Mouse)
J3TRD1
L_HTRV
MNLEALCSRVLSERGLSTGEPGVYDQIFERPGLPNLEVTVDSTGVVVDVGAIPDSASQLGSSINAGVLTIPLSEAYKINHDFTFSGLTKTTDRKLSEVFPLVHDGSDSMTPDVIHTRLDGTVVVIEFTTTRSTNMGGLEAAYRSKLEKYRDPLNRRTDIMPDASIYFGIIVVSASGVLTNMPLTQDEAEELMFRFCVANEIYSQARAMDAEVELQKSEEEYEAISRARAFFTLFDYDDGKLSEAFPNSDIEMLRRFLSQPVDTSFVTTTLKEKEQEAYKRMCEEHYLKSGMSTKERLEANRSDAIDKTRALMERLHNMSSKELHSNKSTVKLPPWVVKPSDRTLDVKTDTGSGELLNHGPYGELWSRCFLEIVLGNVEGVISSPEKELEIAISDDPEADTPKAAKIKYHRFRPELSLESKHEFSLQGIEGKRWKHSARNVLKDEMSHKTMSPFVDVSNIEEFLIMNNLLNDTSFNREGLQETINLLLEKATEMHQNGLSTALNDSFKRNFNTNVVQWSMWVSCLAQELASALKQHCKPGEFIIKKLMHWPIFVIIKPTKSSSHIFYSLAIKKANIKRRLIGDVFTDTIDAGEWEFSEFKSLKTCKLTNLINLPCTMLNSIAFWREKMGVAPWISRKACSELREQVAITFLMSLEDKSTTEELVTLTRYSQMEGFVSPPLLPKPQKMVEKLEVPLRTKLQVFLFRRHLDAIVRVAASPFPIVARDGRVEWTGTFNAITGRSTGLENMVNNWYIGYYKNKEESTELNALGEMYKKIVEIEAEKPTSSEYLGWGDTSSPKRHEFSRSFLKSACISLEKEIEMRHGKSWKQSLEERVLKELGSKNLLDLATMKATSNFSKEWEAFSEVRTKEYHRSKLLEKMAELIEHGLMWYVDAAGHAWKAVLDDKCMRICLFKKNQHGGLREIYVTNANARLVQFGVETMARCVCELSPHETIANPRLKSSIIENHGLKSARQLGQGTINVNSSNDAKKWSQGHYTTKLAMVLCWFMPAKFHRFIWAGISMFRCKKMMMDLRFLEKLSTKANQKTDDDFRKDLAGAFHGNVEVPWMTQGATYLQTETGMMQGILHFTSSLLHSCVQSFYKAYFLSRLKEGIAGRTIKAAIDVLEGSDDSAIMISLKPASDNEEAMARFLTANLLYSVRVINPLFGIYSSEKSTVNTLFCVEYNSEFHFHKHLVRPTIRWVAASHQISESEALASRQEDYANLLTQCLEGGSSFSLTYLIQCAQLVHHYMLLGLCLHPLFGTFVGMLIEDPDPALGFFIMDNPAFAGGAGFRFNLWRSCKFTNLGKKYAFFFNEIQGKTKGDADYRALDATTGGTLSHSVMTYWGDRRKYQHLLDRMGLPKDWVERIDENPSILYRRPENKQELILRLAEKVHSPGVTSSFSKGHVVPRVVAAGVYLLSRHCFRYTASIHGRGASQKASLIKLLVMSSTSAERNQGRLNPNQERMLFPQVQEYERVLTLLDEVTALTGKFVVRERNIVKSRVELFQEPVDLRCKAENLIAEMWFGLKRTKLGPRLLKEEWDKLRASFSWLSTDHKETLDVGPFLSHVQFRNFIAHVDAKSRSVRLLGAPVKKSGGVTTVSQVVKSNFFPGFILDSSESLDDQERVEGVSILKHILFMTLNGPYTDEQKKAMVLETFQYFALPHAAEVVKRSRSLTLCLMKNFIEQRGGSILDQIEKAQSGTVGGFSKPQKPYRKQSGGIGYKGKGVWSGIMENTNVQILIDGDGSSNWIEEIRLSSESRLFDVIESVRRLCDDINVNNRVTSSFRGHCMVRLSNFKVKPASRVEGCPVRLMPSSFRIKELQNPDEVFLRVRGDILNLSILLQEDRVMNLLSYRARDTDISESAASYLWMNRTDFSFGKKEPSCSWMCLKTLDSWAWNQAARVLERNIKTPGIDNTAMGNIFKDCLESSLRKQGLLRSRIAEMVERHVIPLTSQELVDILEEDVDFSEMMQSDIMEGDLDIDILMEGSPMLWAAEVEEMGEAMVILSQSGKYYHLKLMDQAATTLSTILGKDGCRLLLGRPTGRSNLREQVKPYLTLLQIREGDVNWVSEYKDDTRGLDEDSAEMWG
2.7.7.48; 3.1.-.-
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27316}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (By similarity). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:31948728}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27316}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27316}; Note=For polymerase activity. Initiation activity is stronger in the presence of Mn(2+) than in the presence of Mg(2+). {ECO:0000250|UniProtKB:P27316};
DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694]
host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423]
hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA-dependent RNA polymerase activity [GO:0003968]
PF04196;PF12603;PF15518;
null
Bunyavirales RNA polymerase family
null
SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion {ECO:0000250|UniProtKB:P20470}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
null
null
null
null
FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (PubMed:31914382). These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity). {ECO:0000250|UniProtKB:A5HC98, ECO:0000250|UniProtKB:I0DF35, ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:31914382}.
Heartland virus (HTRV)
J3WAX0
GP_HTRV
MIVPIVLFLTLCPSELSAWGSPGDPIVCGVRTETNKSIQIEWKEGRSEKLCQIDRLGHVTSWLRNHSSFQGLIGQVKGRPSVSYFPEGASYPRWSGLLSPCDAEWLGLIAVSKAGDTDMIVPGPTYKGKIFVERPTYNGYKGWGCADGKSLSHSGTYCETDSSVSSGLIQGDRVLWVGEVVCQRGTPVPEDVFSELVSLSQSEFPDVCKIDGVALNQCEQESIPQPLDVAWIDVGRSHKVLMREHKTKWVQESSAKDFVCFKVGQGPCSKQEEDDCMSKGNCHGDEVFCRMAGCSARMQDNQEGCRCELLQKPGEIIVNYGGVSVRPTCYGFSRMMATLEVHKPDRELTGCTGCHLECIEGGVKIVTLTSELRSATVCASHFCASAKGGSKTTDILFHTGALVGPNSIRITGQLLDGSKFSFDGHCIFPDGCMALDCTFCKEFLRNPQCYPVKKWLFLVVVIMCCYCALMLLTNILRAIGVWGTWVFAPIKLALALGLRLAKLSKKGLVAVVTRGQMIVNDELHQVRVERGEQNEGRQGYGPRGPIRHWLYSPALILILTTSICSGCDELVHAESKSITCKSASGNEKECSVTGRALLPAVNPGQEACLHFSVPGSPDSKCLKIKVKSINLRCKQASSYYVPEAKARCTSVRRCRWAGDCQSGCPTYFSSNSFSDDWANRMDRAGLGMSGCSDGCGGAACGCFNAAPSCIFWRKWVENPSNRVWKVSPCASWVLAATIELTLPSGEVKTLEPVTGQATQMFKGVAITYLGSSIEIVGMTRLCEMKEMGTGIMALAPCNDPGHAIMGNVGEIQCSSIESAKHIRSDGCIWNADLVGIELRVDDAVCFSKLTSVEAVANFSKIPATISGVRFDQGNHGESRIYGSPLDITRVSGEFSVSFRGMRLKLSEISASCTGEITNVSGCYSCMTGASVSIKLHSSKNTTGHLKCDSDETAFSVMEGTHTYRPHMSFDKAVIDEECVLNCGGHSSKLLLKGSLVFMDVPRFVDGSYVQTYHSKVPAGGRVPNPVDWLNALFGDGITRWILGIIGVLLACVMLFVVVVAITRRLIKGLTQRAKVA
null
null
fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036]
null
PF19019;PF07243;PF07245;
2.60.40.3770;2.60.98.50;
Phlebovirus envelope glycoprotein family
PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins Glycoprotein C, and Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03518}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000250|UniProtKB:P09613}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03518}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000250|UniProtKB:P09613}.
null
null
null
null
null
FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (Probable). Plays a role in the packaging of ribonucleoproteins during virus assembly (By similarity). {ECO:0000250|UniProtKB:P03518, ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401, ECO:0000305|PubMed:33561699}.; FUNCTION: [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (PubMed:29070692). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (Probable). {ECO:0000250|UniProtKB:P03518, ECO:0000250|UniProtKB:P09613, ECO:0000269|PubMed:29070692, ECO:0000305|PubMed:33561699}.
Heartland virus (HTRV)
J4KMC1
TENS_BEAB2
MSPMKQNESESHSVSEPIAIVGSAYRFPGGCNTPSKLWDLLQQPRDILKELDPERLNLRRYYHPDGETHGSTDVSNKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQVQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRPQFFECHGTGTRAGDPVEARAISDAFLPSHRTNGGGAATTVDDPLYVGSIKTVVGHLEGCAGLAGLVKVLLSLKHGIIPPNLWFDKLNPEIARYYGPLQIPTKAIPWPELAPGTPLRASVNSFGFGGTNAHAIIERYDASQSYCSQWRRDMTEEKTIARTQNNDDVEIPVPLVLTAKTGGALWRTVDAYAQHLRQHPKLRVANLSQFMHSRRSTHRVRASFSGASREELVENMANFVQAHAADAKSPASQNRIGYSPLLIDPKEVSGILGIFTGQGAQWPAMGRDMMHQSPLFRKTIADCESVLQALPLKDAPAWSLSEELKKDASTSRLGEAEISQPLCTAVQLALVNVLTASGVYFDAVVGHSSGEIAATYASGIINLKAAMQIAYYRGLYAKLARGQSDEAGGMMAAGLSMDDAVKLCRLPEFEGRIQVAASNAPQSVTLSGDKEAIKAAKAKLDADGVFARELKVDTAYHSHHMLPCAEPYLKALLACDIQVSAPTKTPGRKCMWSSSVRGDAELLRRDRNLDSLKGPYWVANMVQTVQFSRAIQSTIWHGGPFDLAVEVGPHPALKGPTEQTLKAVYGSAPLYTGVLSRGANDAVAFSTAIGNIWSHLGPAFVDITGYQSIFSGTCEGHGGSEAPFISDLPLYPWDHDEEYWRESRISRRYRTGKDESHELLGRRMPDDNEREIRWRNLLKVSELPWTQGHRVLGEVLLPGAAYISMAIEAGRRLALDQGREVSLLEVSDVDILRPVVVADNKEGTETLFTVRLLDEYASTGKKSDELMTASFSFYIYNSPASTSIVHTCEGRIAVHLGAKLGSEAAANSTPQLPPREPSVSNLQQLDCEKLYSVFETIGLEYSGAFRRIVSSSRCLGHATATASWPTADLNDCYLVHPAILDVAFQTIFVARAHPDSGQLSSALLPSRIERVRVVPSLAMGSKLQNNENFNAAIDSWALNQTASSLTGNINVYDADSERALIQVEGFEVRAVGEPDASKDRLLFYETVWGRDISIMGLSDPIRDETSDAMVQNLSEAIERVSLFYVRQLMGELSTADRRQANWYHTRMLAAFDHHLAKVHEETHLHLRPEWLADDWTVIQTIDEAYPDAVELQMLHAVGQNVADVIRGKKHLLEVLRVDNLLDRLYTEDKGMHMANLFLANALKEITFKFPRCKILEIGAGTGATTWAALSAIGEAFDTYTYTDLSVGFFENAVERFSAFRHRMVFRALDIEKDPASQSFDLNSYDIIIATNVLHATRNLGVTLGNVRSLLKPGGYLLLNEKTGPDSLRATFNFGGLEGWWLAEEKERQLSPLMSPDGWDAQLQKAQFSGVDHIVHDVQEDQQDKQQNSMIMSQAVDDTFYARLSPLSEMANLLPMNEPLLIIGGQTTATLKMIKEIQKLLPRQWRHKVRLIASVNHLEAEGVPAHSNVICLQELDRGLFTTAMTSKCLDALKTLFINTRNLLWVTNAQHSSSMTPRASMFRGITRVLDGEIPHIRTQVLGIEPRATSSATARNLLEAFLRLRSDDGRHAANVDEDGADGSSQQVLWLHEPEAELLSNGTMMIPRVKARKSLNDTYLASTRAISTTVDARCVSVQAVAGPAKMLLRPVEDFAVEHAISSQSTDSKVHIQVESTLHIPEALDGTCLYLVCGWTRTAETSVPVIALSTSNASIVAVESKAVAMIDEADVKPETLFRVFQHMAMQALDSAVGRHGQGQSTALIYGADEELAKLTSERFAVRESKVYFASTRTSAPGDWLKVQPLLSKFALSQMMPADVEVFIDCLGDTESFDACRTLESCLSTTSTVHRLDACLLSRMSQCSPDTLADAYSHAKTQSNAEFSWNGNVQTFTAAELAGKLSHSLMHSVYMTDWQEKDSILVTVPPLQTRGLFKSDRTYLMVGAAGGLGTSICRWMVRNGARHVVVTSRNPKADPEMLNEARRYGAAVKVVPMDACSKDCVQTVVDMIRDTMPPIAGVCNAAMVLRDKLFLDMNVDHMNNVLGPKMQGTEHLDSIFAQEPLDFFVLLSSSAAILNNTGQSNYHCANLYMDSLVTNRRSRGLAASIIHVGHVCDTGYVARLVDDSKVQMSLGTTRVMSVSETDVHHAFAEAVRGGQPDSRSGSHNIIMGIEPPTKPLDVAKRKPVWISDPRLGHMLPFSTLENQMVASEQAAASAADSLAQQVSEATTDEEAAAAALKGFATKLEGILLLPLGSIGEDSAGRPVTDLGIDSLVAVEIRTWFLKQLRVDVPVMKILGGSTVGQLSALAAKLARQDAKKRAQLEEASGNQPVALPPLNDKETGPSKKGKAQEFPETVQVVGTAAERTEPLVLEASDRGGSSTANFTTSSSVSELDDSLQESTLQSSENNGESTPSKSSNCNSDSGSDNQAPREISSNGFFTQPAATARPNVLREAPMSPAQSRIWFLSKHIAEPDAYNMVFHYRVRGPLSMVRLRHALQTVTNHHECLCMCFYASADNGQPMQGLLASSASQMTIVPGGEEQDLQRELRKLKTRVWSVESGQTLELVVVGPRPGTAAAEEEEFSLLFGYHHIVMDAISFSIFLADLDKAYRMLPLDKASAGSHLDLAAHQRQQEHAGAWKESLEFWQAEFETIPEMLPPLSVALPTLQRGAVGTHRVLRELAHEQGGDAAIKKTCKNLRVSPFNLHIAVLQVVIARLGSIEDVCVGIVDANRSDSRASRMVGCFVNMLPVRSRILPSATLADVARAASSKALAAFAHGQVPLDSILDKVKAPRPAGSTPLFQVALNYRPAAAIASKQSLGGECEMELLADDFKDAENPFEISVLVSEMPGGRIAVEVVCQKSRYTMQATEALLDAYLNVLAGFLSDTAQSVGDCVVHDQSKVEHALDLGKGAQKSFGWPRTLSERVMSICQQHSTKSAIKDGRNELSYAQLASKVNHTASALVNAGCSVGSRIAVLCNPSIDAIVAMLAILHIGGVYVPLDTSLPEARHQSLASNCTPSLIISHAATRERAHKLSAVISAPGHEPARELTLDDLSPDETGYMAPLNAEPNAPAILLYTSGSTGTPKGVLLTQANFGNHIALKTDILGLQRGECVLQQSSLGFDMSLVQVFCALANGGCLVIVPQDVRRDPMELTSLMAQHKVSLTIATPSEYLAWLQYGSDALAQATSWKHLCMGGEPIPQLLKDELRRRLERKDLVVVSNCYGPTETTAAISFQSIALDSQDSHEQLPGESELANYAVGKALPNYSIRIRDPAGGAWLPVNHTGEIVIGGAGVALGYLDMPEETRARFLQTPGEEDGMLLYRTGDKGRLLSDGTLLCFGRITGDNQVKLRGLRIELGEVEAALLQASQGLIHTAVVSRRGDVLVAHCARSHESSRETTGGGGEQQDAATAILRRVSELLPQYSVPAAIALLPSLPTNANGKLDRTAIAALPLSPQDEAAAATSPSNDNNNNNTPSGGGGEKMTVRQGELRLLWERVLPRDATTTTTTNSVRITPESDFFLRGGNSLLLMKLQAAIRESMGVRVSTKALYQASTLSGMARCVAEQRSDDDEAEEDIDWAAEVAVPPSMLAQIEKLQHSSASSSSSSSSSSAGSSSTQRPRKTSGLQILLTGATGFLGGQLLERLVQSPRVSTVHCVAVPVDEQSLLEPFLQQQADGTRRKVRCYIGNLAAPALGLTAADQTALSQTADVIVHAGSMGHCLNTYATLSAPNFASTRHLCALALSRSPPIPLAFASSNRVALLTGSTAPPPGSAAAFPPPPGAQGFTASKWASEAFLEKLTASMSDVSKTKTKTTTTVMPWRVSIHRPCALISDRAPNSDALNAILRYSTSMRCVPSLPEHRAEGYLDFGQVDKVVEEMVGDILGLADERPQEGPAVVYRHHSGGVKVPIHEFREHMESVYGGRFESVQLGQWIIRAVDAGMDPLISAYLETFLEGDASMVFPYMGEQAV
2.3.1.-; 6.3.2.-
null
amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403]
null
fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;
3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;
NRP synthetase family
null
null
null
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}.
null
null
FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:18266306, PubMed:20575135, PubMed:34903054). TenS catalyzes the assembly of the polyketide-amino acid backbone (PubMed:18266306, PubMed:34903054). Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC (PubMed:18266306, PubMed:34903054). Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D (PubMed:18266306, PubMed:34903054). The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054). {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}.
Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae)
J4UHQ6
OPS1_BEAB2
MPSFFPVFSGLGSGSVFSEENVGRAEENALSPECAVLLQSCHRTFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYHHESLLEVRNLVMADLERQDTLLQARVELSAPILSTKTGKPLALSSVTTLEQVACAILDLIFIEKVDWLNLQQSIVSHTSQDALDRPINIVNYGPGLGMAPSAFAQAQEKDVCIMDAAKISKGSFQNSGASRLAWDDIAIVGMAVELPGASDADTLWQNLVDGYQACSEIPPSRFNVNDYNNGKGSRTLNTKYGNFLENPFLFDAEHFGISRREAKSMDPQQRILLQTAYRALEDAGYVPDTTTSSARDTFGCWIGNATLDYVDNLRSDIDVYYSTGTLRAFLSARISYVFGWSGPSITLDTACSSSIVALHQAARSILAGDCRSALVGAANTITSPDMYLGLDRAHFLSPSGQCKAFDASADGYCRAEGCGVFVIKRLSDALAEGDRIHGVIKAIEINQSGNTHSITHPHVPTQEALFDKMFRESRINPHEISVVEMHGTGTQAGDPNEVESVRRALCKARSPLNPVYLTSLKANIGHAEAVSGIAGLAKLILMTRNGYIPPQVSLKTLNPRIRPLGVDGAAIDANGTEWPRAGPKKARMSMLNNFGAGGSNAAVIIGEHLSQDESEAQQPACGATIFVCGVSAKNDRALVKLQETVADYLTSAGQSRKPPSLADVCATLTSRRQMYNHRVAVVASSLEELAENLRSASSHNVSKSICEAPEAVFIFSGQGSQYLGMGRELIEQYEDFAHTVNVCDGWLVKNNYPSCLAVITGEQRESEDDKVDAHTWQSFQSAIYVIEVALAKLLESWGIRPQAVAGHSLGEYAALVTAGVIRLMDGLKLVAHRAKLMMEQCDLGQTSMLAVNCSAAVITSIIEASTDFEGLAISCNNSETDCVVGGPVPQLVLLKKHLTDRAQVRSKLLDVPMAFHTAAMDPILEEFTAFAAREVRVFPPTLPVVSNVLGRTVAVGEQAFSPEYFAKQCRGTVAFDDGIKHFLALGDCESTPYRWIEIGPHPSVQPMLRGRLGKAATSHIQLTTLKKNVPPASTLSQLLSHFYQTSSGVNWRSVFSRNAHRRFKLIQLPGMPFFPSEFHVPYREMAGEPASTSQSSGDAASNVVPNSFAVHAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIEQALKRATRSSPNAAVSASHPAQPKRRNDVTSFVNAQSVERMALPRAAAPVRAAPEVSVPELVAKVCGLDAGQLGVDSRLDAHGVDSLMGIEIAAALSSALGVDVLPDTLGSCDTVGDIERLCEALSPTPVGNDVDNDSPTPGSERGSDSAISTPASVSTVDASSIDMVQIVAELCGARAEAVSPDSELRALGVDSLMFLELADRLQDLDRGIALSSNDLADCQTIGDIERLIVKRPGTPAYQSGISTKIYPEAVHASSEAVRLSAQQPATQISLLASEEAVLPQIERLLHLSQQPEEIQVGSLDRKFSGKSPLFLIHDGSGICTHYRGLRPLGRRVLALHDPKFLIQSSKQRSWASLTTMANEYASSISSTMGMTGGEDCILGGWSFGGVVAFEAARILMSRGHRVKGVVLIDSPPPIGHIPLSESIISAVTAQPAEKDAAAGSTTASKCVSPVASAIRKLVQQSFRICAGLIGDFGTSAELQQRGLSNKPVGPVPRVILLRSAVGWTPPRGYTGAAVEEMENPWLQDRRDRSLATAGWEILTGGPIQCLDIPGNHFQVFDAPNIAAVSAALVDACSEFELK
2.3.1.-
null
fatty acid biosynthetic process [GO:0006633]; organic cyclic compound biosynthetic process [GO:1901362]; secondary metabolite biosynthetic process [GO:0044550]
cytoplasm [GO:0005737]; fatty acid synthase complex [GO:0005835]; plasma membrane [GO:0005886]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]
PF00698;PF00109;PF02801;PF00550;PF16073;PF00975;
3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.30.70.250;3.40.366.10;3.10.129.110;
null
null
null
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + orsellinate; Xref=Rhea:RHEA:62972, ChEBI:CHEBI:15378, ChEBI:CHEBI:16162, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:26305932}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62973; Evidence={ECO:0000269|PubMed:26305932};
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26305932}.
null
null
FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932). OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae)
J4W0G2
ATG1_BEAB2
MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENFFAHHVVTGDILGLVEDDIPKPPKRELETIRQGEALPSSPRVQMARQLSSDPRDTRSSPKSPRSSPRSSTVNSSADAAPRRQSQNAERRLSISSHNSGQGLGIQRPAPPIQSHTAPNHPRAADRSGREPQPSSLRVARQPSDVSLTEEEKAAQDVMFERDYVVVERRHVEVNALADELAANEKLGQNNSSAKSSPLQRRYTQQGSATSTTGAIPTPASRTALVAQGRAGQDRRSSYEKALSASPGSASSAISKAIQDASLRLFGYKVNTMRQKGSSPPLYQPFPAYPTPTSAGLLSDGKGSQVSDEDAKAAQAIEEFATRSDCVYGFAEVKYKQLLPMAPSMDYGLGGVSPDKGTSEEDGLTVDATVALSEEALVLYVKSLTLLARAMDIASLWWSKKTRAESSVVSQTLVQRINAVVQWVRQRFNEVLEKSEVVRLKLTEAQKLLPEDHPSNPAHQGEDSIASSAVGAKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLPGCEISYLTAIRMLEAVLDSDDEATARNISSGKEIAKDATQEGSDLDTEEAAHVRKMITMITGRLNMVRKKQQMIAEANNQAKHVSAMRRLSGDVTPRSVPSYGST
2.7.11.1
null
autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709]
Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF12063;PF21127;PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104};
null
null
null
null
FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (PubMed:27197558). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Contributes to conidiation by regulating the conidial levels of the conidiation-related protein CP15 and mediates fungal oxidation resistance by controlling total superoxide dismutase (SOD) activity (PubMed:27197558). {ECO:0000250|UniProtKB:P53104, ECO:0000269|PubMed:27197558}.
Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae)
J5JV76
BSLS_BEAB2
MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDCFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDEHGRVFSLQPTTDLVESENGDCLSTPASERTVGIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTSTVVPFRVLCAPNQSVSEVMEAITTYDHDMRQFAHAGLCNISRIGDDASAACGFQTVLMVTDSRTASADEIHHVLEEPEKFIPCTDRALLLSCQMTDEGVLLVARYDQSILEPLQMARFLRQLGFLINKLQSTDGSPCVGQLDVLAPEDRTEIEGWNSEPLQTQDCLIHSEVVKNADDTPNKPAVCAWDGEWTYSELNNVSSRLASYISSLDLGQQLIVPIYLEKSKWVMAAILAVLKAGHAFTLIDPNDPPARTAQIIKQASASIALTSALHQSKMQTVVGRCITVDDDLFQTLTTFEGSQVASAAKPGDLAYVIFTSGSTGDPKGIMIEHRAFYSSVVKFGKALGIRSSTRALQFATHGFGAFLLEVLTTLIHGGCICIPSDHDRMHNIPGFIRQSQINWMMATPSYMTTMKPEDVPGLETLVLVGEQMSSSINDVWLSELQLLDGYGQSESSSICFVGKISDSSRDPNNLGRAIGSHSWIVNPDNPDQLVPIGAIGELLIESPGIARGYLFSQSTETPFLERAPAWYASKQPPYGVKFYRTGDLARYAPDGTVICLGRMDSQVKIRGQRVELDAIENLLRRQFPSDVTVVAEAVKRSDLPSSVVITGFLISSEYVVGAPSTEDTYILDQAVTQEINAKMRQILPAHSIPSFYICMKSLPRTATGKVDRRKLRSIGSSLLALQAQSTAPRSSQAPDASAGVTKLEEVWMDIFNLTPNSHNIGGNFFALGGDSITAIKMVNMARAAGIQLKVSDIFQNPTLASLQAAIGGSSMTVTSIPALALDGPVEQSYSQGRLWFLDQLEIGANWYTIPYAVRLRGPLDVDALNRALLALEKRHETLRTTFEDQDGVGVQIIHETLLDQLRIINADHADYVQLLKQEQTAPFNLASESGWRVSLIRLDDDDNILSIVMHHIISDGWSIDVLRRELGQLYAAALHGADLFGSALSPLPIQYRDFSVWQKQDAQVAEHERQLQYWQKQLADCSPAKLPTDFHRPALLSGKATTVPVTITSELYYRLQEFCSTFNTTSFVVLLATFRAAHYRLTGVDDAVIGTPIANRNRHELENLIGFFVNTQCMRITINEDEETFESLVRQVRSTTTAAFEHEDVPFERVVSAMLPGSRDLSQNPLAQLVFAIHSHKDLGKFELEALESEPLQNEVYTRFDAEFHFFQAPDGLTGYINFATELFKVETIQNVVSVFLQILRHGLEHPQTLISVVPLTDGLAELRSMGLLEIKKVEYPRDSSVVDVFATQVASYPDTLAVVDSSSRLTYAELDHQSDLLATWLRQQNLPTEALVVVLAPRSCETIITFLGILKANLAYLPLDIRSPITRMRDVLSTLPGRTIALLCSDEVAPDFQLPSIELVRIADALEEAAGMTSLNGHEHVPVPSPSPTSLAYVLYTSGSTGRPKGVMIEHRAIVRLARSDIIPDYRPACGDTMAHMFNTAFDGATYEIYTMLLNGGTLVCVDYMDTLSPKSLEAVFKKEQVNATIMAPALLKLYLADARDALKGLDVLISGGDRFDPQDAVDAQSLVRGSCYNGYGPTENGVFSTVYKVDKNDPFVNGVPLGRAVNNSGAYVVDRNQQLVGPGIIGELVVTGDGLARGYTERAFDQNRFIQLKIEGQSVRGYRTGDRVRYRVGEGLIEFFGRMDFQFKIRSNRIEAGEVEAAILSHPAVRNAAVILHVQEKLEPEIVGFVVAEHDDTAEQEEAGDQVEGWQAFFESTTYTELDTVSSSEIGKDFKGWTSMYDGNEIDKAEMQEWLDDTIHTLTDGQALGHVLEIGTGSGMVLFNLGSGLQSFVGLEPSKSAAAFVNNAIKSTPALAGKAHVFVGTATDTNKLDDLHPDLVIFNSVLQYFPTRDYLEQVVDALVHLRSAKRIFFGDVRSYATNRHFLAARAIYTLGNHTTKDEVRKKMAEMEEREEEFLVEPAFFTTLVNRLPDVRHVEIIPKNMQATNELSAYRYAAVVHLRGPDELTRPVHLIKMDDWVDFQASHMHKDALREYLRLAENTKTVAISNIPYGKTIFERQVVESLDDTSEDAPHASLDGAAWISAVRSDAKARSSLSVPDLVLLAKETGFRVEVSAARQWSQSGALDAVFHRYHPAEPDVRTLFQFPTDNDVRMSALLTNQPLQRLQKRRVAVQVREWLQDRIPSYMIPSHIVALDQMPLNTSGKVDRKELSRQAKAIKKVQKSAPPTAPAFPLSEVEVMLCEELTKTFEMDVNITDDFFQLGGHSLLATRLVARISHRLGARLTVKDVFDYPVFSELADIIRQQLASKNTLLPTASAGGGGQDKKESAGVAPTTDMEAMLCEEFANILGMDVGITDNFFDLGGHSLMATRLAARIGHRLNTTISVKDIFSHPVIFQLSAKLEVSQLESSSGGTDIKMPDYTAFQLIPAADAEKFMQDHIYPQINFSQDMVQDVYLATHLQQCFLRDVFGRPKPLVPFYVEFPPDSNPHTLATACTSLVDKYDIFRTIFVEAEGNLYQVVLKHLNLDIDVVETDANVHKTSSDLVDAIAKEPVRLGQPMIQVKVLKQTSSVRVLLWLSHALYDGLSWEHIVRDLHILSKERSLPPATQFSRYMQYVDHTRGPGCDFWRDVLQNAPITNLSDAGSGGRPTKAGDPRVWHAGKVISGPSQAIRSSITQATVFNAACAIVLSKETGTDNVVFGRIVSGRQGLPVRWQNIIGPCTNAVPVRAVVDAHGNHQQMLRDLQEQYLLSLPYETIGFDEIKRSCTDWPDSARNYGCCVTYQNFEYHPESEVDQQRVEMGILAKKAELIKEEPLYNVAIAGEVEPDGVHLQVTVVVDSQLFSQEGATHLMEQVCNTFQALNASL
2.1.1.-; 6.1.2.-
null
amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550]
cytosol [GO:0005829]
isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177]
PF00501;PF00668;PF00550;
3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150;
NRP synthetase family
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; KM=2.8 uM for L-leucyl-N-acetyl-cysteamine thioester(by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.41 uM/min/mg enzyme toward L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.05 uM/min/mg enzyme toward L-leucyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353};
null
null
null
FUNCTION: Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity (PubMed:19285149, PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). BSLS first catalyzes the iterative synthesis of an enzyme-bound dipeptidol monomer intermediate from D-2-hydroxyisovalerate and L-leucine before performing the condensation and cyclization of 4 dipeptidol monomers to yield the cyclic tetrameric ester bassianolide (PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). The N-methyltransferase MT domain is responsible for the methylation of the leucine residues of bassianolide (PubMed:29163920, PubMed:31388353). BSLS is flexible with both the amino acid and hydroxyl acid precursors, and produces bassianolide as the major product (containing N-methyl-L-Leu), together with small amounts of beauvericin and its analogs beauvericins A-C (containing N-methyl-L-Phe) (PubMed:31388353). {ECO:0000269|PubMed:19285149, ECO:0000269|PubMed:23608474, ECO:0000269|PubMed:23727842, ECO:0000269|PubMed:29163920, ECO:0000269|PubMed:31388353, ECO:0000269|PubMed:31471217}.
Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae)
J7FIX8
IDTG_CLAPA
MAPSPIMPRYHVGPMASTRRAISKKGFPRTRSFPVLTAPLDYLRDSPGKDIRSGLTDAFNEFLCVPEDKVVTIKRIIDLLHNASLLIDDIQDDSKLRRGVPVAHSIFGIAQTINSANLAYFLAQQELKKLSNPDAFAIYTDELINLHRGQGMELHWRESLHCPTEEEYMRMVQNKTGGLFRLAIRLLQGESRSDRDYVPLVDTLGTLFQIRDDYQNLQSDVYSKNKGFCEDISEGKFSYPVIHSIRARPGDLRLLNILKQRSEDLMVKQYAVSYINSTGSFEFCRGKIDCLAQWANLQLAALEEAEGAGRGDKLRAVLRLLDMKASGKQADVAS
2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]
null
dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]
PF00348;
1.10.600.10;
FPP/GGPP synthase family
null
null
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051};
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29457197}.
null
null
FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals (PubMed:23468653, PubMed:29457197, PubMed:32077051). The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline (PubMed:32077051). The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively (PubMed:32077051). The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable). {ECO:0000269|PubMed:23468653, ECO:0000269|PubMed:29457197, ECO:0000269|PubMed:32077051, ECO:0000305|PubMed:29457197}.
Claviceps paspali (Rye ergot fungus)
J7GQ11
TYRDC_LEVBR
MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEGIYFYLHVDAAYGGYARALFLDEDDQFIPYKNLQKVHAENHVFTEDKEYIKPEVYAAYKAFDQAESITIDPHKMGYVPYSAGGIVIQDIRMRDTISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHTLPLNVTGYGKLEGASIEGAHRYYDFLKNLKFEVAGKRISVHPLISPDFNMVDYVLKEDGNDDLIEMNRLNHAFYEQASYVKGSLYGKEYIVSHTDFAIPDYGDSPLAFVESLGFSEVEWRHAGKVTIIRASVMTPYMNQRENFDYFAPRIKKAIQADLEKVYASVNQKENV
4.1.1.25
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:24211777};
carboxylic acid metabolic process [GO:0019752]
null
L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837]
PF00282;PF21391;
3.40.640.10;
Group II decarboxylase family, Tyrosine decarboxylase subfamily
null
null
CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000305|PubMed:24211777, ECO:0000305|PubMed:27292129}; CATALYTIC ACTIVITY: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for L-tyrosine {ECO:0000269|PubMed:24211777}; KM=0.6 mM for L-tyrosine {ECO:0000269|PubMed:27292129}; KM=0.8 mM for L-dopa {ECO:0000269|PubMed:27292129}; Vmax=147.1 umol/min/mg enzyme for the decarboxylation of L-tyrosine {ECO:0000269|PubMed:24211777}; Note=kcat is 343.1 sec(-1) for the decarboxylation of L-tyrosine (PubMed:24211777). kcat is 124.8 sec(-1) for the decarboxylation of L-tyrosine. kcat is 76.5 sec(-1) for the decarboxylation of L-dopa (PubMed:27292129). {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129};
PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:24211777}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0 for the decarboxylation of L-tyrosine. Is not active at pH below 3.5 or above 9.0. More than 90% of activity remains over pH range from 5.0 to 6.0, and activity decreases rapidly at pH below 5.0 or higher than 6.0. {ECO:0000269|PubMed:24211777};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Only 8.5% of activity remains at 70 degrees Celsius. However, the enzyme shows poor stability at 50 degrees Celsius, the relative activity dropped to 14% after 1 h of incubation. {ECO:0000269|PubMed:24211777};
FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777). {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}.; FUNCTION: Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro. {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}.
Levilactobacillus brevis (Lactobacillus brevis)
J7H670
OXLA_LACMT
MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRITFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKKDIQTFCYPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL
1.4.3.2
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:22963728};
amino acid catabolic process [GO:0009063]
extracellular region [GO:0005576]
L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729]
PF01593;
3.90.660.10;3.50.50.60;1.10.405.10;
Flavin monoamine oxidase family, FIG1 subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22963728}.
CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:22963728};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for L-Leu {ECO:0000269|PubMed:22963728}; Vmax=0.063 umol/min/mg enzyme for L-Leu {ECO:0000269|PubMed:22963728};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for L-Leu. {ECO:0000269|PubMed:22963728};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4 degrees Celsius. {ECO:0000269|PubMed:22963728};
FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:22963728). Is highly active on L-Met=L-Leu>>L-Phe>L-Trp>L-Tyr>L-Ile, and weakly or not active on L-His, L-Arg, L-Val, L-Gln, L-Thr, L-Lys, and L-Ser (PubMed:22963728). Exhibits a low myotoxicity (a mild myonecrosis is observed after injection in mice quadriceps muscle) (PubMed:22963728). In vitro, is cytotoxic to a lot of human cell lines, including AGS (IC(50)=22.7 ug/ml), MCF-7 (IC(50)=1.4 ug/ml), HL-60, HeLa and Jurkat cells, as well as to the parasite Leishmania brasiliensis (IC(50)=2.22 ug/ml) (PubMed:22963728). This cytotoxicity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger (PubMed:22963728). {ECO:0000269|PubMed:22963728}.
Lachesis muta (South American bushmaster)
J7I4B7
WBDD_ECOLX
MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDMLAAGEEIDREKILGSLLRSLAALEKQGFWHDDVRPWNVMVDARQHARLIDFGSIVTTPQDCSWPTNLVQSFFVFVNELFAENKSWNGFWRSAPVHPFNLPQPWSNWLYAVWQEPVERWNFVLLLALFEKKAKLPSAEQQRGATEQWIIAQETVLLELQSRVRNESAGSEALRGQIHTLEQQMAQLQSAQDAFVEKAQQQVEVSHELTWLGENMEQLAALLQTAQAHAQADVQPELPPETAELLQRLEAANREIHHLSNENQQLRQEIEKIHRSRSWRMTKGYRYLGLQIHLLRQYGFVQRCKHFIKRVLRFVFSFMRKHPQVKHTAVNGLHKLGLYQPAYRLYRRMNPLPHSQYQADAQILSQTELQVMHPELLPPEVYEIYLKLTKNK
2.1.1.294; 2.7.1.181
null
methylation [GO:0032259]; O antigen biosynthetic process [GO:0009243]; phosphorylation [GO:0016310]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; methyltransferase activity [GO:0008168]; protein kinase activity [GO:0004672]
PF13847;PF00069;
1.10.510.10;3.40.50.150;
WbdD family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:19734145}; Peripheral membrane protein {ECO:0000269|PubMed:19734145}; Cytoplasmic side {ECO:0000269|PubMed:19734145}.
CATALYTIC ACTIVITY: Reaction=3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-adenosyl-L-methionine = 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36639, Rhea:RHEA-COMP:9559, Rhea:RHEA-COMP:9560, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74008, ChEBI:CHEBI:74009; EC=2.1.1.294; Evidence={ECO:0000269|PubMed:21990359}; CATALYTIC ACTIVITY: Reaction=alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + ATP = 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + ADP + H(+); Xref=Rhea:RHEA:40371, Rhea:RHEA-COMP:9558, Rhea:RHEA-COMP:9559, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74008, ChEBI:CHEBI:74010, ChEBI:CHEBI:456216; EC=2.7.1.181; Evidence={ECO:0000269|PubMed:21990359};
null
PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:15184370, ECO:0000269|PubMed:21990359}.
null
null
FUNCTION: Regulates the length of the LPS O-antigen polysaccharide chain (PubMed:15184370, PubMed:19734145, PubMed:21990359). Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar (PubMed:15184370, PubMed:21990359). This terminal modification is essential for export of the O-antigen across the inner membrane (PubMed:15184370). WbdD is also required for correct localization of the WbdA mannosyltransferase (PubMed:19734145, PubMed:25422321). {ECO:0000269|PubMed:15184370, ECO:0000269|PubMed:19734145, ECO:0000269|PubMed:21990359, ECO:0000269|PubMed:25422321}.
Escherichia coli
J7QLC0
CYAA_BORP1
MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPSGRSKFSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSVDVFVDRFVQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLDVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQTTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAAGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR
4.6.1.1
null
cAMP biosynthetic process [GO:0006171]; hemolysis in another organism [GO:0044179]
extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium ion sequestering activity [GO:0140314]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; calmodulin binding [GO:0005516]; channel activity [GO:0015267]; ion binding [GO:0043167]; toxin activity [GO:0090729]
PF03497;PF06594;PF00353;PF02382;
1.10.150.920;3.30.70.1720;3.90.1760.10;2.150.10.10;
Adenylyl cyclase class-2 family; RTX prokaryotic toxin family
PTM: Released in a processed form. {ECO:0000250|UniProtKB:P0DKX7}.; PTM: [Hemolysin]: Palmitoylated at Lys-860 and Lys-983 by CyaC (PubMed:11031260). The toxin only becomes active when modified in position Lys-983 (PubMed:11031260). Palmitoylation Lys-983 is required for efficient membrane insertion and pore formation of the acylated Hemolysin chain (By similarity). {ECO:0000250|UniProtKB:P0DKX7, ECO:0000269|PubMed:11031260}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2905265}.; SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane {ECO:0000305|PubMed:7525549}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: [Calmodulin-sensitive adenylate cyclase]: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000250|UniProtKB:P0DKX7};
null
null
null
null
FUNCTION: Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization (PubMed:2905265). It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function (PubMed:2905265). {ECO:0000269|PubMed:2905265}.; FUNCTION: [Calmodulin-sensitive adenylate cyclase]: Adenylate cyclase that is activated by host intracellular calmodulin and catalyzes un-regulated conversion of ATP to cAMP, thereby impairing microbicidal functions of immune effector cells and inducing apoptosis of lung macrophages. {ECO:0000269|PubMed:2905265, ECO:0000269|PubMed:8406793, ECO:0000269|PubMed:9529102}.; FUNCTION: [Hemolysin]: Hemolysin that forms small cation-selective membrane channels, leading to hemolytic activity (PubMed:7525549). The hemolytic activity of CyaA is weak compared with that of the HlyA of E.coli (PubMed:7525549). {ECO:0000269|PubMed:7525549}.
Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323)
J7RUA5
CAS9_STAAU
MKRNYILGLDIGITSVGYGIIDYETRDVIDAGVRLFKEANVENNEGRRSKRGARRLKRRRRHRIQRVKKLLFDYNLLTDHSELSGINPYEARVKGLSQKLSEEEFSAALLHLAKRRGVHNVNEVEEDTGNELSTKEQISRNSKALEEKYVAELQLERLKKDGEVRGSINRFKTSDYVKEAKQLLKVQKAYHQLDQSFIDTYIDLLETRRTYYEGPGEGSPFGWKDIKEWYEMLMGHCTYFPEELRSVKYAYNADLYNALNDLNNLVITRDENEKLEYYEKFQIIENVFKQKKKPTLKQIAKEILVNEEDIKGYRVTSTGKPEFTNLKVYHDIKDITARKEIIENAELLDQIAKILTIYQSSEDIQEELTNLNSELTQEEIEQISNLKGYTGTHNLSLKAINLILDELWHTNDNQIAIFNRLKLVPKKVDLSQQKEIPTTLVDDFILSPVVKRSFIQSIKVINAIIKKYGLPNDIIIELAREKNSKDAQKMINEMQKRNRQTNERIEEIIRTTGKENAKYLIEKIKLHDMQEGKCLYSLEAIPLEDLLNNPFNYEVDHIIPRSVSFDNSFNNKVLVKQEENSKKGNRTPFQYLSSSDSKISYETFKKHILNLAKGKGRISKTKKEYLLEERDINRFSVQKDFINRNLVDTRYATRGLMNLLRSYFRVNNLDVKVKSINGGFTSFLRRKWKFKKERNKGYKHHAEDALIIANADFIFKEWKKLDKAKKVMENQMFEEKQAESMPEIETEQEYKEIFITPHQIKHIKDFKDYKYSHRVDKKPNRELINDTLYSTRKDDKGNTLIVNNLNGLYDKDNDKLKKLINKSPEKLLMYHHDPQTYQKLKLIMEQYGDEKNPLYKYYEETGNYLTKYSKKDNGPVIKKIKYYGNKLNAHLDITDDYPNSRNKVVKLSLKPYRFDVYLDNGVYKFVTVKNLDVIKKENYYEVNSKCYEEAKKLKKISNQAEFIASFYNNDLIKINGELYRVIGVNNDLLNRIEVNMIDITYREYLENMNDKRPPRIIKTIASKTQSIKKYSTDILGNLYEVKSKKHPQIIKKG
3.1.-.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01480};
defense response to virus [GO:0051607]; maintenance of CRISPR repeat elements [GO:0043571]
null
DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
PF18070;PF21574;PF18061;PF13395;PF18541;
3.30.420.10;
CRISPR-associated Cas9 family, Subtype II-A subfamily
null
null
null
null
null
null
null
FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer; Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes the protospacer adjacent motif (PAM) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. {ECO:0000255|HAMAP-Rule:MF_01480, ECO:0000269|PubMed:25830891, ECO:0000269|PubMed:26098369}.
Staphylococcus aureus
J7SHB8
FLDH_CLOS1
MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPNVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLERLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFELKGTCKNQRVCK
1.1.1.110
null
L-phenylalanine catabolic process [GO:0006559]; tryptophan catabolic process [GO:0006569]; tyrosine catabolic process [GO:0006572]
null
4-phosphoerythronate dehydrogenase activity [GO:0033711]; D-lactate dehydrogenase activity [GO:0008720]; hydroxyphenylpyruvate reductase activity [GO:0047995]; indolelactate dehydrogenase (NADH) activity [GO:0047722]; NAD binding [GO:0051287]; phenyllactate dehydrogenase activity [GO:0097256]
PF00389;PF02826;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH; Xref=Rhea:RHEA:38351, ChEBI:CHEBI:11009, ChEBI:CHEBI:15378, ChEBI:CHEBI:18005, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.110; Evidence={ECO:0000269|PubMed:29168502, ECO:0000269|PubMed:4384683}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38353; Evidence={ECO:0000269|PubMed:29168502}; CATALYTIC ACTIVITY: Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780, ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.110; Evidence={ECO:0000269|PubMed:29168502, ECO:0000269|PubMed:4384683}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10782; Evidence={ECO:0000269|PubMed:29168502}; CATALYTIC ACTIVITY: Reaction=3-(indol-3-yl)lactate + NAD(+) = H(+) + indole-3-pyruvate + NADH; Xref=Rhea:RHEA:20133, ChEBI:CHEBI:15378, ChEBI:CHEBI:17282, ChEBI:CHEBI:17640, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.110; Evidence={ECO:0000269|PubMed:29168502, ECO:0000269|PubMed:4384683}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20135; Evidence={ECO:0000269|PubMed:29168502};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.075 mM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:4384683}; KM=0.106 mM for phenylpyruvate {ECO:0000269|PubMed:4384683}; KM=0.0142 mM for NADH (in the presence of indolepyruvate) {ECO:0000269|PubMed:4384683}; KM=1.03 mM for indolelactate {ECO:0000269|PubMed:4384683}; KM=1.77 mM for p-hydroxyphenyllactate {ECO:0000269|PubMed:4384683}; KM=2.21 mM for phenyllactate {ECO:0000269|PubMed:4384683}; KM=0.691 mM for indoleglycollate {ECO:0000269|PubMed:4384683}; KM=0.195 mM for NAD(+) (in the presence of indolelactate) {ECO:0000269|PubMed:4384683};
PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:29168502}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for indolepyruvate reduction. Optimum pH is 8.5 for indolelactate oxidation. {ECO:0000269|PubMed:4384683};
null
FUNCTION: Essential for the reductive metabolism of L-phenylalanine, L-tyrosine and L-tryptophan (PubMed:29168502). Catalyzes the conversion of phenylpyruvic acid to phenyllactic acid, 4-hydroxy-phenylpyruvic acid to 4-hydroxy-phenyllactic acid, and indolepyruvic acid to indolelactic acid (PubMed:29168502, PubMed:4384683). {ECO:0000269|PubMed:29168502, ECO:0000269|PubMed:4384683}.
Clostridium sporogenes (strain ATCC 15579)
J8G6Z1
THSA_BACCS
MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNIVSGFGLGVGSFVINGVLEELYMNQGTIDDDRLILRPFPQGKKGEEQWDKYRRDMITRTGVSIFLYGNKIDKGQVVKAKGVQSEFNISFEQNNYVVPVGATGYIAKDLWNKVNEEFETYYPGADARMKKLFGELNNEALSIEELINTIIEFVEILSN
3.2.2.5
null
defense response to virus [GO:0051607]
cytoplasm [GO:0005737]
hydrolase activity [GO:0016787]; nucleotide binding [GO:0000166]
PF13289;PF18185;
null
Soluble Thoeris ThsA family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:29371424}.
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5; Evidence={ECO:0000269|PubMed:32499527, ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:32499527, ECO:0000269|PubMed:36048923};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=269.8 uM for NAD(+) {ECO:0000269|PubMed:32499527}; Note=kcat is 33.9 min(-1) (PubMed:32499527). {ECO:0000269|PubMed:32499527};
null
null
null
FUNCTION: NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB. Activated by a signal molecule generated by endogenous ThsB (AC J8G8J6) or ThsB' (AC J8CSK2, probably 3'cADPR), by TIR1 and TIR2 from B.dafuensis or by BdTIR from B.distachyon (AC I1GTC2, probably 2'cADPR). Upon activation binds and hydrolyzes NAD(+), leading to cell death and inhibition of phage replication. Not seen to bind DNA (PubMed:32499527, PubMed:34853457, PubMed:36174646). Activation is 50-100x more sensitive to 3' cyclic ADP-D-ribose (3'cADPR) than 2'cADPR (PubMed:36174646). In another paper ThsA is not activated by any tested cADPR isomer, although it binds 3'cADPR; it was suggested the protein is already in a fully active state (PubMed:36048923). Expression of ThsA and ThsB in B.subtilis (strain BEST7003) confers resistance to phages phi29, SBSphiC, SBSphiJ and SPO1 (PubMed:29371424, PubMed:34853457). At multiplicity of infection (MOI) of 0.05 Thoeris-encoding cultures grow normally when infected with SPO1, at MOI 5 cultures collapse prematurely by 90 minutes post-infection, thus the phage are not able to complete a replication cycle. NAD(+) levels fall and ADP-D-ribose levels rise 60 minutes post-infection. Thoeris cultures eventually recover, but retain the same susceptibility to SPO1 (PubMed:34853457). {ECO:0000269|PubMed:29371424, ECO:0000269|PubMed:32499527, ECO:0000269|PubMed:34853457, ECO:0000269|PubMed:36048923}.
Bacillus cereus (strain MSX-D12)
J8H9C1
GAJA_BACC6
MKFSNITIKNFRNFEKVNINLDNKNVIFGMNDIGKTNFLYALRFLLDKEIRKFGFNKSDYHKHDTSKKIEIILTLDLSNYEKDEDTKKLISVVKGARTSANADVFYIALESKYDDKELYGNIILKWGSELDNLIDIPGRGNINALDNVFKVIYINPLVDLDKLFAQNKKYIFEESQGNESDEGILNNIKSLTDQVNQQIGEMTIIKGFQQEITSEYRSLKKEEVSIELKSEMAIKGFFSDIIPYIKKDGDSNYYPTSGDGRRKMLSYSIYNYLAKKKYEDKIVIYLIEEPEISLHRSMQIALSKQLFEQSTYKYFFLSTHSPELLYEMDNTRLIRVHSTEKVVCSSHMYNVEEAYGSVKKKLNKALSSALFAERVLLIEGPSEKILFEKVLDEVEPEYELNGGFLLEVGGTYFNHYVCTLNDLGITHIIKTDNDLKSKKGKKGVYELLGLNRCLNLLGRENLDEITIDIPEDIKGKKKKERLNERKKEIFKQYKNEVGEFLGERIYLSEIDLENDLYSAIGESMKRIFENEDPVHYLQKSKLFNMVELVNNLSTKDCFDVFEHEKFACLKELVGSDRG
3.1.-.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33885789}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:33885789}; Note=Rapid, sequence-specific cleavage at physiological concentrations of Mg(2+) (4-5 mM) or Mn(2+) (15 uM). In presence of >20 uM Mn(2+) has rapid non-specific cleavage activity. {ECO:0000269|PubMed:33885789};
defense response to virus [GO:0051607]
null
endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]
PF13175;PF20469;
3.40.50.300;
null
null
null
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:33885789};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-42 degrees Celsius. {ECO:0000269|PubMed:33885789};
FUNCTION: Component of antiviral defense system Gabija type I, composed of GajA and GajB (PubMed:29371424). Endonuclease that nicks double-stranded DNA within the sequence 5'-TNNNCGGGNNA-3' in the absence of nucleotides (NTP, dNTP and NDPs), cleaving after C-1 (PubMed:33885789, PubMed:37992757). Has no detected ATPase activity (PubMed:33885789). Expression of Gabija type I in B.subtilis (strain BEST7003) confers resistance to phages phi105, phi29, rho14, SpBeta and SBSphiC (PubMed:29371424). Expression of Gabija type I in E.coli B (strain ATCC 11303) confers resistance to phage T7 (PubMed:33885789). It is thought that this enzyme is strongly suppressed during physiological growth (in E.coli total nucleotide concentration is over 8.7 mM in mid-log phase), but during viral replication, when nucleotides are rapidly consumed, it is de-suppressed and degrades target DNA (Probable). {ECO:0000269|PubMed:29371424, ECO:0000269|PubMed:33885789, ECO:0000269|PubMed:37992757, ECO:0000305|PubMed:33885789}.
Bacillus cereus (strain VD045)
J9VE33
CRZ1_CRYNH
MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPSNPALEHLTGMAGISPIAPNADGPMICIQPSTPISGLKEGRGLFDAALRRAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLSSDQVNQGVEMQGMDFAAQMQSYEQQGWANDTLRIAGPSRPRAKSDSIIPSPTADSFDRQAFLAFIGAGNAQPPPPNVEMQPGYVDVSEQWRNTVSAWKAGLGEGELNSQPTLDPRLLPGRESNEAVYQQLLMQQQTGQMPRLDPDQLHQLTQLEGQRARFSLNTNIAPPKYEPGEISPTSMVFYQSMGLYPHAAPELSGTVSAPWSQTAFGQVPGPGPVGHPATAGPAQQHFLTPTLSHATVRRRSFGGGEHPAMGAGTPGYGMEFSSPFAGKSVGQIRGVNMGHRRAARSEDFGRGGTGWGVGAGGSTAEFLQSITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDMPDSIYPGHPIIAPATPLQVSGLYEEQQTPARVAKMKVTSVATEVASTSRRTNSGIFKCPVPGCGSTFTRHFNLKGHLRSHNDERPFKCLYEGCPKAIVGFARQHDCKRHMLLHEGLRLFECEGCGKKFARLDALTRHHKSEQGQECAITHPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED
null
null
calcineurin-mediated signaling [GO:0097720]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transepithelial migration of symbiont in host [GO:0140471]; regulation of fungal-type cell wall organization [GO:0060237]
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
null
PTM: Phosphorylated (PubMed:21487010, PubMed:27611567). Dephosphorylated by calcineurin (CNA1) which promotes nuclear localization (PubMed:27611567). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:27611567}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Nucleus {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Note=Localizes to the nucleus during calcium signaling, cell wall and heat stress (PubMed:21487010, PubMed:23251520, PubMed:24520056, PubMed:27611567, PubMed:28376087, PubMed:28898238, PubMed:31266771). Localizes to the nucleus following dephosphorylation by CNA1 (calcineurin) (PubMed:27611567). Localizes to the nucleus during growth on glucosamine carbon source (PubMed:28898238). Localizes to the cytosol during vegetative growth and osmotic stress (PubMed:23251520, PubMed:28376087, PubMed:28898238). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}.
null
null
null
null
null
FUNCTION: DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters (PubMed:28376087). Activates expression of genes required to maintain cell wall integrity during stress (PubMed:23251520, PubMed:28376087). Activates expression of genes required for transepithelial migration through the host blood-brain barrier (PubMed:29113016). Required for adaptation to host temperature during infection (PubMed:28376087). {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:28376087, ECO:0000303|PubMed:28376087, ECO:0000303|PubMed:29113016}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VHN6
X325_CRYNH
MFALKSILVTSLITSTALAHFTLDYPQSRGFVDDTENQFCGGFNTVEARQPFPLGSGPVHIDSHHALATIVAFISTSSNPTSFDDFNTTSNGTAIPLASSIFQVPQGEKCFNIDLQSLNVGLTNGSEVTLQIQYDGGDGNLYQCSDLVLIEGYEVPSNETCTNDASKASNATSTSSGSATATSAAATSSSSGTSGAIKEVVGFGALSLALGIAGLIIL
null
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:31932719}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:31932719};
null
plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metal ion binding [GO:0046872]
PF20238;
null
X325 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Proteins attached to a GPI anchor via their C terminus are found in the outer leaflet of the lipid bilayer facing the extracellular environment. GPI anchors can also be considered as predetermined breaking points, which allow the release of proteins into the extracellular environment upon enzymatic cleavage. {ECO:0000305|PubMed:31932718}.
null
null
null
null
null
FUNCTION: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (Probable). Cell surface-bound protein that functions in the copper-accumulation pathway shared by the CUF1-dependent copper transporter CTR1 (PubMed:31932719, PubMed:35737716). Involved in maintaining cell wall integrity during copper deficiency (PubMed:35737716). Binds Cu(2+) with an estimated 1:1 stoichiometry and might serve as an extracellular copper ligand (PubMed:31932719). FRE4 and FRE7 metalloreductases probably function together with CTR1 and BIM1 to liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (PubMed:31932719). Facilitates copper acquisition in the brain of mammalian hosts and acts as a copper-dependent virulence trait in fungal meningitis (PubMed:31932719). While BIM1 plays a critical role in cryptococcal meningitis, at least in part through its role in copper acquisition, it could play additional roles during copper limitation or as a means to invade and colonize host tissues in the brain, by compromising host carbohydrate integrity via its lytic polysaccharide monooxygenase (LPMO) activity, which has still to be determined (PubMed:31932719). {ECO:0000269|PubMed:31932719, ECO:0000269|PubMed:35737716, ECO:0000305|PubMed:31932718}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VI03
DMT5_CRYNH
MTTALTFGGGLFKDNTKFDIDMRGTADGAVNGGNIPNSQSQKRKRASPSPEIESEEDGDDWYEIDYIADSRVIRRKGRQILQYLIHWAGYAVHERTWEDEDGIGGEDCALVQEFYRKNPGKPRLSPSSVRKEVKLARMVEVVITTRRIDGKSRAASSTDQPSPHRLGITSPQANNIGGEDPNPSLTRRPVRSTVSEIAKRPTSKKVHPNKKCKASSDDESDFVFEEGEWDEDEDDDNDVDFRSSEDDEDDEQERSAEEPESDEEIIKPAKKTKSSLPKAKLRPKPANLGGFVTGVRPLNQGLDIKAAVRNMSDDLPPISDIEAMFDHLVSRIPDIVELVRQLNGRKLRVATMCSGTESPLLALNMIAKAIKAQHGLTLAFEHVFSCEIEPFKQAYIERNFTPPILFRDVTELGKKRAHTAYGSMVDVPGDVDILIAGTSCVDYSNLNNVQQDIDANGESGRTFRGMLQWVKKHQPPIVILENVCNAPWDKVVEYFGQIDYDAQYTRLDTKEFYIPHTRTRVYLFATPSSSESDDLPEKWAQTVKDLRRPWSSPFEAFLLHTDDPNIHRARLELASARAQTDGTSRKTTDWNRCESRHQRARQDEALGLLRPLTSWQEAGVCKGLDWTWNDWLLAQTERVVDLLEISTLRMAKDGIDSGFKACIWNVSQNVDRQTGSSKTALAPCLTPNMIPWVTIRGGPVTGREALALQGIPVRELLLTSENEDQLADLAGNAMTTTVVGSAMIAALKVACHKITEGANPEKEAALILEKEAVDDEQVANRIIGEDYLEHHDLDLAKVTKSNLSEILDLACRSSRHCQCEGQSGTAPNILECQECSYRACKSCGGRPEHVYAPCANQRVEPAEFEKRFKGLLPMRVRIAGLTDQCLNAVRKAAEKSNKGSVNDNDWQLWSTALLEGIHDAEFRFRYLKRQSTWTAVYEARRAMLSLVLRNQIPEWRLTIKAPASEPNNSQLRALLLHPVARLQIDIAGQDVLCGPWELCIPSMKTIDIEITGKGELLPSWQASLGLQGPFANTTRWSEVEISLQAEDENTLDRKLSGTYQLLPRCGQAMSSLHKKRPDLSDDGLPQLYFFLDPTRCGESREDRYVFSTSTERLDYGTERPVIARLDSHWREGNEKQRKVKLDVSGAWVKCPEAHLTAIGGDDIAVVANDAAANEIHRDRATFAIPSSASAISASLTTEGCSHAMALLSCRVPLDPTHSESMWRRGAWAEIDLSHQGNTTFANLAWITERLPPLDGLKNWAHIADDVSEHVCERCAPRPPKIHWIKREGKANKKGNKTKSTIIAFEDKLEAGQYEHALKHRPSPFVVQLRLDQDIGSFRIGLNIVSLAHRALSRLPPTTSEHKISLSWRLTPGHVTESPQPRRVFILPSNKQDPENSQPEAFKLPLRKEQLRSLWWMLEQEKATGKTHTFVEEEISESLLPAVGWRAEGKAERPVMVRGGVIADQVGYGKTVISIALVAQTLSLPAPEPATPGLIDLKATLIVVPGHLSKQWPNEIARFTGSMFKVIVIQGMKDLQEKTIAELGKADIIVMASEIFESDVYWSRLEYLSAQPREWLHDTQGGRFFCDRLDAAMESLVSQTKILKEKGSEAAMRAMEDKKKSLVDNVGSKKEVHTAVNFGKRMKGQAYRDKHDSDSKAKPITKEELERWEASEDEDDDENSKTYIPIPKFHSFTGSESIFSASVKKDYKLLPNPVLHMFRFRRVIADEFTYLQKKSLAAVLRLSSSYRWILSGTPPVSDFAAIRSIATFMGIHLGVEDDGEGDVQYQKARAKDQTQAEKFHAFREVHSRAWHNRRDELAQEFLNVFVRQNIAEIEDIPTVEHIHTFKLPASEGAVYLELEHHLQALEMQARKETKFKNVSQGDRNARLEEALSDSKTAEEALLKRCCHFTLDLSDKTQDAKSAQEACDHITSARARQLLACQEDLSRSVNQAIALHGWIKKKGGFSKNDDERQPFAEWIAFSSNISKHQGDIEAARILLKVIEKCGVKDGNIPPSPSDKQSPSIASGAKMDDVKWQLREQTHLLRKLVKELVARVRSLRFFEVVRKIQKGKSDAQIVLESSECGHKPSTNPDIEMAILSCCGHVACHKCMRKAAASQRCVKSGECQAAVRPTNIVKVSSLGVEGELSSGRYGAKLEHLVNLIHSIPKNERVLVFLQWEDLAGKVSEALSAGRIPHVTLSGSAKSRANTLDRFQSTNADSARVLLLKMNDASAAGSNLTTANHAVFLGPLFTNSLFNYRAVETQAIGRVRRYGQQKKVHIHRLLALDTIDMTIFNARRTELKEKTDWEEIPQEEYKGRGSSISMTNEKRTPTLTVKSNPFKRSSSWALASSFRSKKRSMEARDAEGVSDDDENSELSDII
3.6.4.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32437639};
DNA methylation-dependent heterochromatin formation [GO:0006346]; methylation [GO:0032259]; nucleotide-excision repair [GO:0006289]
chromosome [GO:0005694]; nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; ATP-dependent DNA (cytosine-5-)-methyltransferase activity [GO:0120328]; chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; sequence-specific DNA binding [GO:0043565]
PF00385;PF00145;PF00271;PF00176;
2.40.50.40;3.40.50.300;3.40.50.10810;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family; SNF2/RAD54 helicase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31955845}. Chromosome {ECO:0000269|PubMed:31955845}. Note=Localizes to heterochromatin characterized by trimethylation of histone H3 'Lys-9'. {ECO:0000269|PubMed:31955845}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + ATP + H2O + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + ADP + 2 H(+) + phosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68984, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31955845, ECO:0000269|PubMed:32437639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68985; Evidence={ECO:0000269|PubMed:31955845, ECO:0000269|PubMed:32437639};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 uM for ATP (in the presence of unmethylated DNA and at 23 degrees Celsius) {ECO:0000269|PubMed:32437639}; KM=6.2 uM for ATP (in the presence of hemimethylated DNA and at 23 degrees Celsius) {ECO:0000269|PubMed:32437639}; Note=kcat is 5.0 min(-1) for ATP (in the presence of unmethylated DNA and at 23 degrees Celsius) (PubMed:32437639). kcat is 11.1 min(-1) for ATP (in the presence of hemimethylated DNA and at 23 degrees Celsius) (PubMed:32437639). {ECO:0000269|PubMed:32437639};
null
null
null
FUNCTION: ATP-dependent cytosine methylase that maintains DNA methylation by acting at hemimethylated palindromic 5'-CG-3' sites to produce symmetrically methylated DNA strands (PubMed:24630728, PubMed:31955845, PubMed:32437639). DNA methylation may play a role in transcriptional silencing, particularly at transposable elements (PubMed:24630728). {ECO:0000269|PubMed:24630728, ECO:0000269|PubMed:31955845, ECO:0000269|PubMed:32437639, ECO:0000303|PubMed:24630728}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VJP1
PUR9_CRYNH
MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGADRMSSFGDFIALSHTVDTPTAKIISREVSDGVIAPGYEPEALEILSKKKGGKYCVLQMDPTYVPPEIETRQVYGISLQQKRNDCKIDESLFKNVVTANKDLPKSAVTDLVVATLALKYTQSNSVCYALNGTVIGLGAGQQSRIHCTRLAGDKADNWWLRHHPRVLELPFKKGTKRADKANAIDLFVTGQAFEAEGGERAQWESLFETVPEPLTKEEREKHMKELTGVACASDAFFPFPDNVHRAKRSGATYLAAPSGSIMDKECIKAADESNLVFCHTDLRLFHH
2.1.2.3; 3.5.4.10
null
'de novo' IMP biosynthetic process [GO:0006189]
cytosol [GO:0005829]
IMP cyclohydrolase activity [GO:0003937]; phosphoribosylaminoimidazolecarboxamide formyltransferase activity [GO:0004643]
PF01808;PF02142;
1.10.287.440;3.40.140.20;3.40.50.1380;
PurH family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}.
CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; Evidence={ECO:0000269|PubMed:36063996}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; Evidence={ECO:0000269|PubMed:36063996};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:36063996}; KM=30 uM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:36063996}; Note=kcat is 7.5 sec(-1) with AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:36063996). kcat is 7.7 sec(-1) for FAICAR cyclization activity (at pH 7.5 and 37 degrees Celsius) (PubMed:36063996). {ECO:0000269|PubMed:36063996};
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. {ECO:0000269|PubMed:36063996}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1. {ECO:0000269|PubMed:36063996}.
null
null
FUNCTION: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:36063996). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:36063996). Also catalyzes the cyclization of FAICAR to IMP (PubMed:36063996). {ECO:0000269|PubMed:36063996}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VLJ9
SODC_CRYNH
MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST
1.15.1.1
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445};
removal of superoxide radicals [GO:0019430]; symbiont defense to host-produced reactive oxygen species [GO:0052164]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]; plasma membrane raft [GO:0044853]
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
PF00080;
2.60.40.200;
Cu-Zn superoxide dismutase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33567338}. Mitochondrion {ECO:0000269|PubMed:33567338}. Cell membrane {ECO:0000269|PubMed:16524904}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to lipid rafts in the cell membrane. {ECO:0000269|PubMed:16524904}.
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:12496163, ECO:0000305|PubMed:16524904};
null
null
null
null
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (PubMed:12496163, PubMed:16524904). Destroys radicals produced by host defense mechanisms (PubMed:12496163). {ECO:0000269|PubMed:12496163, ECO:0000269|PubMed:16524904}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VND2
CDA2_CRYNH
MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLNHELTNYTMSVFMTMFPKIKSAFNYIVPICTAYNITQPYAESNITCPNFETYISGVTNISSSTTQKDGSSSTNTASGSGAAGSASATSSSDDSSSSGGSSGSSGSNNASSGALGMFDSLSGVGLILGGVVAGVMLL
3.5.1.41
COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3};
cell wall chitin catabolic process [GO:0006039]; cell wall organization [GO:0071555]; fungal-type cell wall biogenesis [GO:0009272]; polysaccharide catabolic process [GO:0000272]
extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872]
PF01522;
3.20.20.370;
Polysaccharide deacetylase family
PTM: The GPI anchor is required for the attachment to the cell membrane but not for cell surface targeting. {ECO:0000269|PubMed:22354955}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22354955}. Secreted, cell wall {ECO:0000269|PubMed:22354955}. Cell membrane {ECO:0000269|PubMed:22354955}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22354955}. Note=GPI-anchored cell membrane protein (GPI-PMP) (PubMed:22354955). Non-covalently associated to the cell wall independently of both its GPI-anchor and beta-1,6-glucan (PubMed:22354955). Cell membrane localization is critical for effective deacetylase activity (PubMed:22354955). {ECO:0000269|PubMed:22354955}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:22354955}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:22354955};
null
null
null
null
FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:17400891, PubMed:22354955). Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (PubMed:17400891). Chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms (PubMed:21784998, PubMed:27165801, PubMed:32071275). {ECO:0000269|PubMed:17400891, ECO:0000269|PubMed:21784998, ECO:0000269|PubMed:22354955, ECO:0000269|PubMed:27165801, ECO:0000269|PubMed:32071275}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VNT4
CHS5_CRYNH
MAQQPPPSRFLGVTDLSSLAVTEDTVLVTLQERYISHKPYTSLSPAALVFLSPYSHLPIDDEESLLHYVEEYYQCNNEEGGSRNEQGWWKKKMEQPHVFQLALSAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIGLQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKLMGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINVETLDIVAEFLGVHSESLAEIFSLKTVLVRKEVCTTFLGPEQAEQVRDELARTLYSLLFSWINEHINTKLCKDSFGSFIALVDLPGIQRNSGSMGSFNSVDQFCLNFAAEKMHNWVLHRVHETTRQEAETERLLISRVPYFDNSECLGMLSNPRGGLISVIDDLSQKKRSESNLLESLGKRFHNHPSMSISPQGNRSSASFTINHYDGPVTYSTSNFLERNANETSTDIIQLLRGDTTSRSQVSTTEGHGSSNPFIKGLFGMKNIAMQTHPRSDSTIVAAQQSVRPVRAPSTRRKKMMSLVPVSEEGGEETSDFQVGGGNDESYSSKELHCIAGQHWAAVDSLLKSFDQTQTWYIFALRPNDSQLPSQFDLRSMKQQVRSFGLVEMAQQLQTSWEVRLSHKEACERYNEELLYRGIPEGTGDVERLRDLKRLMSLNDADMGIGLQRVFLSHDLFRFLEDRLRAKEPGEQHAYEDLGHRKLQTDPFSPHRYQPTSFDSQDHVYKDPSIRPVDSSANLPLMEHAQPIVNSSLEIEDRESSAAPYVSYGGRSITDIEGYASSRDLLASSIHKSEKDPLDTEPQAGETTEVYRESIARRRWVWLCSILTWWIPGFLLSKIAGMKRQDIRQAWREKLAINMIIWFICGCAIFVIAILGPVICPTQHVYSTNELASHSYTLDPNNAFVAIRGEVFDLSQFAPTHLTAVSVVPTKSIMQYGGLDASELLPVQVSALCGGVSGSISQYVTLDSTNTTDVYSQYHDFRAFTNDSRPDWYAEMMIMMRHRFRVGFMGYTKKDLKKMAAQGKAVAIYDNLVYDMSNYIRQNGGGLKAPDGVNLTAQDQADRQFMSDQVVSLFKYNSGKDITTLLDNLGSTIGTDVVDRQKTCLRNLFILGKLDTRDSAQCQFSTYILLALSCVMVAVIGFKFLSALHFGSVRAPESHDKFVICQVPCYTEGEESLRRTIDSLCKLRYDDKRKLILVICDGNIKGFGNDKPTPAIVLDILGVDVNSDPEPLSFQSLGEGAKQHNMGKVYAGLYECAGHVVPYLVVAKVGKPNERQKPGNRGKRDSQMLVMHFLNKVHFSAPMNPLELEMYHQIKNVIGVNPSFYEYLFMVDADTTVDEMSLNRLVSAMRHDKKIIGVCGETSIANAKQSIVTMSQVYEYFISHHLSKAFESLFGSITCLPGCFSMYRLRSPDTNKPLFISHGIIQDYSENRVDTLHLKNLLHLGEDRYLTTLVLKHFQDYKTKFVRHAYAKTVAPDSIKVLLSQRRRWINSTVHNLAELVFLDQLCGFCCFSMRFVVFIDLLSTIIAPVTVAYIVYLIYLIVHDGSSIPTLSIIMLAAIYGLQAMIFIFRMRWDMIAWMIFYICAIPVFSFLLPLYSFWKMDDFSWGSTRLVVGDKGKKIVIHDEGKFDPSSIPLRSWEEYENELWDQESVHSGSYMPPKAEYSYDYPRTRSTYSHGGYAYGQPIHPMQTRSTSPVSSRYQMSQFRQSPYQSPYQGPYGGSTADFRSSRMDMAHRPSLDDTSSFHQPYQPAPRPQSSYAFNLPDPSSDSFTAPAVDYLGAQAITDSQLERSIRKICANAELDKLTKKGVRKELEREYGVELTERREAINRLVEKVLTE
2.4.1.16
null
cell wall organization [GO:0071555]; fungal-type cell wall chitin biosynthetic process [GO:0034221]
cell septum [GO:0030428]; myosin complex [GO:0016459]; plasma membrane [GO:0005886]
actin binding [GO:0003779]; ATP binding [GO:0005524]; chitin synthase activity [GO:0004100]; cytoskeletal motor activity [GO:0003774]
PF03142;PF00173;PF08766;PF00063;
1.10.10.820;1.20.58.530;3.10.120.10;1.10.10.60;3.40.850.10;1.20.120.720;
TRAFAC class CC myosin-kinesin ATPase superfamily, Myosin family; Chitin synthase family, Class V subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evidence={ECO:0000250|UniProtKB:P29465};
null
null
null
null
FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:16278457). Produces a large proportion of the chitin that is not deacetylated to chitosan (PubMed:16278457). {ECO:0000269|PubMed:16278457}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VP29
MRJ1_CRYNH
MLSFQATVRPLAVSSRLHSPAAHIWRRNAHTAAMSDDSLDQGSSSSYGDSASQPHLGKGKGRQDSLAQSYRFPEKGMNGGPPDPFEVMALDRSATQQEVKQQYYKLALLLHPDSSHPSSSPDHFATLNKAYNLLSKQSSRSAFLKTGYGWDVSTSSGGNQTWSDSLMRAEIARRRNGGAAAWNGASRRYRDSDAGRGAWGGFDGSQGWRPYEDPSKGFSPPTSGPAEERYMSNPRFLAVVGVASAVIAWVHWHRLGYAAETHRDMLDKQNIDASRALAQARYEAATHGHIRREQIRRRVREAEVLKELEKADQGHIAVAGPPTAYPPSHRE
null
null
chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; protein refolding [GO:0042026]
mitochondrion [GO:0005739]; respirasome [GO:0070469]
unfolded protein binding [GO:0051082]
PF00226;
1.10.287.110;
DnaJ family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:32518190}.
null
null
null
null
null
FUNCTION: Mitochondrial co-chaperone required for ubiquinol-cytochrome c oxidoreductase (mitochondrial respiratory chain complex III) activity. {ECO:0000269|PubMed:32518190}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VPD7
CDA1_CRYNH
MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAPKLDTGFITLEHDIYQQSVDLAVGYILPQVLANGTYQLKSIINCLGKDTSEAYIETSSNQTTTQITAATGSQSTFFQPIVGTATGAEVSAPSEATGSTAAGSAASTTSGSGASASTGAASNTSSSGSGRSATMGGALIALAAVAVGMVYVA
3.5.1.41
COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3};
cell wall chitin catabolic process [GO:0006039]; cell wall organization [GO:0071555]; evasion of host immune response [GO:0042783]; fungal-type cell wall biogenesis [GO:0009272]; polysaccharide catabolic process [GO:0000272]
extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872]
PF01522;
3.20.20.370;
Polysaccharide deacetylase family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:30459196}. Cell membrane {ECO:0000269|PubMed:30459196}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:30459196}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:30459196};
null
null
null
null
FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:17400891, PubMed:30459196). Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (PubMed:17400891). Plays a major role in synthesizing cell wall chitosan during host infection; chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms (PubMed:21784998, PubMed:27165801, PubMed:30459196, PubMed:32071275). {ECO:0000269|PubMed:17400891, ECO:0000269|PubMed:21784998, ECO:0000269|PubMed:27165801, ECO:0000269|PubMed:30459196, ECO:0000269|PubMed:32071275}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VWU3
ATM1_CRYNH
MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLNSAIKDTPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSNSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHRLWQAQLTESTQPTDEEIERQREELEVVDEKKKQ
7.-.-.-
null
intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:29089435, ECO:0000305|PubMed:29420779}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of mitochondrial Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (PubMed:29089435, PubMed:29420779). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Plays a role during copper stress, in a manner dependent on the copper metalloregulatory transcription factor CUF1 (PubMed:29089435). {ECO:0000250|UniProtKB:P40416, ECO:0000269|PubMed:29089435, ECO:0000269|PubMed:29420779}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VWW9
SODM_CRYNH
MITAITRTALPRATLRTSLATMSTIRAKHTLPPLPYAYDALEPSISAEIMNLHHTKHHQTYVNGLNAAEESLQKASADGDFKTAISLQPALKFNGGGHINHSLFWKNLAPTGSAQVKVPTSGVFYDQVQADFGGFENLKKEMNAKTAAIQGSGWGWLGYNKATKKLEIVTTPNQDPLLSHVPIIGIDIWEHAFYLQYKNVKPDYLNAIWNVINYEEAESRLKAAQ
1.15.1.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UQX0}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0};
removal of superoxide radicals [GO:0019430]; symbiont defense to host-produced reactive oxygen species [GO:0052164]
cytosol [GO:0005829]; mitochondrion [GO:0005739]
metal ion binding [GO:0046872]; superoxide dismutase activity [GO:0004784]
PF02777;PF00081;
1.10.287.990;3.55.40.20;
Iron/manganese superoxide dismutase family
null
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:33567338}. Note=Localizes to the mitochondrion both in copper-replete and copper-limiting conditions. {ECO:0000269|PubMed:33567338}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:33567338}.
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:33567338};
null
null
null
null
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:15643059, ECO:0000269|PubMed:16524904}.; FUNCTION: [Isoform 1]: Destroys mitochondrial radicals produced by oxidative stress. {ECO:0000269|PubMed:33567338}.; FUNCTION: [Isoform 2]: Destroys cytoplasmic radicals produced in low copper environments; a condition which inactivates the cytoplasmic copper-dependent superoxide dismutase SOD1. {ECO:0000269|PubMed:33567338}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VXM5
CHS3_CRYNH
MSRPHLQQNVSFQDTKPPSRRAGRDDIPPRPPTKSDPSKASLTTTTTVQSVGGYNNHQLDFDDNAYVDAGSSNPQGFSDYNGVRRKKSMVRPERERIDPNHRLWHYREHAAEDQVDIQPSSTGNQPYNQYNNQRPGANLRRGKSLLARETDDVDDSSGLNIFKRGATIRRKASRATPRQAPTGAQSNRVSAGQKEDEECCCLGNFAPGPKNCWMIYCYLLTICIPGFVIAKVFGKKTPDAQRAWREKIGIVSIVLYLMGAVGFITFGFTQTVCGDTQLRLPGGSANTGSLVINGYDYDFSTWRHPVAGDTFNGTTSPLYMDQYMAGGMDASFLFQNVNQNCLGLITPASGTGIDHDGDQMGWYFPCNLHDQNGTSAANLTGITDRTNCHVSSYARSNFSAVVPTAEIYYTWDRVKDESRNLAVYKSAVIDMNLLQWLDDTQVSYPEFFNTIKNRNDSYAGKDITALIERAGLSQYARCLTDVIQIGFVDTITIGCIMSELVLYVSLVFILGAVFIKFGMAVVFGWFLSWRMGNFKGESYQERMKRAAEIENWTDDIYRPAPGYLRPNATGTARTGVKKNFLPTTSRFSRAEPMLVSSSRPSTSYGMVGETRRQGSSIYGNKLGPPAHTTPPGSPLLRNSRSSTSLPFRDDSRHSISDRSVNNNVPCPFPLGNVVPQPAPDFEPFGYPLIHSICLVTAYSESIEGLRTTLDSLATTDYPNSHKLILVICDGMVRGSGSKQYTPEIVLGMMKELVTPAEEVEAHSYVAIADGHKRHNMAKVYAGFYAYDSETVEASKQQRVPMVLVSKVGNPLEVNDAKPGNRGKRDSQIVLMSFLQKVMFDERMTTLEYEFFNAVWRCTGIPPDRYETVLCVDADTKVFPDSLTRMNACMVNDHEIMGLCGETKIANKSETWVTMIQVFEYYISHHNTKAFESVFGGVTCLPGCFSMYRIKAPKGERGFWVPILANPDICEHYAENVVDTLHKKNLLLLGEDRYLSTLMLKTFPKRKMVFCPQAVCKTIVPDTFRVLLSQRRRWINSTVHNLCELILVRDLCGTFCFSMQFVVFMDLVGTLVLPAAISFTLYIIMISIIPQSVTGMPRPYVSLVLLAFILGLPGVLIVITSRKIAYVGWMLVYLISLPVWNLILPAYSYWHMDDFTWGETRKIAGEVKEEAHGGKEGTFDSSHIVMKKWAEFERERRWRTGTASRDSQYFDVVQRANSPRSGIPSNRYSIVSTSETFNSGLGTAESNHLFRQSQSFASMSQVAPSPETNYGNVPQLALPPPRGASIGREHSPSSTESGTSNNYAYGSTEEPTASNVDPYYQPFTNEVYQDEAEQPILPSEYTTTSPEPVYQTAPARVRQPSQRGVSLVDTGPVRSAQAAPHDAVRRVSRHQRRSSSKNQLVSPISSGGHTGSLPPGAAPPQY
2.4.1.16
null
cell wall organization [GO:0071555]; fungal-type cell wall chitin biosynthetic process [GO:0034221]; protein localization to bud neck [GO:0097271]
cell septum [GO:0030428]; cellular bud neck [GO:0005935]; chitosome [GO:0045009]; incipient cellular bud site [GO:0000131]; plasma membrane [GO:0005886]
chitin synthase activity [GO:0004100]
PF03142;
null
Chitin synthase family, Class IV subfamily
PTM: Palmitoylated by PFA4; required for proper subcellular localization. {ECO:0000269|PubMed:25970403}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25970403}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evidence={ECO:0000250|UniProtKB:P29465};
null
null
null
null
FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:16278457). Activated by CSR2, it produces chitin that is deacetyled to chitosan, which is required to maintain cell wall integrity (PubMed:16102007, PubMed:16278457, PubMed:17400891, PubMed:32743128). Conversion of chitin to chitosan offers an advantage during infection, as chitosan is less readily detected by host immunosurveillance mechanisms (PubMed:32071275). {ECO:0000269|PubMed:16102007, ECO:0000269|PubMed:16278457, ECO:0000269|PubMed:17400891, ECO:0000269|PubMed:32071275, ECO:0000269|PubMed:32743128}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9VYP5
PUR2_CRYNH
MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL
6.3.3.1; 6.3.4.13
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305};
'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084]
cytosol [GO:0005829]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641]
PF00586;PF02769;PF01071;PF02843;PF02844;
3.40.50.20;3.30.1490.20;3.30.470.20;3.90.600.10;3.90.650.10;3.30.1330.10;
GARS family; AIR synthase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20772}.
CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000250|UniProtKB:P20772}; CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000269|PubMed:34416230};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for ATP (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=496 uM for glycine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=131 uM for phosphoribosyl-amine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; Note=kcat is 27.3 sec(-1) for phosphoribosylamine--glycine ligase activity (at 37 degrees Celsius). {ECO:0000269|PubMed:34416230};
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305|PubMed:34416230}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. {ECO:0000305}.
null
null
FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities. {ECO:0000269|PubMed:34416230}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
J9W0G9
YPK1_CRYNH
MMSWKFGKKFKEGGFLSGKHHSSNNNSPSDTSRSTTPTPGNPHPEDAVKPPVPRSGMLKIRVTAAKGLSLPQGVSVPAPVQEALTTHPTLASRIATSPPTAIVKAAGANRDSLQRRQVWWLPYLVLEFDKNEVLVDALGGDLASPVWMYSATFDVSRISEISATVYLRTREPHAEGREKSNGEGEGEDMGNSDLCLGSIRFTPNLDSLRVTDDWVTVQGGGGSGSINVQVSFKPASGQILTIDSFELLKVIGKGSFGKVMQVRKRDTLRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVNCPFIVPLKFSFQSKEKLYLVLAFINGGELFHHLQREGKFNETRSRFYSAQLLLALEHLHSFNVIYRDLKPENILLDYAGNIALCDFGLCKLNMSNSDTTNTFCGTPEYLAPELLSGHGYTKCVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILTEPLRFPDGVRSEARSLLTGLLNRDPRQRLGVNGAQDIKNHPFFAKHINFTKLWNKQIQPPFKPAVASAIDTSNFDEEFTNEVPLDSVVDDSHLSQTVQQQFEGFSWSVSPLGESVGRY
2.7.11.1
null
phosphorylation [GO:0016310]; regulation of sphingolipid biosynthetic process [GO:0090153]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF00433;
1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, RAC subfamily
null
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P7J8}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P7J8};
null
null
null
null
FUNCTION: Probable serine/threonine-protein kinase which may act in the sphingolipid-mediated signaling pathway (PubMed:22339665). May act downstream of TORC2 (TOR complex 2) and PDK1 to regulate sphingolipid metabolism (PubMed:22339665). {ECO:0000269|PubMed:22339665}.
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
K0I210
FOMT4_OCIBA
MAVDKEVELHAQAWDHALSYITPTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSNDCYAQSPLSRVFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTPLYLKSIRGEDSWNDPAYGFHMRAFTNGMAAHARLTAAAIVTNYPTAFNGVRSVVDVGGRHGMAIGKLVEAFPWVRGIAFDLPEVVADAPPRKGVDFVGGDMFESLPKADAVMLMWVLHDWSDDKCIEILKKCKEAIPTSTGKVMIVDAIINEEGEGDEFSGARLSLDMTMMAMTTQGKERSYKEWVHLLNEAGFSKHTVKNIKTIEFVIEAYP
2.1.1.-
null
melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983]
PF08100;PF00891;
3.40.50.150;1.10.10.10;
Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=ladanein + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + salvigenin; Xref=Rhea:RHEA:73247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192702, ChEBI:CHEBI:192703; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73248; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 7-methyl ether = cirsimaritin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73243, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81337, ChEBI:CHEBI:192701; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73244; Evidence={ECO:0000305|PubMed:22923679};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=54 nM for ladanein (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=21 uM for S-adenosyl-L-methionine (in the presence of scutellarein) {ECO:0000269|PubMed:22923679}; Note=kcat is 130x10(-3) sec(-1) with scutellarein-7-methyl ether as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 140x10(-3) sec(-1) with ladanein as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). {ECO:0000269|PubMed:22923679};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Flavonoid 6-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin (SALV), aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 6-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and ladanein (LAD) (PubMed:22923679). {ECO:0000269|PubMed:22923679}.
Ocimum basilicum (Sweet basil)
K0I7Q2
FOMT3_OCIBA
MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTVKNIKSIESVIEAYP
2.1.1.-
null
melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983]
PF08100;PF00891;
3.40.50.150;1.10.10.10;
Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 7-methyl ether = H(+) + ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73239, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192701, ChEBI:CHEBI:192702; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73240; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=cirsimaritin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + salvigenin; Xref=Rhea:RHEA:73251, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81337, ChEBI:CHEBI:192703; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73252; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=cirsiliol + S-adenosyl-L-methionine = eupatorin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73259, ChEBI:CHEBI:3719, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136666; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73260; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=genkwanin + S-adenosyl-L-methionine = apigenin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73263, ChEBI:CHEBI:2769, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192700; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73264; Evidence={ECO:0000305|PubMed:22923679};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=410 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=42 nM for cirsimaritin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=130 nM for genkwanin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=36 uM for S-adenosyl-L-methionine (in the presence of cirsimaritin) {ECO:0000269|PubMed:22923679}; Note=kcat is 85x10(-3) sec(-1) with scutellarein-7-methyl ether as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 98x10(-3) sec(-1) with cirsimaritin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 57x10(-3) sec(-1) with genkwanin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). {ECO:0000269|PubMed:22923679};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and cirsimaritin (CIRM), and, with a lower efficiency, hispidulin, ladanein (LAD), cirsioliol (CIRL) and genkwanin (GENK) (PubMed:22923679). {ECO:0000269|PubMed:22923679}.
Ocimum basilicum (Sweet basil)
K0I977
FOMT1_OCIBA
MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAGFRKYVVNNIKALESLIEAYP
2.1.1.-; 2.1.1.232
null
melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983]
PF08100;PF00891;
3.40.50.150;1.10.10.10;
Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=(2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31539, ChEBI:CHEBI:15378, ChEBI:CHEBI:17846, ChEBI:CHEBI:28927, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.232; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31540; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein = S-adenosyl-L-homocysteine + scutellarein 7-methyl ether; Xref=Rhea:RHEA:73079, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78328, ChEBI:CHEBI:192701; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73080; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=apigenin + S-adenosyl-L-methionine = genkwanin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73071, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58470, ChEBI:CHEBI:59789, ChEBI:CHEBI:192700; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73072; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=luteolin + S-adenosyl-L-methionine = H(+) + luteolin 7-methyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73075, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192705; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73076; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=chrysoeriol + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + velutin; Xref=Rhea:RHEA:73083, ChEBI:CHEBI:57799, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:177047; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73084; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=diosmetin + S-adenosyl-L-methionine = luteolin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73103, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192749, ChEBI:CHEBI:192751; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73104; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=acacetin + S-adenosyl-L-methionine = apigenin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73107, ChEBI:CHEBI:2769, ChEBI:CHEBI:57284, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73108; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 4'-methyl ether = ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73111, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192702, ChEBI:CHEBI:192755; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73112; Evidence={ECO:0000305|PubMed:22923679};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 nM for apigenin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=240 nM for luteolin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=580 nM for scutellarein (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=2.5 uM for S-adenosyl-L-methionine (in the presence of apigenin) {ECO:0000269|PubMed:22923679}; Note=kcat is 91x10(-3) sec(-1) with apigenin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 100x10(-3) sec(-1) with luteolin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 47x10(-3) sec(-1) with scutellarein as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). {ECO:0000269|PubMed:22923679};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 7-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including apigenin (API) and luteolin (LUT), and, with a lower efficiency, scutellarein (SCU), naringenin (NAR), chrysoeriol (CHRYS), diosmetin (DIOS), acacetin (ACA) and scutellarein-7-methyl ether (SCU7Me) (PubMed:22923679). {ECO:0000269|PubMed:22923679}.
Ocimum basilicum (Sweet basil)
K0ICR0
FOMT5_OCIBA
MVADEEAQLHAQAWDHALSYIKPTALSAAVELEIPDILENHGGPMTLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTTENLGPYMLMQATPVTRCPTGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMTAHARLTAAAIVRNYPAAFDGVQSVVDVGSRHGTAIGKLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPANIGKVMIVDAIINEDGEGDEFSGTRLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTIKNIKAMEFVIEAYP
2.1.1.-
null
melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983]
PF08100;PF00891;
3.40.50.150;1.10.10.10;
Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=genkwanin + S-adenosyl-L-methionine = apigenin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73263, ChEBI:CHEBI:2769, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192700; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73264; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=cirsiliol + S-adenosyl-L-methionine = eupatorin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73259, ChEBI:CHEBI:3719, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136666; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73260; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=cirsimaritin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + salvigenin; Xref=Rhea:RHEA:73251, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81337, ChEBI:CHEBI:192703; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73252; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 7-methyl ether = H(+) + ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73239, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192701, ChEBI:CHEBI:192702; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73240; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=(2S)-sakuranetin + S-adenosyl-L-methionine = (2S)-naringenin 4',7-dimethyl ether + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73255, ChEBI:CHEBI:15378, ChEBI:CHEBI:28927, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192816; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73256; Evidence={ECO:0000305|PubMed:22923679};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=87 nM for cirsimaritin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=130 nM for genkwanin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=41 uM for S-adenosyl-L-methionine (in the presence of cirsimaritin) {ECO:0000269|PubMed:22923679}; Note=kcat is 66x10(-3) sec(-1) with scutellarein-7-methyl ether as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 50x10(-3) sec(-1) with cirsimaritin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 72x10(-3) sec(-1) with genkwanin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). {ECO:0000269|PubMed:22923679};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and, with a lower efficiency, cirsimaritin (CIRM), sakuranetin (NAR7Me), ladanein (LAD) and genkwanin (GENK) (PubMed:22923679). {ECO:0000269|PubMed:22923679}.
Ocimum basilicum (Sweet basil)
K0II72
FOMT2_OCIBA
MGRDEEAAARAEAWNHGFGFIKTSVIKTAIELEIPDILHNHGAPLSLSALSSAVGVPPDRLHRIMRFLTHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGAFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTKMVFRDAMACHARLTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPQVVAKAKPLHGVEFVAGSMFESVPEADVVMLMFVLHNWSDNECIDILKRCKEAIPRETGKVMIIDAIIEEDGEGDEFAEARLGLDVTMMAVTFEGKERTHREWAFILKEAGFRKYVVKNIKALESLIEAYP
2.1.1.-; 2.1.1.232
null
melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983]
PF08100;PF00891;
3.40.50.150;1.10.10.10;
Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 4'-methyl ether = ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73111, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192702, ChEBI:CHEBI:192755; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73112; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=acacetin + S-adenosyl-L-methionine = apigenin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73107, ChEBI:CHEBI:2769, ChEBI:CHEBI:57284, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73108; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=diosmetin + S-adenosyl-L-methionine = luteolin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73103, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192749, ChEBI:CHEBI:192751; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73104; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=chrysoeriol + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + velutin; Xref=Rhea:RHEA:73083, ChEBI:CHEBI:57799, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:177047; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73084; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=(2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31539, ChEBI:CHEBI:15378, ChEBI:CHEBI:17846, ChEBI:CHEBI:28927, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.232; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31540; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=apigenin + S-adenosyl-L-methionine = genkwanin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73071, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58470, ChEBI:CHEBI:59789, ChEBI:CHEBI:192700; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73072; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=luteolin + S-adenosyl-L-methionine = H(+) + luteolin 7-methyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73075, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192705; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73076; Evidence={ECO:0000305|PubMed:22923679}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein = S-adenosyl-L-homocysteine + scutellarein 7-methyl ether; Xref=Rhea:RHEA:73079, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78328, ChEBI:CHEBI:192701; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73080; Evidence={ECO:0000305|PubMed:22923679};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 nM for apigenin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=250 nM for luteolin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=250 nM for scutellarein (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=1.9 uM for S-adenosyl-L-methionine (in the presence of apigenin) {ECO:0000269|PubMed:22923679}; Note=kcat is 43x10(-3) sec(-1) with apigenin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 49x10(-3) sec(-1) with luteolin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 29x10(-3) sec(-1) with scutellarein as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). {ECO:0000269|PubMed:22923679};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
FUNCTION: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 7-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including apigenin (API) and luteolin (LUT), and, with a lower efficiency, scutellarein (SCU), naringenin (NAR), chrysoeriol (CHRYS), diosmetin (DIOS), acacetin (ACA) and scutellarein-7-methyl ether (SCU7Me) (PubMed:22923679). {ECO:0000269|PubMed:22923679}.
Ocimum basilicum (Sweet basil)
K0J4Q8
AHPC_AMPXN
MSLIGTEVQPFRAQAFQSGKDFFEVTEADLKGKWSIVVFYPADFSFVCPTELEDVQKEYAELKKLGVEVYSVSTDTHFVHKAWHENSPAVGSIEYIMIGDPSQTISRQFDVLNEETGLADRGTFIIDPDGVIQAIEINADGIGRDASTLINKVKAAQYVRENPGEVCPAKWEEGGETLKPSLDIVGKI
1.11.1.26
null
cell redox homeostasis [GO:0045454]; cellular response to stress [GO:0033554]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]
cytosol [GO:0005829]
NADH-dependent peroxiredoxin activity [GO:0102039]; thioredoxin peroxidase activity [GO:0008379]
PF10417;PF00578;
3.40.30.10;
Peroxiredoxin family, AhpC/Prx1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CATALYTIC ACTIVITY: Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+); Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.26; Evidence={ECO:0000269|PubMed:10960086};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.9 uM for H(2)O(2) {ECO:0000269|PubMed:10960086}; KM=10 uM for cumene hydroperoxide {ECO:0000269|PubMed:10960086};
null
null
null
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000269|PubMed:10960086}.
Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / Ep01)
K0P2S0
IF4E1_ARAHY
MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI
null
null
defense response to virus [GO:0051607]
cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]
RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]
PF01652;
3.30.760.10;
Eukaryotic initiation factor 4E family
PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28344571}. Cytoplasm {ECO:0000269|PubMed:28344571}.
null
null
null
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as peanut stripe virus (PStV) (PubMed:28344571). {ECO:0000250|UniProtKB:A0A075QQ08, ECO:0000269|PubMed:28344571}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:28344571}.
Arachis hypogaea (Peanut)
K1WG73
CFM6_MARBU
MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL
null
null
biological process involved in interaction with host [GO:0051701]
extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metal ion binding [GO:0046872]
PF05730;
null
RBT5 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}. Host chloroplast envelope {ECO:0000269|PubMed:36439212}.
null
null
null
null
null
FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}.
Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus)
K1XT82
CFM9_MARBU
MRVLKFLSLMAMLGCTIGQSGSATPGSLHLLGGPTTTDWYPECALRCWENTKYVTKCSEDQQCLCSDVNYQNSVFQCIYSQCDTVHFGSALHHAIAQCLGTDNEVFFAIPPIPDRDALRRREDEYAAGAKLFGSGSAAGYPTESAAFPVQSANYPTDSVGGPYSPSPTASVPFPYFSLTSVTSPAAKSATTTEATRNTVPASTTAPSPSPQLYTGNASTSRATVSLTVVLTVAAVYLVL
null
null
biological process involved in interaction with host [GO:0051701]
extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metal ion binding [GO:0046872]
PF05730;
null
RBT5 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}.
null
null
null
null
null
FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}.
Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus)
K1XVG1
CFM1_MARBU
MKFSAPVLAIFLASASAQSTAELAAQIPSCAQTCLATAITGAGCTAGDYACQCGTSQNTITASATPCVISACTSEEALNTQRTTSQICALVAAGSASSPSASSSASASASSSASSTSGAASASASASSSASSASAAASALTLAHPIPNPSHPPSPTIQTNLRKKVRNSNRLTPASLSSVSSALVSSASSVRASASSAVSAATTAANPAATTAAGVKEEASFFIPAAVALFAVFAV
null
null
biological process involved in interaction with host [GO:0051701]
extracellular space [GO:0005615]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metal ion binding [GO:0046872]
PF05730;
null
RBT5 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host cytoplasm {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}.
null
null
null
null
null
FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}.
Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus)
K1XW16
CFM8_MARBU
MQFSIVVMAALASLASAQSMDGIPTCALQCLAQAVVTGGCEASDQACQCGPAREAITAAATPCLLSACTDAADLATAASVGNGMCDKYKMGGDDAAPSPSVNTPAAAAPYPTAPAPNGTVPIGTAAAPSPTANTNETTTVATGSAPQNVAGGLAGIFGLVVAAAFAL
null
null
biological process involved in interaction with host [GO:0051701]
extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
metal ion binding [GO:0046872]
PF05730;
null
RBT5 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}.
null
null
null
null
null
FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}.
Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus)
K4BNG7
NAP2_SOLLC
MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ
null
null
abscisic acid homeostasis [GO:1902265]; abscisic acid-activated signaling pathway [GO:0009738]; leaf senescence [GO:0010150]; regulation of DNA-templated transcription [GO:0006355]; regulation of reproductive fruiting body development [GO:0031155]; response to abscisic acid [GO:0009737]; response to absence of light [GO:0009646]
nucleus [GO:0005634]
sequence-specific DNA binding [GO:0043565]
PF02365;
2.170.150.80;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
null
null
null
null
null
FUNCTION: Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing abscisic acid (ABA) homeostasis. Activates the expression of senescence and ABA associated genes including NCED1, ABCG40, CYP707A2, SAG113, SGR1 and PAO, by directly binding to their promoters. {ECO:0000269|PubMed:29760199}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
K4C9E2
NSY_SOLLC
METLLKPFPSLLLSSPTPYRSIVQQNPSFLSPTTKKKSRKCLLRNKSSKLFCSFLDLAPTSKPESLDVNISWVDPNSNRAQFDVIIIGAGPAGLRLAEQVSKYGIKVCCVDPSPLSMWPNNYGVWVDEFENLGLEDCLDHKWPMTCVHINDNKTKYLGRPYGRVSRKKLKLKLLNSCVENRVKFYKAKVWKVEHEEFESSIVCDDGKKIRGSLVVDASGFASDFIEYDRPRNHGYQIAHGVLVEVDNHPFDLDKMVLMDWRDSHLGNEPYLRVNNAKEPTFLYAMPFDRDLVFLEETSLVSRPVLSYMEVKRRMVARLRHLGIKVKSVIEEEKCVIPMGGPLPRIPQNVMAIGGNSGIVHPSTGYMVARSMALAPVLAEAIVEGLGSTRMIRGSQLYHRVWNGLWPLDRRCVRECYSFGMETLLKLDLKGTRRLFDAFFDLDPKYWQGFLSSRLSVKELGLLSLCLFGHGSNMTRLDIVTKCPLPLVRLIGNLAIESL
5.3.99.9; 5.5.1.19
null
carotene biosynthetic process [GO:0016120]; ubiquinone biosynthetic process [GO:0006744]; xanthophyll biosynthetic process [GO:0016123]
chloroplast [GO:0009507]; mitochondrion [GO:0005739]
lycopene beta cyclase activity [GO:0045436]; neoxanthin synthase activity [GO:0034020]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]
PF05834;
3.50.50.60;
Lycopene cyclase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:11029576}.
CATALYTIC ACTIVITY: Reaction=all-trans-violaxanthin = all-trans-neoxanthin; Xref=Rhea:RHEA:10128, ChEBI:CHEBI:32446, ChEBI:CHEBI:35288; EC=5.3.99.9; Evidence={ECO:0000269|PubMed:11029576}; CATALYTIC ACTIVITY: Reaction=a carotenoid psi-end group = a carotenoid beta-end derivative; Xref=Rhea:RHEA:55620, ChEBI:CHEBI:139114, ChEBI:CHEBI:139120; EC=5.5.1.19; Evidence={ECO:0000269|PubMed:10995464};
null
PATHWAY: Carotenoid biosynthesis; neoxanthin biosynthesis. {ECO:0000305}.; PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis. {ECO:0000305}.
null
null
FUNCTION: Involved in the synthesis of neoxanthin, the last product of carotenoid synthesis and a precursor of abscisic acid (PubMed:11029576). Involved in the beta-carotene biosynthesis (PubMed:10995464). {ECO:0000269|PubMed:10995464, ECO:0000269|PubMed:11029576}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
K4CI52
ABAH2_SOLLC
MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKVLNWQDTRQMPMTTRVIQETLRVASILSFTFREAVEDVEFEGYLIPKGWKVLPLFRNIHHSPDNFPEPEKFDPSRFEVSPKPNTFMPFGNGVHSCPGNDLAKLEILILVHHLTTKYRWSMVGPQNGIQYGPFALPQNGLPIKLSLKTSST
1.14.14.137
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};
abscisic acid catabolic process [GO:0046345]; abscisic acid metabolic process [GO:0009687]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; response to water deprivation [GO:0009414]; sterol metabolic process [GO:0016125]
membrane [GO:0016020]
(+)-abscisic acid 8'-hydroxylase activity [GO:0010295]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=2-cis-(+)-abscisate + O2 + reduced [NADPH--hemoprotein reductase] = (+)-8'-hydroxyabscisate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:12897, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:37569, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58490; EC=1.14.14.137; Evidence={ECO:0000250|UniProtKB:Q949P1};
null
PATHWAY: Plant hormone degradation; abscisic acid degradation. {ECO:0000269|PubMed:25039074}.
null
null
FUNCTION: Negative regulator of fruit ripening involved in the oxidative degradation of abscisic acid (ABA). {ECO:0000269|PubMed:25039074}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
K4CWS6
U75C1_SOLLC
MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQEEEKEEEKLSCMMELEKQGKIVPWCSQLEVLTHPSLGCFVSHCGWNSTLESLSSGVPVVAFPHWTDQGTNAKLIEDVWKTGVRMRVNEDGVVESDEIKRCIEIVMDGGEKGEEMRKNAQKWKELARAAVKEGGSSEVNLKAFVLQVSKSC
2.4.1.121; 2.4.1.263
null
abscisic acid-activated signaling pathway [GO:0009738]; fruit ripening [GO:0009835]; negative regulation of response to water deprivation [GO:0080148]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; response to abscisic acid [GO:0009737]; seed germination [GO:0009845]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
abscisic acid glucosyltransferase activity [GO:0010294]; indole-3-acetate beta-glucosyltransferase activity [GO:0047215]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28482127}. Nucleus {ECO:0000269|PubMed:28482127}.
CATALYTIC ACTIVITY: Reaction=2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-glucopyranosyl cis-(+)-abscisate + UDP; Xref=Rhea:RHEA:31031, ChEBI:CHEBI:22151, ChEBI:CHEBI:37569, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.263; Evidence={ECO:0000269|PubMed:28482127}; CATALYTIC ACTIVITY: Reaction=(indol-3-yl)acetate + UDP-alpha-D-glucose = 1-O-(indol-3-ylacetyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:14921, ChEBI:CHEBI:17990, ChEBI:CHEBI:30854, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.121; Evidence={ECO:0000269|PubMed:28482127};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.27 mM for abscisic acid {ECO:0000269|PubMed:28482127}; Vmax=0.026 umol/min/ug enzyme with abscisic acid as substrate (in the presence of UDP-glucose) {ECO:0000269|PubMed:28482127};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.67-8. {ECO:0000269|PubMed:28482127};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:28482127};
FUNCTION: Glucosyltransferase acting on both abscisic acid (ABA) and auxin (IAA). Required for ABA-mediated fruit ripening, seed germination, and negative responses to drought. {ECO:0000269|PubMed:28482127}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
K4L7X3
SPCAD_ADVMD
MYELTPEQRTLQTQARELAQSVFASTAVQTDLTEQYPWDNVAQLRDAGFMGMMLPTSVGGRGLSTLDTVIVIEEMAKACATMGRITVDSNLGAIGAITKYGSEEQIKLAADLVLAGDKPAICISEPNAGSAASEMTTRADKNGDHYILNGEKYWITGGGVSKLHLIFARVFDDGVEQGIGAFITVLDDHGPEGLKVGRRLYAMGVRGIPETHLEFHDLKIHKSMMITFPDGLKRGFAALMSAYNAQRVGAGAVALGIAQCAFEEGVAYLKRREQFGRPLAEFQGLQWMVADMSVQLEAARLMLRSAAVSGETFPDINKAAQAKIFAAETANKVTNDALQFFGSSGYGRHNPMERHVRDARMFTIAGGTAQILRTQVASKILDMKLPQTRDGYLKAAQNSKR
3.13.1.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:26057676};
leucine catabolic process [GO:0006552]
null
flavin adenine dinucleotide binding [GO:0050660]; hydrolase activity [GO:0016787]; isovaleryl-CoA dehydrogenase activity [GO:0008470]
PF00441;PF02770;PF02771;
1.10.540.10;2.40.110.10;1.20.140.10;
Acyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=3-sulfinopropanoyl-CoA + H2O = H(+) + propanoyl-CoA + sulfite; Xref=Rhea:RHEA:41624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:57392, ChEBI:CHEBI:78349; EC=3.13.1.4; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41625; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.013 mM for 3SP-CoA {ECO:0000269|PubMed:23354747}; Vmax=4.19 umol/min/mg enzyme {ECO:0000269|PubMed:23354747}; Note=kcat is 3.13 sec(-1). {ECO:0000269|PubMed:23354747};
null
null
null
FUNCTION: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite (PubMed:23354747, PubMed:26057676). Does not show dehydrogenase activity (PubMed:23354747). Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs) (PubMed:23354747). {ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}.
Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7)
K4LLQ2
VSP_BOTBA
APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP
3.4.21.-
null
regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
extracellular region [GO:0005576]; secretory granule [GO:0030141]
serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729]
PF00089;
2.40.10.10;
Peptidase S1 family, Snake venom subfamily
PTM: Glycoprotein, contains approx. 52% carbohydrate which could be removed by N-glycosidase. Glycosylation is important, since deglycosylated barnettobin loses its clotting and defibrinogenating effects. {ECO:0000269|PubMed:23578498}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23578498}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:23578498};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23578498};
FUNCTION: Thrombin-like snake venom serine protease that releases only fibrinopeptide A from human Aalpha chain of fibrinogen (specific coagulant activity was 251.7 NIH thrombin units/mg). Also shows fibrino(geno)lytic activities in vitro and defibrinogenating effects in vivo. {ECO:0000269|PubMed:23578498}.
Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti)
K4REZ6
ROSB_STRDJ
MALKALILNTTLRRSPSRSQTQGLIDKAVPLYEKEGIETEVVRVIDHDIEQEYWDDYDDWNAGEKARREDEWPWLLEKIREADILVIATPITLNMCTSAAHVILEKLNLMDELNGDTKQFPLYNKVAGLLMCGNEDGAHHVAGTVLNNLGRLGYSVPPNAAAYWLGPAGTGPGYIEGKGDRHFHTNKLIRFMVANTSHLARMLQETPYTTDLEACAQAAREESDDVFAIRVNVNTPAIRYKRFQKLGEVKVEESQLG
2.6.1.114
null
antibiotic biosynthetic process [GO:0017000]; antibiotic metabolic process [GO:0016999]
null
oxidoreductase activity [GO:0016491]; transaminase activity [GO:0008483]
PF03358;
3.40.50.360;
SsuE family
null
null
CATALYTIC ACTIVITY: Reaction=3 A + FMN + H2O + L-glutamate + O2 = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5'-phosphate + 3 AH2 + CO2 + H(+); Xref=Rhea:RHEA:54992, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499, ChEBI:CHEBI:29985, ChEBI:CHEBI:58210, ChEBI:CHEBI:139569; EC=2.6.1.114; Evidence={ECO:0000269|PubMed:27062037, ECO:0000269|PubMed:27981706, ECO:0000305|PubMed:27331868};
null
PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:27062037}.
null
null
FUNCTION: Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin) (PubMed:27062037). Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined oxidation, decarboxylation and transamination reaction (PubMed:27062037, PubMed:27331868, PubMed:27981706). The catalysis is initiated by an oxidation step in which the C-8 methyl group on the dimethylbenzene ring of FMN is converted to a formyl group to yield the 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) intermediate (PubMed:27062037). In the presence of thiamine, the formyl group is oxidized into a carboxyl group to yield the 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate (PubMed:27062037). Finally, in the presence of L-glutamate as an amino donor, decarboxylation and aminotransfer occur, resulting in production of 8-demethyl-8-aminoriboflavin-5'-phosphate (PubMed:27062037). Addition of NAD (but not NADP) to the reaction increases the yield 1.7-fold (PubMed:27062037). The reaction also proceeds without the addition of any electron acceptor, and it is possible that molecular oxygen serves this role (PubMed:27062037). {ECO:0000269|PubMed:27062037, ECO:0000269|PubMed:27331868, ECO:0000269|PubMed:27981706}.
Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
K4ZRC1
PPEP2_PAEA2
MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN
3.4.24.89
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:29794027}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:29794027};
proteolysis [GO:0006508]
extracellular region [GO:0005576]
metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]
PF07737;
3.40.390.10;
Peptidase M34 family, Pro-Pro endopeptidase subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29794027}.
CATALYTIC ACTIVITY: Reaction=The enzyme catalyzes the hydrolytic cleavage of peptide bonds between two proline residues.; EC=3.4.24.89; Evidence={ECO:0000269|PubMed:29794027};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for a FRET peptide containing PLPPVP {ECO:0000269|PubMed:29794027}; KM=330 uM for a FRET peptide containing VLPPVP {ECO:0000269|PubMed:29794027}; Note=kcat is 8 sec(-1) with a FRET peptide containing PLPPVP as substrate. kcat is 3 sec(-1) with a FRET peptide containing VLPPVP as substrate. {ECO:0000269|PubMed:29794027};
null
null
null
FUNCTION: Zinc-dependent endoprotease with a unique preference for proline residues surrounding the scissile bond, which cleaves in a PLP-|-PVP motif. Cleaves the cell surface protein encoded by an adjacent gene, which contains two PPEP-2 cleaving sites and putative extracellular matrix-binding domains. Thereby, may have a role in the regulation of P.alvei adhesion. Is not able to cleave within the PVP-|-PVQ motif, and only shows a very poor cleavage of the VNP-|-PVP motif in vitro, which is the optimal substrate peptide for PPEP-1 from P.difficile. {ECO:0000269|PubMed:29794027}.
Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352) (Bacillus alvei)
K5B7F3
MET1_MYCHD
MTDIRDTDALFALADRVTGFMPADEGRTLYETAVRYLGDGVGVEIGTYCGKSTVLLGAAARQTGGVVFTVDHHHGSEEHQPGWEYHDPSLVDPVTGLFDTLPRLRHTLDEADLYDHVVAVVGKSAVVARGWRTPLRFLFIDGGHTEEAAQRDFDGWARWVEVGGALVIHDVFPDPKDGGQAPFHIYQRALNTGDFREVNAYGSMRVLERTSGIAGQPL
2.1.1.365
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30606802};
chondroitin sulfate biosynthetic process [GO:0030206]; DIM/DIP cell wall layer assembly [GO:0071770]; methylation [GO:0032259]
plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]
PF13578;
3.40.50.150;
Methyltransferase superfamily
null
null
CATALYTIC ACTIVITY: Reaction=3,3'-di-O-methyl-4alpha-mannobiose + S-adenosyl-L-methionine = 1,3,3'-tri-O-methyl-4alpha-mannobiose + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62408, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:145745, ChEBI:CHEBI:145746; EC=2.1.1.365; Evidence={ECO:0000269|PubMed:30606802}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62409; Evidence={ECO:0000269|PubMed:30606802};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for 3,3'-di-O-methyl-4alpha-mannobiose {ECO:0000269|PubMed:30606802}; KM=0.055 mM for S-adenosyl-L-methionine {ECO:0000269|PubMed:30606802}; Vmax=75 nmol/min/mg enzyme toward 3,3'-di-O-methyl-4alpha-mannobiose {ECO:0000269|PubMed:30606802}; Vmax=85 nmol/min/mg enzyme toward S-adenosyl-L-methionine {ECO:0000269|PubMed:30606802}; Note=kcat is 0.037 min(-1). {ECO:0000269|PubMed:30606802};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30606802};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-55 degrees Celsius. {ECO:0000269|PubMed:30606802};
FUNCTION: Involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria (PubMed:30606802). Specifically methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobiose, a probable early precursor of MMP, yielding the reducing end dimannoside of MMP (PubMed:30606802). {ECO:0000269|PubMed:30606802}.
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
K5BDL0
GGH_MYCHD
MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTETAAQFAPLLCGGLPHDRERALLKLLEGPRFCGHPDLKYGLIPSTSPVSRDFRPREYWRGPVWPVLTWLFSWCFARRGWAERARLLRQEGLRQASDGSFAEYYEPFTGEPLGSMQQSWTAAAVLDWLG
3.2.1.208
null
oligosaccharide metabolic process [GO:0009311]; protein N-linked glycosylation [GO:0006487]
null
Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [GO:0004573]; glucosylglycerate hydrolase activity [GO:0102547]
null
1.50.10.10;
Glycosyl hydrolase 63 family
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510; EC=3.2.1.208; Evidence={ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=11.2 mM for glucosylglycerate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=13.7 umol/min/mg enzyme with glucosylglycerate as substrate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=15.2 umol/min/mg enzyme with glucosylglycerate as substrate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=12.3 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=3.6 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802}; Vmax=3.09 umol/min/mg enzyme with mannosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is 5.8 (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-55 degrees Celsius (tag-less variant) (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
FUNCTION: Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}.
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
K6UCV4
ADA_PLACD
MNILQEPIDFLKKDEIKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFLSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYKLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHRADFVGFDHGGHEVDLKQYKEIFDYVRESGIPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKVKNLYF
3.5.4.31; 3.5.4.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01};
adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166]
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]
2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872]
PF00962;
3.20.20.140;
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
null
null
CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:19728741};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=8.7 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 5.3 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741). {ECO:0000269|PubMed:19728741};
PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}.
null
null
FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable). {ECO:0000269|PubMed:19728741, ECO:0000305|PubMed:19728741}.
Plasmodium cynomolgi (strain B)
K7EJ46
SIM22_HUMAN
MAVSTEELEATVQEVLGRLKSHQFFQSTWDTVAFIVFLTFMGTVLLLLLLVVAHCCCCSSPGPRRESPRKERPKGVDNLALEP
null
null
lipid droplet formation [GO:0140042]; positive regulation of cell migration [GO:0030335]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]
late endosome [GO:0005770]; membrane [GO:0016020]
null
PF15831;
null
null
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Late endosome. Note=Partially colocalizedes with LAMP1 in late endosome. {ECO:0000269|PubMed:29765154}.
null
null
null
null
null
FUNCTION: May modulate lipid droplet formation throught interaction with SQLE. {ECO:0000269|PubMed:29765154}.
Homo sapiens (Human)
K7FQW8
SCNNB_PELSI
MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQQDYIPYLTSTAGARLMLHEQRSFPFLKDLGIYAMSGTETSIGVLVDELERMGFPYSDCTMNGSDVPVKNLYNEYNTTYSIQACLRSCFQAQMFETCGCGHYLFPLPEGVSYCNSEDDPDWAYCYSSLRSSIGHRQFCIDSCKETCNDIQYKMTISMADWPSEASEEFQYMQHPLTYERDQSRNATLDRNGIIKLNIYFQEYNYRTISESAATTIVWLLSSLGGQFGFWMGGSVLCLIEFGEIIIDFLWITVIKISNWGKGLKQKRARAQYPDAPPTVSELVEAHINL
null
null
aldosterone metabolic process [GO:0032341]; artery smooth muscle contraction [GO:0014824]; cellular response to acidic pH [GO:0071468]; cellular response to aldosterone [GO:1904045]; epithelial fluid transport [GO:0042045]; erythrocyte homeostasis [GO:0034101]; gene expression [GO:0010467]; intracellular sodium ion homeostasis [GO:0006883]; leukocyte activation involved in inflammatory response [GO:0002269]; mucus secretion [GO:0070254]; multicellular organism growth [GO:0035264]; multicellular organismal-level water homeostasis [GO:0050891]; neutrophil activation involved in immune response [GO:0002283]; neutrophil-mediated killing of bacterium [GO:0070944]; potassium ion homeostasis [GO:0055075]; renal system process [GO:0003014]; response to food [GO:0032094]; response to xenobiotic stimulus [GO:0009410]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725]
apical plasma membrane [GO:0016324]; cytoplasmic vesicle membrane [GO:0030659]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; sodium channel complex [GO:0034706]
ligand-gated sodium channel activity [GO:0015280]; WW domain binding [GO:0050699]
PF00858;
2.60.470.10;1.10.287.770;
Amiloride-sensitive sodium channel (TC 1.A.6) family, SCNN1B subfamily
null
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial cells. {ECO:0000250|UniProtKB:P37090}.
null
null
null
null
null
FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. {ECO:0000250|UniProtKB:P51168}.
Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
K7MTW9
TAP1_SOYBN
MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH
2.3.1.48
null
defense response [GO:0006952]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
histone H2A acetyltransferase activity [GO:0043998]; histone H3 acetyltransferase activity [GO:0010484]; N-acetyltransferase activity [GO:0008080]
PF00583;
3.40.630.30;
Acetyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30346270}. Nucleus {ECO:0000269|PubMed:30346270}. Note=Localizes to the cytoplasm, but is relocated to the nucleus when interacting with the effector Avh52 from the pathogen Phytophtora sojae. {ECO:0000269|PubMed:30346270}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:30346270};
null
null
null
null
FUNCTION: Acetylates histones H2A and H3 in vitro. {ECO:0000269|PubMed:30346270}.; FUNCTION: (Microbial infection) Acts as a negative regulator of immunity when hijacked and relocated to the nucleus by the effector Avh52 from the pathogen Phytophtora sojae (PubMed:30346270). Acts as a susceptibility factor that is hijacked by Avh52 in order to promote acetylation of histones H2A and H3 during early infection by Phytophtora sojae (PubMed:30346270). These epigenetic modifications may up-regulate the expression of potential plant susceptibility genes, thereby promoting susceptibility to Phytophtora sojae (PubMed:30346270). {ECO:0000269|PubMed:30346270}.
Glycine max (Soybean) (Glycine hispida)
K7N5M8
DYP2_AMYS7
MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHAHIRKTNPRGSGGAEAPEEERKHLMARRGQTYGRRHDDPNADLPPRLRPAKDVGLLFMAFNSNLGNQFEFTQQIWANNPAFPFPPDGSQPGLDPVIGQGARAPQKYAPEWGHNNVAEATDPIPQAVTMKGGEYFFMPSLAFLRSL
1.11.1.16; 1.11.1.19; 1.11.1.7
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:23054399}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:23054399}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23054399};
null
cytosol [GO:0005829]; extracellular region [GO:0005576]
heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; manganese ion binding [GO:0030145]; manganese peroxidase activity [GO:0016689]; peroxidase activity [GO:0004601]; reactive-black-5:hydrogen-peroxide oxidoreductase activity [GO:0052750]
PF21105;
null
DyP-type peroxidase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23054399}. Note=Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 could be secreted and still possibly play a role in extracellular oxidation chemistry (PubMed:23054399).
CATALYTIC ACTIVITY: Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin; Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591, ChEBI:CHEBI:53650; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:23054399}; CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+); Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:23054399}; CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:23054399}; CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23054399};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for ABTS {ECO:0000269|PubMed:23054399}; KM=48 uM for Reactive Blue 5 {ECO:0000269|PubMed:23054399}; KM=2.4 uM for Reactive Black 5 {ECO:0000269|PubMed:23054399}; KM=1.2 mM for 2,4-dichlorophenol {ECO:0000269|PubMed:23054399}; KM=210 uM for Mn(2+) (when assaying manganese peroxidase activity) {ECO:0000269|PubMed:23054399}; KM=760 uM for Mn(2+) (when assaying 4-methoxymandelate oxidase activity) {ECO:0000269|PubMed:23054399}; Note=kcat is 87 sec(-1) for peroxidase activity with ABTS as substrate. kcat is 34 sec(-1) for peroxidase activity with Reactive Blue 5 as substrate. kcat is 0.38 sec(-1) for peroxidase activity with Reactive Black 5 as substrate. kcat is 68 sec(-1) for peroxidase activity with 2,4-dichlorophenol as substrate. kcat is 24 sec(-1) for manganese peroxidase activity.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for the H(2)O(2)-dependent oxidation of Reactive Blue 5, and 5.0 for the O(2)-dependent oxidation of 4-methoxymandelate. {ECO:0000269|PubMed:23054399};
null
FUNCTION: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde. {ECO:0000269|PubMed:23054399}.
Amycolatopsis sp. (strain ATCC 39116 / 75iv2)
K7N6K2
TR34B_MOUSE
MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILGSKCFSSGKHYWEVDVSEKNAWTLGVYTRKRTLRFDVRQRKGQPNGYHRYKPQNGYWVIGLQHGSKYSIFEDSSNCDPTVLNPFVATPLHRVGIFLDCEEGTVSFLNVTNHGSLIYKFSQCCFSQPAYPYFNPWDCPAPMTLCPLNS
2.3.2.27
null
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF00622;PF00643;PF13445;
2.60.120.920;3.30.160.60;3.30.40.10;
TRIM/RBCC family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYJ4}. Mitochondrion {ECO:0000250|UniProtKB:Q9BYJ4}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9BYJ4};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9BYJ4}.
null
null
FUNCTION: Functions as antiviral protein and contributes to the defense against retroviral infections (By similarity). Acts as a capsid-specific restriction factor with the help of TRIM5 and prevents infection from non-host-adapted retroviruses. During influenza A virus infection, promotes programmed cell death by targeting ZBP1 for 'Lys-63'-linked polyubiquitination. In turn, promotes ZBP1 recruitment of RIPK3 to mediate virus-induced programmed necrosis (By similarity). Negatively regulates the function of mitochondria by enhancing mitochondrial depolarization leading to cytochrome c release and mitochondria-dependent apoptosis. Promotes also the formation of multinucleated giant cells by means of cell fusion and phagocytosis in epithelial cells (By similarity). Regulates intestinal inflammation by controlling the exocytosis of the major component of colonic mucus MUC2 from colonic goblet cells (PubMed:32094504). {ECO:0000250|UniProtKB:Q9BYJ4, ECO:0000269|PubMed:32094504}.
Mus musculus (Mouse)
K7NBW3
74AC1_SIRGR
MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVESVAEKGLVVSWCSQLEVLAHPSVGCFFTHCGWNSTLEALCLGVPVVAFPQWADQVTNAKFLEDVWKVGKRVKRNEQRLASKEEVRSCIWEVMEGERASEFKSNSMEWKKWAKEAVDEGGSSDKNIEEFVAMLKQT
2.4.1.350
null
null
null
quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; UDP-glucosyltransferase activity [GO:0035251]
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP; Xref=Rhea:RHEA:52044, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:138974, ChEBI:CHEBI:138975; EC=2.4.1.350; Evidence={ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52045; Evidence={ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41.4 uM for mogrol {ECO:0000269|PubMed:25759326}; KM=49.4 uM for mogrol {ECO:0000269|Ref.3}; KM=890.2 uM for UDP-alpha-D-glucose {ECO:0000269|Ref.3}; KM=58.2 uM for quercetin {ECO:0000269|PubMed:25759326}; KM=54.7 uM for naringenin {ECO:0000269|PubMed:25759326};
null
null
null
FUNCTION: Catalyzes the transfer of a glucose moiety to the C-3 hydroxyl of mogrol to form mogroside IE (PubMed:25759326, Ref.3). Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin and naringenin as substrate (PubMed:25759326). {ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3}.
Siraitia grosvenorii (Monk's fruit) (Luo han guo)
K7QHS5
BCAT2_HUMLU
MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRKSIIDVARTLGFQVEERLVHVDELLDADEVFCTGTAVVVSPVGSITYHGERVPYNEGGVGAVSQQLYSALTRLQMGFIKDNMNWTVELS
2.6.1.42
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|RuleBase:RU004516};
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099]
chloroplast [GO:0009507]
L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]
PF01063;
3.30.470.10;3.20.10.10;
Class-IV pyridoxal-phosphate-dependent aminotransferase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23347725}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=690 uM for glutamate {ECO:0000269|PubMed:23347725}; KM=120 uM for ketoisocarpoate {ECO:0000269|PubMed:23347725}; KM=160 uM for ketoisomethylvalerate {ECO:0000269|PubMed:23347725}; KM=200 uM for ketoisovalerate {ECO:0000269|PubMed:23347725}; KM=210 uM for 2-oxoglutarate {ECO:0000269|PubMed:23347725}; KM=280 uM for leucine {ECO:0000269|PubMed:23347725}; KM=250 uM for isoleucine {ECO:0000269|PubMed:23347725}; KM=130 uM for valine {ECO:0000269|PubMed:23347725}; Vmax=135.9 umol/min/mg enzyme with glutamate as substrate {ECO:0000269|PubMed:23347725}; Vmax=119.2 umol/min/mg enzyme with ketoisocarpoate as substrate {ECO:0000269|PubMed:23347725}; Vmax=84.68 umol/min/mg enzyme with ketoisomethylvalerate as substrate {ECO:0000269|PubMed:23347725}; Vmax=96.38 umol/min/mg enzyme with ketoisovalerate as substrate {ECO:0000269|PubMed:23347725}; Vmax=36.92 umol/min/mg enzyme with 2-oxoglutarate as substrate {ECO:0000269|PubMed:23347725}; Vmax=43.43 umol/min/mg enzyme with leucine as substrate {ECO:0000269|PubMed:23347725}; Vmax=88.08 umol/min/mg enzyme with isoleucine as substrate {ECO:0000269|PubMed:23347725}; Vmax=23.29 umol/min/mg enzyme with valine as substrate {ECO:0000269|PubMed:23347725};
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. {ECO:0000305}.
null
null
FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA biosynthesis. {ECO:0000269|PubMed:23347725}.
Humulus lupulus (European hop)
K7QKH1
BCAT1_HUMLU
MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID
2.6.1.42
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|RuleBase:RU004516};
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099]
mitochondrion [GO:0005739]
L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]
PF01063;
3.30.470.10;3.20.10.10;
Class-IV pyridoxal-phosphate-dependent aminotransferase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23347725}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=720 uM for glutamate {ECO:0000269|PubMed:23347725}; KM=35 uM for ketoisocarpoate {ECO:0000269|PubMed:23347725}; KM=99 uM for ketoisomethylvalerate {ECO:0000269|PubMed:23347725}; KM=99 uM for ketoisovalerate {ECO:0000269|PubMed:23347725}; KM=30 uM for 2-oxoglutarate {ECO:0000269|PubMed:23347725}; KM=40 uM for leucine {ECO:0000269|PubMed:23347725}; KM=230 uM for isoleucine {ECO:0000269|PubMed:23347725}; KM=340 uM for valine {ECO:0000269|PubMed:23347725}; Vmax=5.59 umol/min/mg enzyme with glutamate as substrate {ECO:0000269|PubMed:23347725}; Vmax=4.5 umol/min/mg enzyme with ketoisocarpoate as substrate {ECO:0000269|PubMed:23347725}; Vmax=2.95 umol/min/mg enzyme with ketoisomethylvalerate as substrate {ECO:0000269|PubMed:23347725}; Vmax=4.23 umol/min/mg enzyme with ketoisovalerate as substrate {ECO:0000269|PubMed:23347725}; Vmax=4.5 umol/min/mg enzyme with 2-oxoglutarate as substrate {ECO:0000269|PubMed:23347725}; Vmax=4.84 umol/min/mg enzyme with leucine as substrate {ECO:0000269|PubMed:23347725}; Vmax=19.4 umol/min/mg enzyme with isoleucine as substrate {ECO:0000269|PubMed:23347725}; Vmax=12.6 umol/min/mg enzyme with valine as substrate {ECO:0000269|PubMed:23347725};
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. {ECO:0000305}.
null
null
FUNCTION: Converts 2-oxo acids to branched-chain amino acids (BCAA). Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA catabolism. {ECO:0000269|PubMed:23347725}.
Humulus lupulus (European hop)
K7QRJ5
PYRE3_STRRG
MSDTVIIAGGGPVGLMLACELGLAGVDTVVLERHDAPREPSRGGAINATVVELFTQRGIMESLRDDGFEFRMAHFAHIPLAPERVPGDRAFSFAVPHAQVERRLEERARSLGVRVRRSTEITSVRQTPDGVQVTTGDGEVVEGAYLVGCDGSASLVREQAGIPFPGVDPDFHGLWGDIKVEPGAPVLERIGARQYELGLCMVAPIGPDTVRVITGEFDVPSPPADQEVGFDELRAAVARIAGVELDGVPGWLSRWTATSRQAERYREGRILLAGDAAHTLFPLGGQALGTGIEDAVNLGWKLAATVQGWAPPSLLDSYHEERHAAGARACASTRAQTTIMRSLARVGELRALLTELAGLEEVNAYLVRMVGGIDGSRLPDVPLVTAEGETSVYRLLEAGRGVLLDLGAGLPAVRHPQVTYVRAEPTNRLDATAVLLRPDGVVAWRAPQDGLEAALETWFGPAA
5.5.1.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:29657086}; Note=Binds 1 FAD per subunit. The FAD cofactor does not cycle between oxidized and reduced forms and therefore does not have a typical redox role in the reaction; it plays a structural role essential for PyrE3 catalysis, to maintain the requisite geometry of the protein and position the 1,3-diene and dienophile groups through specific interactions with the substrate. {ECO:0000269|PubMed:29657086};
antibiotic biosynthetic process [GO:0017000]; ubiquinone biosynthetic process [GO:0006744]
null
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase activity [GO:0043719]; FAD binding [GO:0071949]; isomerase activity [GO:0016853]
PF01494;PF21274;
3.40.30.120;3.50.50.60;
PheA/TfdB FAD monooxygenase family
null
null
CATALYTIC ACTIVITY: Reaction=4-[(2E,7S,8E,10E,13R,14R,16E,18E)-14-ethyl-7,13-dihydroxy-2,16,18-trimethylicosa-2,8,10,16,18-pentaenoyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate = 4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate; Xref=Rhea:RHEA:64476, ChEBI:CHEBI:155854, ChEBI:CHEBI:155855; Evidence={ECO:0000269|PubMed:25730548}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64477; Evidence={ECO:0000269|PubMed:25730548};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=51.5 uM for 4-[(2E,7S,8E,10E,13R,14R,16E,18E)-14-ethyl-7,13-dihydroxy-2,16,18-trimethylicosa-2,8,10,16,18-pentaenoyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate {ECO:0000269|PubMed:25730548}; Note=kcat is 223.2 min(-1). {ECO:0000269|PubMed:25730548};
PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:25730548}.
null
null
FUNCTION: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the dialkyldecalin moiety in pyrroindomycins, via an endo-selective [4+2] cycloaddition reaction. {ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:29657086}.
Streptomyces rugosporus
K7QVW7
PYRI4_STRRG
MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC
5.-.-.-
null
antibiotic biosynthetic process [GO:0017000]
null
isomerase activity [GO:0016853]
PF18678;
null
null
null
null
CATALYTIC ACTIVITY: Reaction=4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate = (1S,3R,6R,8R,9R,11R,14S,15S,19R,20R)-8-ethyl-9,15-dihydroxy-3,4,6,20-tetramethyl-21,23-dioxo-24-azapentacyclo[20.2.1.0(1,6).0(11,20).0(14,19)]pentacosa-4,12,22(25)-trien-25-olate; Xref=Rhea:RHEA:64480, ChEBI:CHEBI:155855, ChEBI:CHEBI:155856; Evidence={ECO:0000269|PubMed:25730548}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64481; Evidence={ECO:0000269|PubMed:25730548};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=224 uM for 4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate {ECO:0000269|PubMed:25730548}; Note=kcat is 342.6 min(-1). {ECO:0000269|PubMed:25730548};
PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:25730548}.
null
null
FUNCTION: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the spiro-conjugate moiety in pyrroindomycins, via an exo-selective [4+2] cycloaddition reaction. {ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:26877021}.
Streptomyces rugosporus
K7SGN7
ZAR2B_XENLA
MAGFMYAPYNVYQGYGGNFGQNPHVAQPLAKNKQAAWKSNKASEPTDYLDNFQRAQLKAILSQVNPNLTPRLRKANTKEIGVQVNPRVDTGVQCSLGPRTLRRPPPPPCSPVKAADCVRFTRPLAVYSPVVDRRLFSLPQGGRLPKKSPDSQSQPLKERAPSPEDKEREKVSEKEPDTKDELEKRPVPGTEEPGNEEQTKSAFQFLEQKYGYFHCKDCKTRWESAYVWCISGSNKVYFKQLCRKCQKGYNPYRVEAIQCQVCAKTRCSCPQKQRHIDLKRPHRQELCGRCKNKRLSCDNTYSYKYIV
null
null
negative regulation of translation [GO:0017148]; oocyte maturation [GO:0001556]; translation [GO:0006412]
cytoplasmic ribonucleoprotein granule [GO:0036464]
metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]
PF13695;
null
ZAR1 family
null
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:C3VD30}.
null
null
null
null
null
FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (PubMed:22732570). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs, inhibiting their translation (PubMed:22732570). {ECO:0000250|UniProtKB:Q80SU3, ECO:0000269|PubMed:22732570}.
Xenopus laevis (African clawed frog)
K7TLS0
MYB69_MAIZE
MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY
null
null
positive regulation of DNA-templated transcription [GO:0045893]; regulation of lignin biosynthetic process [GO:1901141]; response to auxin [GO:0009733]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF00249;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:35640133}.
null
null
null
null
null
FUNCTION: Transcription factor that binds to the promoter of MYB31 and MYB42 and activates directly their expression, thus repressing lignin biosynthesis. {ECO:0000269|PubMed:35640133}.
Zea mays (Maize)
K7U9N8
OP1_MAIZE
MSYRKGLKVWVEEKGEGWVEAEVVEAKERAVVVFSSQRKKITVSPEKLLPRDTDEDLGGGHVDDMTKLTYLNEPGVLYNLKKRYALNEIYTYTGSILIAVNPFTRLPHLYNEYMMEQYKGIRLGELSPHVFAVADASYSRAMVNDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRAALDDRTVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDSSGRISGAAIRTYLLERSRVVQITDPERNFHCFYQLCASGKDAELYKLGHISSFHYLNQSNTHDLEGTNNEDEYWKTKRAMDIVGISREDQDAIFRTLAAILHLGNIEFVPGKDADSSKIKDSTSNFHLQTAAKLFMCDSDLLVSTLCSRSIHTREGIIVKALDCAAAAANRDALAKTVYARLFDWLVENINKSIGQDVDSKLQIGVLDIYGFESFKNNSFEQFCINFANEKLQQHFNEHVFKMEQEEYKSEEINWSYIEFIDNQDVLDLIEKKPIGIIALLDEACMFPKSTHETFATKMFRNFSSHLRLERTKFSETDFTISHYAGKVTYQTDSFLEKNRDYIVAEHCNLLSSSRCPFVSGLFTSLPEESIRSSYKFSSVASRFKLQLQALMETLNSTEPHYVRCVKPNSANRPQLFENQSVLHQLRCGGVLEAVRISLAGYPTRRTYAEFVDRFAVLVPELMIGSYDEKMMTKGILEKMKLENFQLGKTKVFLRAGQIAILDMRRAEILDNAARHIQGRFRTFITRKEFVKTREASISIQAYCRGCLARKMFANRRETAAAVIVQKYVRRWLLRRAHLQACLAALLIQSYIRGFIARRYFSVIREHKAATVIQSTWRRRKFVILFQNYRQATVAIQCSWRQKLARKELRKLKMAANEAGALREAKNKLEKKMDDLALRLTLERRLRASSEESKSVEILKRDKIIESLSAECAAAKSAAQNEHAKKLLLQKQLDDSLREITMLQSKKIMSAEAAEENSNLKNLVESLSTKNSILENELIVTRKSSDDTMEKLKEVEGKCNHLQQNLDKLQEKLTNLENENHVLRQKAFNMPTMNNLSVAPKTLSEKFSASIGLPNSEPKHIYESPTPTKYLASLPQTLSTSRRSRLPVERHEQNHEILLRCIKENLGYKDGKPVAACIIYKCLLHWRAFESERTAIFDHVIEAINDVLKGNEADGRLPYWLSNTSALLCLLQRNLRSNGLFTTPSRRSGGALGKIAQTLRSPSKFIGRSDTLPHVDARYPAILFKQQLTACVEKIFGQLRDNLKKEISPLLNVCIQAPKSTRGQSGKASKSSGVGAHPASNSNWDNIVNFLDLLMDTLRENYVPSFFIRKLITQLFSFINIQLFNSLLLRRECCTFSNGEYVKAGLSLLEKWITDVTDEFAGTSWHELNYIRQAVGFLVIHQKRKKTLEEIKQDLCPSLSVRQIYRICSMYWDDKYGTQGISTEVVAAMREMVNKDTQNLVSNSFLLDDDLSIPFSTEDLSMAIPSIDYADVDLPESLQHYTSVQFLLRQQDPQPAQ
null
null
actin filament organization [GO:0007015]; vesicle transport along actin filament [GO:0030050]
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin complex [GO:0016459]; vesicle [GO:0031982]
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
PF01843;PF00612;PF00063;
1.10.10.820;1.20.5.190;1.20.58.530;3.30.70.1590;3.40.850.10;1.20.120.720;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family, Plant myosin class XI subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22892319}. Note=Associated with the endoplasmic reticulum membrane. {ECO:0000269|PubMed:22892319}.
null
null
null
null
null
FUNCTION: Myosin XI motor protein required for endoplasmic reticulum motility and protein body formation (PubMed:22892319). May function by binding with its tail domain to receptor proteins on membranes and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables (By similarity). {ECO:0000250|UniProtKB:Q0WPU1, ECO:0000269|PubMed:22892319}.
Zea mays (Maize)
K7W9N9
CPT6_SOLLC
MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY
2.5.1.92
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23134568};
plastid membrane organization [GO:0009668]; polyprenol biosynthetic process [GO:0016094]; response to cold [GO:0009409]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
2-cis,6-cis-farnesyl pyrophosphate synthase activity [GO:0102059]; dehydrodolichyl diphosphate synthase activity [GO:0045547]; dimethylallylcistransferase activity [GO:0047863]; magnesium ion binding [GO:0000287]; polyprenyltransferase activity [GO:0002094]; prenyltransferase activity [GO:0004659]
PF01255;
3.40.1180.10;
UPP synthase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23134568}. Note=Localizes in punctuate patterns inside the chloroplasts. {ECO:0000269|PubMed:23134568}.
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + 2 isopentenyl diphosphate = (2Z,6Z)-farnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:27810, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769; EC=2.5.1.92; Evidence={ECO:0000269|PubMed:23134568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27811; Evidence={ECO:0000269|PubMed:23134568}; CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate; Xref=Rhea:RHEA:11328, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57665, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:23134568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11329; Evidence={ECO:0000269|PubMed:23134568}; CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate + neryl diphosphate = (2Z,6Z)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:64572, ChEBI:CHEBI:33019, ChEBI:CHEBI:57665, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:23134568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64573; Evidence={ECO:0000269|PubMed:23134568};
null
null
null
null
FUNCTION: Uses neryl diphosphate to catalyze the cis-prenyl chain elongation and produce the 15 carbon product (2Z,6Z)-farnesyl diphosphate. {ECO:0000269|PubMed:23134568}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
K7WDL7
IRIS_CATRO
MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVWDEIVKKNNLVPTKLKEIAAFWFADIAFCSENLISSMNKSKELGFLGFRNSMKSFVSCIDKMRDYRFIP
1.3.1.122
null
monoterpenoid biosynthetic process [GO:0016099]
cytosol [GO:0005829]
identical protein binding [GO:0042802]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; protein homodimerization activity [GO:0042803]
PF01370;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23172143}.
CATALYTIC ACTIVITY: Reaction=(S)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial + H(+) + NADPH; Xref=Rhea:RHEA:62592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64239, ChEBI:CHEBI:144481; EC=1.3.1.122; Evidence={ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0000269|PubMed:30531909}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62594; Evidence={ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0000269|PubMed:30531909}; CATALYTIC ACTIVITY: Reaction=(S)-8-oxocitronellyl enol + NAD(+) = (6E)-8-oxogeranial + H(+) + NADH; Xref=Rhea:RHEA:62596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64239, ChEBI:CHEBI:144481; EC=1.3.1.122; Evidence={ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0000269|PubMed:30531909}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62598; Evidence={ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0000269|PubMed:30531909};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:23172143}; KM=10.6 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:26868105}; KM=4.7 uM for NADPH {ECO:0000269|PubMed:23172143}; Note=kcat is 1.6 sec(-1) with (6E)-8-oxogeranial. kcat is 2.2 sec(-1) with NADPH.;
null
null
null
FUNCTION: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities. {ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:30531909}.
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)