ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q16549 | MPKGRQKVPHLDAPLGLPTCLWLELAGLFLLVPWVMGLAGTGGPDGQGTGGPSWAVHLESLEGDGEEETLEQQADALAQAAGLVNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGPHQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDKMLRSIVTTDWDLQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYEDRRAEWVTNEAGFSHSHQHGFGLLNAWRLVNAAKIWTSVPYLASYVSPVLKENKAIPQSPRSLEVLWNVSRMDLEMSGLKTLEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDESFQVGILRQWQLTLYGSVWSAVDIRDRQRLLESAMSGKYLHDDFALPCPPGLKIPEEDGYTITPNTLKTLVLVGCFTVFWTVYYMLEVYLSQRNVASNQVCRSGPCHWPHRSRKAKEEGTELESVPLCSSKDPDEVETESRGPPTTSDLLAPDLLEQGDWSLSQNKSALDCPHQHLDVPHGKEEQIC | Function: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway.
PTM: Cysteine residues in the cytoplasmic tail are probably palmitoylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86247
Sequence Length: 785
Subcellular Location: Golgi apparatus
EC: 3.4.21.-
|
O75340 | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes . Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes . Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats . In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification . Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway . Promotes localization and polymerization of TFG at endoplasmic reticulum exit site . Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity . Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway . In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21868
Sequence Length: 191
Domain: Interacts with different set of proteins thanks to 3 different hydrophobic pockets . Hydrophobic pockets 1 and 2, which mediate interaction with PDCD6IP, are largely formed by residues from EF-hand 3 (EF3) to 5 (EF5), as well as by Tyr-180 (EF5) of a dimerizing molecule (Pocket 1) and from EF-hand (EF2) to 4 (EF4) (Pocket 2) . Hydrophobic pocket 3, which mediates interaction with SEC31A, is mainly formed by residues from EF-hand 1 (EF1) to 3 (EF3) .
Subcellular Location: Endoplasmic reticulum membrane
|
P12815 | MAAYSYRPGPGGGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair . Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes . Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes . Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (By similarity). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (By similarity). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (By similarity). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis . May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity). Its role in apoptosis may however be indirect, as suggested by knockout experiments . May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21867
Sequence Length: 191
Domain: Interacts with different set of proteins thanks to 3 different hydrophobic pockets. Hydrophobic pockets 1 and 2, which mediate interaction with PDCD6IP, are largely formed by residues from EF-hand 3 (EF3) to 5 (EF5), as well as by Tyr-180 (EF5) of a dimerizing molecule (Pocket 1) and from EF-hand (EF2) to 4 (EF4) (Pocket 2). Hydrophobic pocket 3, which mediates interaction with SEC31A, is mainly formed by residues from EF-hand 1 (EF1) to 3 (EF3).
Subcellular Location: Endoplasmic reticulum membrane
|
G3V7W1 | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKHELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (By similarity). Involved in ER-Golgi transport . Regulates ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (By similarity). Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (By similarity). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (By similarity). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (By similarity). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21905
Sequence Length: 191
Domain: Interacts with different set of proteins thanks to 3 different hydrophobic pockets. Hydrophobic pockets 1 and 2, which mediate interaction with PDCD6IP, are largely formed by residues from EF-hand 3 (EF3) to 5 (EF5), as well as by Tyr-180 (EF5) of a dimerizing molecule (Pocket 1) and from EF-hand (EF2) to 4 (EF4) (Pocket 2). Hydrophobic pocket 3, which mediates interaction with SEC31A, is mainly formed by residues from EF-hand 1 (EF1) to 3 (EF3).
Subcellular Location: Endoplasmic reticulum membrane
|
Q0VCW8 | MQDPNADTEWNDILRKKGILPSKEDLKDLEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEFNEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIKTSLEENPKKPVEDVLLSAVRCSVPAKRDSDSEDD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity).
PTM: N-terminal methionine acetylation destabilizes the protein.
Sequence Mass (Da): 27479
Sequence Length: 240
Subcellular Location: Cytoplasm
|
Q9H2J4 | MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLAEWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation . Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding . Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis .
PTM: N-terminal methionine acetylation destabilizes the protein.
Sequence Mass (Da): 27614
Sequence Length: 239
Subcellular Location: Cytoplasm
|
Q8BVF2 | MQDPNADTEWNDILRKKGILPPKESLKELEEEEAEKEEQLLQQSVVKTYEDMTLEELEENEDEFSEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTALEENPKKPIQDLLLSSVRGPVPMRRDSDSEDD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation . Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity).
PTM: N-terminal methionine acetylation destabilizes the protein.
Sequence Mass (Da): 27581
Sequence Length: 240
Subcellular Location: Cytoplasm
|
P80284 | MAISKVWISLLLALAVVLSAPAARAEEAAAAEEAAAPEAVLTLHADNFDDAIGQHPFILVEFYAPWCGHCKSLAPEYEKAAQLLSKHDPAIVLAKVDANDEKNKPLAGKYEVQGFPTLKIFRNGGKSIQEYKGPREAEGIVEYLKKQVGPASKEIKAPEDATYLEDGKIHIVGVFTEFSGPEFTNFLEVAEKLRSYYDFGHTVHANHLPRGDAAVERPVVRLFKPFDELVVDSKDFDVSALEKFIDASSTPKVVIFDKNPDNHPYLLKFFQSNAPKAMLFLNFSTGPFESFKSAYYGAVEEFSGKDVKFLIGDIESSQGAFQYFGLKVDQAPLILIQDGDSKKFLKEHVEAGQIVAWLKDYFDGKLTPFRKSEPIPEANNEPVKVVVADNVHDVVFKSGKNVLIEFYAPWCGHCKKLAPILDEAAATLQSEEDVVIAKMDATENDVPGEFDVQGYPTLYFVTPSGKKVSYEGGRTADEIVDYIRKNKETAGQAAAATEKAAEPAATEPLKDEL | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 56463
Sequence Length: 513
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
|
P55059 | MHKAQKFALGLLAAAAVATASDVVQLKKDTFDDFIKTNDLVLAEFFAPWCGHCKALAPEYEEAATTLKEKNIKLAKVDCTEETDLCQQHGVEGYPTLKVFRGLDNVSPYKGQRKAAAITSYMIKQSLPAVSEVTKDNLEEFKKADKAVLVAYVDASDKASSEVFTQVAEKLRDNYPFGSSSDAALAEAEGVKAPAIVLYKDFDEGKAVFSEKFEVEAIEKFAKTGATPLIGEIGPETYSDYMSAGIPLAYIFAETAEERKELSDKLKPIAEAQRGVINFGTIDAKAFGAHAGNLNLKTDKFPAFAIQEVAKNQKFPFDQEKEITFEAIKAFVDDFVAGKIEPSIKSEPIPEKQEGPVTVVVAKNYNEIVLDDTKDVLIEFYAPWCGHCKALAPKYEELGALYAKSEFKDRVVIAKVDATANDVPDEIQGFPTIKLYPAGAKGQPVTYSGSRTVEDLIKFIAENGKYKAAISEDAEETSSATETTTETATKSEEAAKETATEHDEL | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 55114
Sequence Length: 505
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
|
P17967 | MKFSAGAVLSWSSLLLASSVFAQQEAVAPEDSAVVKLATDSFNEYIQSHDLVLAEFFAPWCGHCKNMAPEYVKAAETLVEKNITLAQIDCTENQDLCMEHNIPGFPSLKIFKNSDVNNSIDYEGPRTAEAIVQFMIKQSQPAVAVVADLPAYLANETFVTPVIVQSGKIDADFNATFYSMANKHFNDYDFVSAENADDDFKLSIYLPSAMDEPVVYNGKKADIADADVFEKWLQVEALPYFGEIDGSVFAQYVESGLPLGYLFYNDEEELEEYKPLFTELAKKNRGLMNFVSIDARKFGRHAGNLNMKEQFPLFAIHDMTEDLKYGLPQLSEEAFDELSDKIVLESKAIESLVKDFLKGDASPIVKSQEIFENQDSSVFQLVGKNHDEIVNDPKKDVLVLYYAPWCGHCKRLAPTYQELADTYANATSDVLIAKLDHTENDVRGVVIEGYPTIVLYPGGKKSESVVYQGSRSLDSLFDFIKENGHFDVDGKALYEEAQEKAAEEADADAELADEEDAIHDEL | Function: Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
PTM: The N-terminus is blocked.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 58227
Sequence Length: 522
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
|
Q32PP3 | MVSSQAKYELIQEVGRGSYGVVYEAVVRQTGARVAVEKIRCHSPENVELALREFWALSSIQSQHPNVIHLEECVLQRDALAQRMSHGSSSSLYLELVETSLKGEITFDPCCAYYMWFVMDFCDGGDMNAYLLSRKPSRKTNTSFMLQLGSALAFLHRNQIIHRDLKPDNILISQGRTPAGSPEPTLKVADFGLSKVCSGSGLNPEEPASVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGVIIWAMVERITFVDVETQKELLGSYVQQGEDIVPLGEALLENPKMELNIPARKKSMNASMKQLIREMLSANPQERPDAFELELRLVRIACRELDWDT | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38205
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q8N165 | MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRPDAFELELRLVQIAFKDSSWET | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38546
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q8QZR7 | MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQSRMDTSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRPDAFELELRLVQIAFKDSSWET | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38550
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q15118 | MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVPSREPKDMTTFRSA | Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
PTM: Phosphorylated by constitutively activated ABL1, FGFR1, FLT3 and JAK2 (in vitro), and this may also occur in cancer cells that express constitutively activated ABL1, FGFR1, FLT3 and JAK2. Phosphorylation at Tyr-243 and Tyr-244 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect.
Catalytic Activity: ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]
Sequence Mass (Da): 49244
Sequence Length: 436
Subcellular Location: Mitochondrion matrix
EC: 2.7.11.2
|
Q63065 | MRLARLLRGGTSVRPLCAVPCASRSLASDSASGSGPASESGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKTIYEFTDTVIRIRNRHNDVIPTMAQGVTEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKHIGSINPNCDVVEVIKDGYENARRLCDLYYVNSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKGVYPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTESIERLPVYNKAAWKHYRTNHEADDWCVPSREPKDMTTFRSS | Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
PTM: Phosphorylated by constitutively activated ABL1, FGFR1, FLT3 and JAK2 (in vitro), and this may also occur in cancer cells that express constitutively activated ABL1, FGFR1, FLT3 and JAK2. Phosphorylation at Tyr-241 and Tyr-242 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect (By similarity).
Catalytic Activity: ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]
Sequence Mass (Da): 49081
Sequence Length: 434
Subcellular Location: Mitochondrion matrix
EC: 2.7.11.2
|
Q38WI8 | MTAIPIFIISDSIGETARTVIAAVNAQFPASVTLKIQRFPFITDQKTLTPILQDAHQEQAIIVSTLVNHTLQETVTQFCQAKHLTLIDLLSPLTTAISERSQTASLETPGSLRKLDEHYFHRISAMEFAVRYDDGQDPRGLLEADIVLLGVSRTSKTPLSMYLANQNYRVANLPLIPNVPLPKELFKVPAHKIIGLTMPLSTLLKIRQERLATLGLPQTTNYSNMTTVGDELAYANQIFEQLNATTINVADRSIEETASLIQTLI | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 29350
Sequence Length: 265
EC: 2.7.11.32
|
Q8Y634 | MENPVIIYVISDAIGETAQHIIRAVTAQFSLNKPADIRRHAFIRDESALLETLEEAKATDGIVVQTLVQAKLAEYATNFCVQNNIPNVDLLHTLTAAVEAKTGLKSKQDPGNMRRLDSNYFDRIAAIEFAVKYDDCKDPRGLLDADIVLVGVSRTSKTPLSSFLANQNWKVANVPLVPEIPIPAELFQIPAERIIGLTTTPEKLAQIRKVRLRSIGLDEASSYSSEKRILEELEYGYDTFKKLGCQVIHVEDKAIEETAALITEIITSYH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30020
Sequence Length: 270
EC: 2.7.11.32
|
Q8UJC7 | MENKKSFFHLHLISDSTGETLMSAGRAVSAQFHTSMPVEHVYPMIRNQKQLAQVIDLIDKEPGIVLYTIVDQQLAEFLDLRCHAIGVPCVNVLEPIIGIFQTYLGAPSRRRVGAQHALNADYFARIEALNFAMDHDDGQMPETYDDADVVIIGISRTSKTPTSIYLANRGIKTANIPVVPNVPLPESLYAATRPLIVGLVATSDRISQVRENRDLGTTGGFDGGRYTDRATIMEELKYARALCARNNWPLIDVTRRSIEETAAAILALRPRTR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30303
Sequence Length: 273
EC: 2.7.11.32
|
Q2GFU3 | MSTSVTLNLHLISDSTCETVASVARSALEHFRSVEVNEFVWSFINNNEQIDKIMSLIEKDKYNFIMYTMFDDELRRYLKQKAGAQEIPCIPVLSHVIREISCYLHIKKDPYISTNIGLDDEYFTRIDAINYTIAHDDGQNLWDIDQADIIILGVSRTSKSPTSIYLAYRGYRVVNIPLVHSINLSVDLSNMKNKLIVGLTIDIDRLIEIRRTRLVSMKNQNNYQYVDYEHVLMEIKETKRICVQNGWPIIDVTQKSVEEIAATIIQYFNKMQH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31704
Sequence Length: 273
EC: 2.7.11.32
|
Q5HBX0 | MSNPVVLNLHLISDSTCETVAAVARSALEHFKSVEVNEFVWSCINSYEQIDKIMLTIEKDKYNFIMYTMFDDDIRKYLKQKAGIHEIPCIPILSHVIREISCYLNIKKDPYINTSIGLDDEYFTRIDAINYTIAHDDGQNLWDIDQADIIILGVSRTSKSPTSIYLAYRGYRVVNIPLINSIELSVDLSKMKNKLIVGLTIDIDRLIEIRRARLVSMKNQNNYGYVDYEHVLMEIRETKKICAKNGWPIIDVTQKSVEEIAATIIQYFTKMQH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31551
Sequence Length: 273
EC: 2.7.11.32
|
Q2N6J9 | MKRIHLHLLSDSTGETLEMIAKAALAQFENADVVRHFWPMVRSRQHLERIVPELSNNPGLVLFTLVNAETRRALRDHCRRLSLPAVDALDEVTAALEVQLGQEAHGRPGRQHKMDEAYFKRVEAIQFTIAHDDGVGWENWEEADIVLAGVSRSSKTPTSIYLANRGYKVANIPLVMESPPPPALYELKNPMVVGLTTAPERLVQIRRNRLLTLNEQAETSYVEKDRVTEEVKFARRLFSDNNWPVIDVTRRSIEETAAAVIRLHNERHARVKPGEKPI | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31611
Sequence Length: 278
EC: 2.7.11.32
|
Q74G02 | MKRSIKHIYLLSDATGETVERVVRAALSQFRDVEARFHRVTRIRSREDVIWALEEVLREPGMVVYTLVDTELAQLLRDEAEAHGLDAIDLISPLLFKLSDFFGEAPQKEPGLLHQINSEYHKRVDAVDFTVKHDDGQDPRGLAKADFILVGVSRSSKTPLSMYLAHKGYKVANVPIVKGIDPPPELYKVDQKRVVGLIIDAERLVQIRTARLRNLGQMPKGSYADYERIEEELEFCRRLYRRNPQWLVIDVTKKSVEESAAEIIQKLAG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30715
Sequence Length: 269
EC: 2.7.11.32
|
Q0BWA1 | MLKDGRETGKWIRVMTAHRMNLHLVSDATGETLNSIARATVSQFEHAQIIYHRWSLIRTRFQLHRVLEGIEAEPGPVLSTLIEPGLRSELENFCSRIGIAVVHVLDPVLSLLQHHIGEQAIARPGRQYVLDADYFRRIDAMHFVLAHDDGQAQVGINEADLCLVGVSRSSKTPTSFYLANRGVKAANIPLVPGLPEPPGLEAPIVPVIGLTIDPEALIEIRRHRLKLIGGQPNVQQNTAYVDLESVKAELIWARRLCARKGWPVIDVTRRSIEETAATVLQLVEAWHERRRSLPPGG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 33116
Sequence Length: 297
EC: 2.7.11.32
|
B8CXH4 | MTEKPRIFIVSDSIGETAQYVVDATVSQFNGYLDSKRFSYVQTTRELNNIIKKATEQKTLIAYTLIDPRLREEIATLARKNNIYAVDIMGPMMEAFEEFFQKKPRLQPGLVHRLDKDYFKRVEAMEFTVKYDDSNDDRGVKEADVVLIGVSRTSKTPMCIYLSYRGYKAANIPLVPEVEPTPLIYENPDNKVIGLTIDPLLLNEIRQERLKSLGIDPESSYASIDRINVELEYAEKTMEKIGCPVIDVTNKSIEESANEVIDYLNG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 30366
Sequence Length: 266
EC: 2.7.11.32
|
Q0C6A8 | MTQPQRPSIYFNVHLVSDSTGETLNAIQRAACAQFENVQPLEHNYYLVRSERQLERVMKEIEAAPGVVWYTISDGALRGRLEAFCRERSIPTLPVLDPSIAMLSRHLGVAPNNRVAGQHALDEDYFERMEAINFTLAHDDGQNVESLIGADVILLGVSRTSKTPTCVYLANRKVRAGNIPLVPGVPLPDFMEKMGDKGPLVVGLKISAERLVQIRRQRLISLNQDEITEYADEEAVRDEITQANRLFQRNGWKTIDVSRRSVEETAAGILNMLHERWGHS | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31514
Sequence Length: 280
EC: 2.7.11.32
|
Q9XDM9 | MSTAINSVEMSLSADEIRERVRAAGVVGAGGAGFPAHVKLQAQVEIFLVNAAECEPMLKVDQQLMWQQAARLVRGVQYAMTATGAREGVIALKEKYRRAIDALTPLLPDGIRLHILPDVYPAGDEVLTIWMATGRRVAPAALPASVGVVVNNVQTVLNIARAVEQRFPVTRRTLTVNGAVARPLTVTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDNPVTKTTGGLLVLPKSHPLIQRRMQDERTVLSVARTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNFHQAATPQLLLSALTCSECNVCESVACPVGISPMRINRMLKRELRAQNQRYEGPLNPADEMAKYRLVPVKRLIAKLGLSPWYQEAPLVEEEPSVEKVTLQLRQHIGASAVANVAVGERVTRGQCVADVPPGALGAPIHASIDGVVSAISEQAITVVRG | Cofactor: Binds 2 [4Fe-4S] clusters (By similarity). The two centers are coupled but must possess different redox potentials (By similarity).
Function: A protein that aids in conversion of cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation . The latter step requires PduO. No free cob(I)alamin is released, suggesting a complex is formed with PduO that finishes conversion to adenosylcobalamin. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC . Another study showed reduction of cob(II)alamin to cob(I)alamin in the absence of PduO. Both reactions require NADH. Cyanocobalamin (CN-Cbl) is not a substrate for the first reaction . Cobalamin reduction probably occurs spontaneously in the presence of free reduced flavin nucleotides, this protein may be involved in electron transfer for this reduction (Probable).
Sequence Mass (Da): 48389
Sequence Length: 451
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Bacterial microcompartment
|
Q9XDM8 | MSQAIGILELTSIAKGMELGDAMLKSANVDLLVSKTICPGKFLLMLGGDIGAIQQAIETGTSQAGEMLVDSLVLANIHPSVLPAISGLNSVDKRQAVGIVETWSVAACISAADRAVKGSNVTLVRVHMAFGIGGKCYMVVAGDVSDVNNAVTVASESAGEKGLLVYRSVIPRPHEAMWRQMVEG | Cofactor: Probably bound by a single Cys residue from each subunit; which protein provides the fourth ligand is unknown.
Function: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 . Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, may selectively transport specific metabolites . May be involved in electron transport across the BMC shell (Probable). Can be engineered to alter permeability of the BMC shell .
Sequence Mass (Da): 19150
Sequence Length: 184
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Bacterial microcompartment
|
P0DUV8 | MERQPTTDRMIQEYVPGKQVTLAHLIANPGKDLFKKLGLPESVSAIGILTITPSEASIIACDIATKSGAVEIGFLDRFTGAVVLTGDVSAVEYALKQVTRTLGEMMRFTACPITRT | Function: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. May selectively transport specific metabolites (By similarity). Not absolutely required to make artificial BMCs . Proteins such as this one with circularly permuted BMC domains may play a key role in conferring heterogeneity and flexibility in this BMC (Probable).
Sequence Mass (Da): 12484
Sequence Length: 116
Domain: One side of the hexamer is concave which is lined by hydrophobic residues, the other side has a slightly protruding, 6-stranded beta-barrel.
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Bacterial microcompartment
|
B1VB80 | MKRIMLIGPSQCGKTSLTQCMRGEALHYQKTQAIVWSPTTIDTPGEYLENRCLYSALLASACEADIIALVLNADAPWSPFSPGFTGPMNRPVIGLVTKADLASPQRISLVESWLVQAGAQKVFFTSALENTGVDEMFIFLNAKESSCLTK | Function: May play a role in the spatial distribution of the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, perhaps being involved in cytoskeleton dynamics; might bind GTP (Probable). This subunit is directly targeted to the BMC .
Sequence Mass (Da): 16332
Sequence Length: 150
Domain: The N-terminus is required for targeting to the BMC; 42 residues target GFP to the BMC, although 98 residues give better targeting.
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Bacterial microcompartment
|
A6TDE9 | MTYKIMAINAGSSSLKFQLLNMPQGALLCQGLIERIGLPEARFTLKTSAQKWQETLPIADHHEAVTLLLEALTGRGILSSLQEIDGVGHRVAHGGERFKDAALVCDDTLREIERLAELAPLHNPVNALGIRLFRQLLPAVPAVAVFDTAFHQTLAPEAWLYPLPWRYYAELGIRRYGFHGTSHHYVSSALAEKLGVPLSALRVVSCHLGNGCSVCAIKGGQSVNTSMGFTPQSGVMMGTRSGDLDPSILPWLVEKEGKSAQQLSQLLNNESGLLGVSGVSSDYRDVEQAADAGNERAALALSLFAERIRATIGSYIMQMGGLDALIFTGGIGENSARARAAICRNLHFLGLALDDEKNQRSATFIQADNALVKVAVINTNEELMIARDVMRLALPQARELAVSA | Function: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of 1,2-propanediol (1,2-PD).
Catalytic Activity: ATP + propanoate = ADP + propanoyl phosphate
Sequence Mass (Da): 43619
Sequence Length: 404
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Cytoplasm
EC: 2.7.2.15
|
P74879 | MSYKIMAINAGSSSLKFQLLEMPQGDMLCQGLIERIGMADAQVTIKTHSQKWQETVPVADHRDAVTLLLEKLLGYQIINSLRDIDGVGHRVAHGGEFFKDSTLVTDETLAQIERLAELAPLHNPVNALGIHVFRQLLPDAPSVAVFDTAFHQTLDEPAYIYPLPWHYYAELGIRRYGFHGTSHKYVSGVLAEKLGVPLSALRVICCHLGNGSSICAIKNGRSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIAQRESKTPQQLNQLLNNESGLLGVSGVSSDYRDVEQAANTGNRQAKLALTLFAERIRATIGSYIMQMGGLDALVFTGGIGENSARARSAVCHNLQFLGLAVDEEKNQRNATFIQTENALVKVAVINTNEELMIAQDVMRIALPATEGLCVPA | Function: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD). Ectopic expression partially complements a cobB deletion allowing some growth on propionate . Restores growth to an eutQ deletion on ethanolamine and tetrathionate under anoxic conditions .
Catalytic Activity: ATP + propanoate = ADP + propanoyl phosphate
Sequence Mass (Da): 43995
Sequence Length: 404
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Cytoplasm
EC: 2.7.2.15
|
B1VB82 | MAVAQCPASCGELIQGWILGSEKLVSCPVEWYSTVEVTSGSPLTDERPLSRAMVDRLLQHWQYPAHLSQDIRIDVQSTIPIAKGMASSTADIAATAIAAAHYLGHQLDEPTLAQLCVSLEPTDSTVFRKLTLFDHNNASTQIGCEAQPQLDLLVLESPETLRTADYHRIPRHSGLQAGAAALQRAWEKVQEACISQNPYRLGEAATLSAIASQLLLPKPDFDSLLALVEECDLYGVNVAHSGSVVGLMLDRNRHDVDYIKWMLTQKKLTIHWPEQHLLRMVTGGVELQ | Function: L-threonine kinase that catalyzes the conversion of L-threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid.
Catalytic Activity: ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine
Sequence Mass (Da): 31681
Sequence Length: 288
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.7.1.177
|
Q164G2 | MSPATAPVLISCGEPAGIGPEIAVAAWDALQGTIPLAWVGDPRHLPASTTFTAITHPRAVADVPTGSLPVLVHDFAAPSTPGHPDPANAQGVIDVIAACVAWVQEGAAAALCTAPIHKKALIDGADFKHPGHTEYLQALAGGRSRAVMMLASDALRVVPTTIHIALEDVPRVLTPALLRETITITHAALQRQFGIQAPRIVVAGLNPHAGEGGAMGLEEQDWIADVISALAASGMNLRGPLPADTMFHARAREGYDAAIAMYHDQALIPIKTLDFDRGVNVTLGLPFIRTSPDHGTAFDIAGKGIANPTSMIEAIKLAAHMAARHV | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 33952
Sequence Length: 326
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
|
Q1GI38 | MTGAPQVIALSCGEPAGIGPEIAVAAWDQLRADCPFVWIGDPRHLPSSHPWQPVSAPAEALQVSADALPVWPLEFAGNTTKGEADPQNASGVIQSIKTGVELVTSGKAAALCTAPIHKKALIDGAGFAYPGHTEFLAALGGVDHVVMMLASAALRVVPATIHIPLSAVPEVLTPDHLRRVITLTDRGLRDQFGLTAPRIAVTGLNPHAGEGGAMGQEEGDWIEALIREMQTEGYRLTGPHPADTLFHAAARARYDAAIAMYHDQALIPIKTLDFDKGVNVTLGLPFIRTSPDHGTAFDIAGKGLANPSSLIEALRLAQTMAKTRQP | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 34339
Sequence Length: 326
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
|
P58717 | MSSAQRVVITPGEPAGSGPDLVVQLAQRAWPIELVVCADGALLTERAAMLGLPLSLLPYSPDVPAAPQPAGTLTLLPVSLRAPAISGQLTVENGPYVVETLARACDGCLNGEFAALITGPVHKGVINDAGISFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRAIADAITPALLHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLDELRAQGMKLNGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGKADVGSFITALNLAIKMIVNTQ | Cofactor: Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 34779
Sequence Length: 329
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
|
Q5PBF2 | MIDFFEGVSWLIMPFSGVCVREADSSPMDVFGLWYSEMLRATGAHMREPSAMVLATCDVQNRPSARVVLLKKYGEAGFEFVTNFNSRKGREIADNPQVALVFDWRHIGRQVRVEGLATLMDASESDAYHASRSRESKISAWCSQQSAVLESRKLLLEQFERERQRFDGQEIPRPGHWGGVRVVPHVVEFWEDGAHRLHSRKQYSRGDSGSWSCVDLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24885
Sequence Length: 218
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
A8HRJ3 | MSDSAMEPQNPLTSGDFTAADEPFRLFSEWLKDAERSEPNDPNAMTLATVDPDGLPDARMVLLKGLDDRGFVFYTNTESAKGRELTAHPKAALVFHWKSLRRQVRVRGPVERVTDAEADAYFATRPRLSQIGAWASQQSRPLEGRFALEAAVATTTARYAVGSVPRPPHWTGFRILPVQIEFWHDRPFRLHDRVVFKRENPEIDWEKSRLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24177
Sequence Length: 212
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q8A7E7 | MKNIADIRQEYTKSGLRESELPCDPLSLFSRWLQEAIDANVEEPTAIIVGTVSPEGRPSTRTVLLKGLHDGKFIFYTNYESRKGRQLAQNPYISLSFVWHELERQVHIEGTAAKVSPEESDEYFRKRPYKSRIGARISPQSQPIASRMQLIRAFVKEAARWLGKEVERPDNWGGYAVTPTRMEFWQGRPNRLHDRFLYTLKTDGKWEINRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24724
Sequence Length: 213
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q6G4D7 | MGNTVQTDNDFMQMQKPFALFAKWLEEATVSEINDPNAMALATVDKTGFPNVRMVLLKDFSPQGFVFYTNYESPKGQEILKSMKASLVFHWKSLRRQVRIRGIVEKVTPQEADAYFQSRPRDSRIGAWASKQSQPLESRFVLEKAIARYTTRYAVGNIPRPPYWSGFRVKPLSIEFWCDRPFRLHDRLLFTRDSVEHVDWKRQKLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24271
Sequence Length: 207
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q6MK45 | MFDINKDPFEHFDRLMKEAVAKQIPEANAMSVATVDEKGVPSVRIVYLKEVSQGGFVFYGNYNSHKGKDIETNPIVCLNFHWPAIWQQIRITGKAEKISAAESDAYFATRARLSQIGAWASHQSETIPALDWLSRRVQEYEKQFDGQVVPRPPHWGGWRVIPTEIEFWFGLGGRLHERHIYQRTEDGGWKTFLRSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 22590
Sequence Length: 196
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q2KVR0 | MSVSDLRQSYERGVLLEQQAAATPIDQFALWFDEAQAAQVPEPNAMTLATVDASGQPSARIVLIKAFDARGFTFFTNYTSRKGEDLLANPRAALLFFWQALERQVRIEGVVERVSADESDAYFHSRPVGSRIGAWASEQSQPITREALEARERDFKARFGDTPPRPPHWGGYRLVPTYFEFWQGRPSRLHDRLRYRPDGKQGWVMDRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 23962
Sequence Length: 210
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q3IDP4 | MKLEDIRREYLQNALSEDNLLDDPFKQFETWLEHAVASNLPDPTAMVVATVDDTGQPSQRIVLLKHLDNDGFVFFTNTGSRKAQELKGNNKISLHFPWHPMERQVIVYGEAKPLPTSAVAKYFLSRPKESQLAAWASAQSRPVSSRKVLMETFANMKNKFAKGEIPLPDFWGGYCVVPQKIEFWQGGAHRLHDRFMYQRQADNSWQITRLNP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24362
Sequence Length: 212
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
Q4FS02 | MNMDFTDQRLSYEKGQLDQQSVPISPFELLKAWMHEAIEEQVQEPYAMSLATCGADDKPSVRIVLLREITDKGIVFYTNYESAKGQDIAENPNAEALFFWHKLERQIRISGSIAKIDADKSAAYFQKRPHDSQVGTWVSQPQSGEVASRDVMEQTFEQLQTDYPDGAAVPTPGFWGGYEITVSEIEFWQGRANRMHDRIVYHKEVDGSFSTKRLLP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24642
Sequence Length: 216
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
A1SUY2 | MSFISKIRCAFTLGQGVLIENEALKETNDPILFFNNWLKKAQDTGIILPESMSISTCTPEGRPSSRMVLLKEVDSKGFVFFTNYDSRKAHDLEANPFAALLFHWNILQRQVRIEGRVERISTAQSNAYFQSRGRGSRIGAWASHQSQELNDRQTLVERVKYFEEKFAGKEIPLPEFWGGYRVIPESIEFWQGKADRLHDRFVYQPTEKNWTVKRLNP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 25178
Sequence Length: 217
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
|
A5FJ95 | MTKLSVNINKIATLRNARGGNVPDLLKVAADIQRFGGQGITIHPRPDERHIRYQDARDLKAIVTTEYNIEGNPQHNFIDLVLECKPDQVTLVPDAIGAITSSAGWDTIKNQEYLKEVIQEFQRNGIRTSIFVDPVLEMIEGAKKTGTDRIELYTEAFAHQYDLGNKNGIDPYVKAAELANELGLGINAGHDLSLDNIQFFKQNIPGLLEVSIGHALISEALYLGLDNVVNMYLKKLK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 26351
Sequence Length: 237
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
B9M5K2 | MARLGVNIDHVATIRQARGGAEPDPVAAAAIAELAGADGITIHLREDRRHIQDRDLRLLRQTIKTRLNLEMAATDEMVSIALSVKPDMCTLVPEKRQELTTEGGLDVRLHLDAIRGAVQKLQDGGLIVSLFIDPDTDQIKAADKSGADYIEIHTGAFAEASDWKAEQEELKKIENAIKLAGKLGLGVNAGHGLNYSNIRKVAALGGIEEYNIGHSIISKAVLVGLDRAVRDMVDLVKYS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 25871
Sequence Length: 239
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
Q3V8C9 | MAKLGVNIDHVATIRQARGGVEPDPVAAAAIAEFAGADGITVHLREDRRHIQDRDLRLLRQTVKTKLNLEMAATDEMVGIALSVKPDMCTLVPERRQELTTEGGLDVRVGMQALADAIGRLQDGGIVVSLFIDPDADQVKASSKVGADYIEIHTGTFAEAREWKKEQAELERIENAIKLGTKLGLGINAGHGLNYTNVRKVAALGGIEEFNIGHSIISRAVFTGLDRAVRDMVDLVKYA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 25887
Sequence Length: 239
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
Q5FNS2 | MIRLGVNIDHVATLRNARGGTFPDPVAAAELAIASGADGITAHLREDRRHIRDADMPRLRALSAPLNFEMAATDEMVRIACDLRPHACCLVPEKRQEVTTEGGLDIVGQSEALKPKIARLRDAGIRVSLFIDPEARQIETAAALGAPVVELHTGAYALGGSEELERLRSAAGTVAACGLELHAGHGLTYDNVGAIADLTGLAELNIGHFLIGQAIFDGLGPVVRKMKSLINS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 24562
Sequence Length: 232
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
O26102 | MRFGLNIDHIVTLREIRKTYEPEILEALFIAKNTHKVDLITIHLREDRRHIQNEDVLKLLEISPLPINIECSINAEITDFLCSLKNKPSKVTIVPENRNEVTTEGGLDCSLKGLGEVIRAYHNKGIEVSLFIDPLKDALHFAREHQVKQVEFHTGVYANLHNALYSNANNQIHAISVLKDKSPKELKEELHNAFLQLRRMSKEAFFMGITACAGHGLNYTNVKELLKIPSLRELNIGHSVVSKAVLVGLEKAILEMAQLIKR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 29721
Sequence Length: 262
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
Q8D304 | MSKLLLGVNVDHVASLRNVRGGKFPDPVQLAILAEIAGADSITTHLREDNRHINEKDVICIKKSIQSRLNLEISTKKEMINKAINILPYSCCLVPENRQEITTESGIDVIKNKKYLKKVICKLKSLGIKVSLFVDPIKNQILSSSEINADCIEINTGKYSEQDKKENKEEINLIKLCAKYANKLGLEVHAGHGLNYFNVRSIVNIKEIKELNIGHSIISRSLIVGMQNAVKEMKDIIYSEKIKWQ | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 27605
Sequence Length: 245
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
B3CLF3 | MKLGVNIDHVATLRNARGASYPDPLKAAKIAINAGADFLTVHLREDRRHIRDEDVFNLKQNISTELNLEIAATEEMLKIAKEVKPYSICIVPEKREELTTEGGLNIVNMHSKLSGIIEEMHSFDIKVSLFIDPNINQLKYLEKLERKPDIIEIHTGDYCDNPSEEKLKLITNSAEYINNLGIECHAGHGINYKHAKEIKKIPHISALNIGHSLISEAIFHGLHSVTKKMKMTISK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 26491
Sequence Length: 235
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
A7IM59 | MAVLKPVRLGVNVDHVATVRNARGGALPDPVRAAALAKAAGAHGITAHLREDRRHIRDADMERLKAEIDLPLNFEMAATDEMVAIACRVRPNACCLVPERREERTTEGGLDAAGQRAELAPRIARLKAAGIRVSLFIAADPAQIAAAAELGADIVELHTGAWCDAVTEGRHVEAEAEFVRLKAGARQAAGLGLEVHAGHGLDYATAERIAAFPQIVELNIGHFLIGEAIFVGLDQAIARMRAAIAAGRAAVGDGAAA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 26963
Sequence Length: 257
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
Q9PH84 | MSQRTRLSVNVNKIAVLRNSRGDGAPDVIRAASACIDAGAHGITVHPRPDARHIRHDDVIGLSALTRARGVEFNIEGNPFAEPRAGYCGLLALCRETRPHQVTLVPDGDQQITSDHGFDFAREGPGLRPLIDEIKQWGCRVSLFVDVNVTGLADAAIWGVDRIELYTGPYAEMHHAGCSDAVLREFATTARLAQDVGLGVNAGHDLSQTNLGVFLGAVPDVLEVSIGHALISEALYEGLVPTVRRYLDILDSVNPAVSMR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 28014
Sequence Length: 260
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
|
O59080 | MDKLKIIMEKGTERLKRGFAKMVKGGVIMDVTNAEQARIAEEAGAVAVMALHKVPADIRKAGGVARMAPVEKIQEIMDAVTIPVMAKCRIGHEAEARILEALGVDMIDESEVLTPADPFFHIYKKKFTAPFVCGARNLGEAVRRIWEGAAMIRTKGEAGTGNIIEAVRHVRLVNENIRLIQRMTDEEIYGVAEKFAEPYLRLAFSVKEISGLPKRVLENEPIYEGFTYREIVEDIYKILLEIKKLGRLPVVNFAAGGVATPADAALMMAMGMDGVFVGSGIFKSSNPPKMARAIVEAVNHWDEPDVLAEISREIGEPMRGQAIEELQVRMEERGI | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 37014
Sequence Length: 335
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
Q9UWX3 | MRLYELSFAQIEDFFYKLAEVKDIIKDHGLLEFLPEFKKLDSTVHTGTTRVKHAFPIFQKGGVVMDITNVQQAQIAEEAGAVAVMVLDKLPYDVRKSGGVARMADPKIIEEVMSSITIPVMAKVRIGHYYEAKLLEALGVDMIDESEVLTPADEEHHINKWEFSVPFVNGARNLGEALRRTSEGASMIRTKGEAGTGNVSEAVKHMKIINSEIRSLISMSEEDRVKKAREYQVPYQIVELTAKIKRLPIVNFAAGGIATPADAALMMWLGADGLFVGSGIFKSQDPDERAKAVVLAAACWEYPEIVLEAQKMISEQKSMMGIDIKSLKPEELLQVRGL | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 37495
Sequence Length: 338
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
A5UY93 | MTVGILALQGDFREHEEMLRRIGAPTLQVRLPKHLQHVERLIIPGGESTTIGKLLAMYGLIDPLRARIRDGMPVWGTCAGAILLAQRIADGRADQPSLRLMDVTARRNAFGSQLESFEVDLPVLGLGDEPLRMVFIRAPVLEDLGRDVTPLAHLDDGRVVAARQGTMLATCFHPELTPDERMHRYFLAM | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21011
Sequence Length: 189
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
Q1AWE7 | MAGRRNGHAGRPRVGVLALQGDFREHAEILERLGAEPVEVRRPEDLRGLDGLIIPGGESTAIGNLMVHSGMLDAIRSFFYQGGAVWGTCAGMVLAASATTGPSQPLLGIMSALVERNGFGRQVHSFEADLEVKGFDRPFRGVFIRAPYFEDVGPGVEVLAEIDGRVVAARAGKVLVTAFHPELTDDTRFHEYFLREVCGSDERS | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 22091
Sequence Length: 204
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
A4FBA2 | MGGVSTARPVIGVLALQGGVAEHLTALERSGAEARPVRRPEELAQVHGLVLPGGESTAMTRLLDGFELFEPLRERLAAGMPAFGSCAGMVLLAGTVLDDRVEQDTPPVRPFGAIDMAVRRNAFGRQVDSFEADLDFAGVTDGPVHAVFIRAPWVDKVGADVRVLASVAPSGHGSEVTAPAGRIVAVQQGPVLATAFHPELVSGDERVHRYFVQTVRAS | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 22963
Sequence Length: 218
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
Q9UWX4 | MKIGIIAYQGSFEEHFLQLKRAFDKLSLNGEIISIKIPKDLKGVDGVIIPGGESTTIGLVAKRLGLLDELKEKITSGLPVLGTCAGAIMLAKEVSDAKVGKTSQPLIGTMNISVIRNYYGRQKESFEAIVDLSKIGKDKAHVVFIRAPAIAKVWGKAQSLAELNGVTVFAEENNMLATTFHPELSDTTSIHEYFLHLVKG | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21693
Sequence Length: 200
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
Q02CB5 | MKKVGVLSLQGDFAAHGAALERAGAQPVFVREREQLNQIEGLILPGGESTTMLKLLRYEDLFDDVAEFGRTKPVFGTCAGAILMAKGVTNPAQESFGLVDIEVERNAYGRQTDSRIAQVRPFPDFENRTAPGELKAVFIRAPIIRRIEDGVRVLASYQGDPVLIEQGRFLVATFHPELTDDARVHSLFLSKL | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21182
Sequence Length: 192
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
|
Q15121 | MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA | Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface.
PTM: Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones.
Sequence Mass (Da): 15040
Sequence Length: 130
Subcellular Location: Cytoplasm
|
Q62048 | MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEEELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA | Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity).
PTM: Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones.
Sequence Mass (Da): 15054
Sequence Length: 130
Subcellular Location: Cytoplasm
|
Q9FR44 | MAASYEEERDIQKNYWIEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESINGHYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHYREPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYERVFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQRGYDLHDVQAYGQMLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLERCASDEQKWGLFIANKN | Function: Involved in phosphocholine biosynthesis . Catalyzes the N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine (PC) . Required for root system development and epidermal cell integrity through its role in choline and phospholipid metabolism . In association with NMT3, regulates PC homeostasis, phase transition at the shoot apex, coordinated organ development, and fertility . In association with NMT3, involved in phosphatidylcholine biosynthesis and vascular development . In association with NMT2, involved in the production of phosphatidylcholine in roots, essential for root development . In association with NMT2 produce phosphocholine mainly for leaf growth maintenance . Contributes to the regulation of overall root zonation dynamics through reactive oxygen species (ROS) and auxin-regulated cell differentiation . Participates in root development of primary root elongation under salt stress conditions by balancing reactive oxygen species (ROS) production and distribution through abscisic acid (ABA) signaling .
Catalytic Activity: phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 56103
Sequence Length: 491
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from phosphoethanolamine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.1.103
|
A0A1B2CTB4 | MLPRALTLSALLALLLAIYLALAPARLSCRCRSWEQCWPSLEAWSHLNASLNSHLVDLRPIASVCHEPILDQPACDIVRRMSNSGRWRTGQPGALINSFWESGFGSNETCSLSSGQENLCHQGRIPLYAAVVESTQEVQTAVKFAREHNLRLVIRNTGHDGAGSSSGPDSFQIFTHRLSDILYHENFRITGSNTSVGPAVSIGAGVLFGDLYVHGGQKGFIVTGGDSATVGAAGGFTQGGGVPGFLGHTWGLAADNVLEFEIVTATGNLVIANAGQHPDLFWALRGGGGGTFGVAVRVTMRTYPDHPAVKSTISITGDGQSPSFWSEGIAGLLTVLQSLNRQGTAGVFRLWQTPAGLLGASTEVYFLNQTEVKDASSVIKSTLGNASDIYIISSNALDTLSSDVEADAPTINELFGSTLVSNGLFQSESGPKLIAERMSQIGLNDGEWILTSNLGGQVNDNKRANTPLHPAWQSSAQLVSLVVNVDTAPGARDRAMRRLTNELMPRLYALDPSQRVSYRNMGDPNEPHFKEVYWGATNYDRLVQIKRDWDPKDLFISRVGIGSERWDFEGFCKV | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group . The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity). PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity). The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene . The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 . The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group . The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C . PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D . Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone .
Catalytic Activity: A + peniprequinolone = AH2 + yaequinolone E
Sequence Mass (Da): 61916
Sequence Length: 574
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.99.-
|
P01212 | MGLEARHCCMFLLVFASLSVEIRADCSKDCASCALHLGQQREINSLACTLECEGKLPSAKAWGTCKELLLLTKVDNVQDGEKYQDNNDSHYAAKKYGGFMKRYGGFMKKMDELYHAEPEEDDAGGEILAKNYGGFMKKEYDSDRDAADLLRELLATSGDPESSIYHDNNSETPGEINKRYGGFMRGYRRSTDLEDETSGIQKRYGGFMRRVGRPEWWEDYQKRYGGFMTRFTDSFLPSDEDGESYSKENPDMEKRYGGFMRF | Function: Enkephalin neuropeptides compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
Sequence Mass (Da): 29932
Sequence Length: 262
Subcellular Location: Secreted
|
P01211 | MARFLGLCTWLLALGPGLLATVRAECSQDCATCSYRLARPTDLNPLACTLECEGKLPSLKTWETCKELLQLTKLELPPDATSALSKQEESHLLAKKYGGFMKRYGGFMKKMDELYPLEVEEEANGGEVLGKRYGGFMKKDAEEDDGLGNSSNLLKELLGAGDQREGSLHQEGSDAEDVSKRYGGFMRGLKRSPHLEDETKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEPLPSEEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 29788
Sequence Length: 263
Subcellular Location: Cytoplasmic vesicle
|
Q28409 | WETCKEFLKLSQLEIPQDGTSALRESSPEESHALRKKYGGFMKRYGGFMKKMDELYPQEPEEEAPAEILAKRYGGFMKKDAEEEEDALASSSDLLKELLGPGETETAAAPRGRDDEDVSKSHGGFMRALKGSPQLAQEAKMLQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFADSLPSDEEGESYS | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Processed and degraded by ACE.
Sequence Mass (Da): 21267
Sequence Length: 187
Subcellular Location: Cytoplasmic vesicle
|
P01210 | MARFLTLCTWLLLLGPGLLATVRAECSQDCATCSYRLVRPADINFLACVMECEGKLPSLKIWETCKELLQLSKPELPQDGTSTLRENSKPEESHLLAKRYGGFMKRYGGFMKKMDELYPMEPEEEANGSEILAKRYGGFMKKDAEEDDSLANSSDLLKELLETGDNRERSHHQDGSDNEEEVSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEALPSDEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 30787
Sequence Length: 267
Subcellular Location: Cytoplasmic vesicle
|
A0A1B2CTC1 | MGSIDDSFSLPAPSDEHGFEALGTQLVEAMSTYAKCLKAENLPPPSLYPMFSASTSVACPEGIEAKRKIVELSQLICAATMDPELNLLISSLQFHFCSSLKVAIDLRIYEYIPVDGTVSLSQLAELAGRIMRVLTNKHVFMQIQPGHYAHTRMSSLLLKTKAKDLLSHRLDDVFRSASREADALAQAGYREPDRRAAKGFNLAFNTDKNFWEYIATDDPKRGARFARAMHAVNINSLDVIPRLYPFDSLATDGSLIVDVGGGQGQVAKRILEYYPNSGLRCIVQDGYVTNGSTAGPAAVEMHRHDFFEAQPIKGAAAYFFRHIFHDWPDNACVTILKQTARAMDKHRSRILICDQVLDDNSPAEASLLYDIDMMSLFGGKERSLAEWKSLIYSAGENLEIVNVLRSPESEAAILDVRLKL | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group . The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity). PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity). The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene . The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 . The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group . The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C . PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D . Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone .
Sequence Mass (Da): 46553
Sequence Length: 420
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
|
P04094 | MAQFLRLCIWLLALGSCLLATVQADCSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSKPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPVEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDSTSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 30932
Sequence Length: 269
Subcellular Location: Secreted
|
Q9GMY3 | MKWMVVVLLCLQLLEAKVVKVPLKKLKSLRETMKEKGLLEEFLKNHKYDPAQKYRYTDFSVAYEPMAYMDAAYFGEISIGTPPQNFLVLFDTGSSNLWVPSVYCQTQACTGHTRFNPSQSSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGMAYPSLAMGGATTALQGMLQEGALTSPVFSFYLSNQQGSQNGGAVIFGGVDNSLYQGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSQGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDQYGQFFVNCNYIQNLPTFTFIINGVQFPLPPSSYILNNNGYCTVGVEPTYLPSQNGQPLWILGDVFLRSYYSVYDMGNNRVGFATAA | Function: Hydrolyzes a variety of proteins.
Catalytic Activity: More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.
Sequence Mass (Da): 42921
Sequence Length: 389
Subcellular Location: Secreted
EC: 3.4.23.3
|
Q48558 | MKQTECTTILVGKKASIDGSTMIARSEDGGRVIIPEGFKVVNPEDQPKHYTSVISKQKIDDEDLAETPLRYTSAPDVSGKNGIWGAAGINADNVAMTATETITTNSRIQGVDPILDPSEGGLGEEDFVTLTLPYLHSAFDGVKRVGYLVEKYGTYEMNGMAFSDKDNIWYLETIGGHHWIARRIPDDAYVIAPNRLNIDTFDFDDSENFATASDLKDLIDEYHLNPDREGYNMRHIFGSSTIKDAHYNNPRAWYIHNYFDPDFGGTPADQDQPFICRANRLISIEDIKWAESSHYQDTPYDAYGDQGTPEQKKTFRPIGINRNFETHILQIRNDVPAEIAGVQWLAFGPNTFNSMLPFYTNVTTTPEAWQTTPKFNLNKIFWLNKLTAQLGDTNYRVYGELEDAFEQKSLAQCHKIQHETDKEVKNLSGKELQDKLIAANQKMSDTVYNNTVELLGQMVDEGHGLMTLKYDLLD | Function: Hydrolyzes a wide range of dipeptides but unable to hydrolyze dipeptides containing proline. Highest activity against Met-Ala.
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Sequence Mass (Da): 53513
Sequence Length: 474
EC: 3.4.13.19
|
Q8G6Z9 | MACTTILVGKDASYDGSTIIARNEDSANGEFNPKRFIVVKPEEQPREYKSVISHLTITLPDDPLQYTAVPNADLKEGIWGEAGVNEANVAMSATETLTTNERVLGADPFVEYTPAKGDEPEVPGGIGEEDFLTIVLPYVKTAREGVQRLGALLEEFGTYEMNGVAFSDSNEIWWLETVGGHHWIAKRVPDEAYVTMPNQLGIDEFDLEDALGDQEAHMCSEDLAEFIETNHLDLAVENTTPFNPRDAFGSHSDSDHVYNTPRAWYMQRFLNPYDEVWDGPDADHKPTSDDIPWARQPERKVTIEDIKYVLSSHYQGTPFDPYGQLGDERTRHMYRTIGINRQSQLAVMQIRPYRPQASRAIQWMAYGSNPFNTLVPFFPNVDTTPAYLEDTTTRVTSENFYWANRIIAALCDGAFRSTSNAVERYQEKTGAMGHRLVAATDEQIARLGLTAAEEAAQSAAEEEFEADNVDGDVQPMTPDETIAALRNPEVREILAAANQTMADQLKEETEKLLDSVLYTRSMEMKNGFHMSDF | Function: Hydrolyzes a wide range of dipeptides. Highest activity against Ala-Gln.
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Sequence Mass (Da): 59751
Sequence Length: 533
EC: 3.4.13.19
|
B8F8H3 | MQQLFSQHIARIQQIVQHALELARLDGLWIYAGQAKYHFLDDQTSPFKINPHFNYIFPDPTVEQSWLFLDGKNKPKLYFYAPQDYWHCTPNPPTSAFFADEFEWQMLTDSQQIQQYIINPTHCAFIGEQTELAKSLGFEHINPQKVLNVLHFERSIKSEFEIECIYQAQLTALAGHHAAKEAFFASKSEFEINLAYLQATKQSDNNVPYGNIVAINQHSAILHYTKLDFTPPCERHSFLLDAGTSYLGYASDLTRTYAFEPQSEFAAMIAQMEQFKLDTIADMQVGMNYLSYHTQMHRWISQMLHQFEFVKLPADQIFEEGISRTFFPHGLGHQLGLQVHDVAGFQQNHRGTRKAPPEIYPSLRCTRDLAEGMVLTIEPGFYFIEMLLNQWKNHPLAPFFNWQKIDEFKRYGGIRTEDNIVMRATGAENLTAKAESISSR | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
Catalytic Activity: H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline
Sequence Mass (Da): 50882
Sequence Length: 440
EC: 3.4.13.9
|
Q2S6U2 | MSDSAYQNHLSILRKRFDQALLETDFDGVILASGRLTYYFGDDHSHPFHPYAMAQQWAPFDLMPDVFIHIQRGETPRLLWPAKQDFWHVVYPIPEGGWCDQWRVEPVSSLQEWLPQISGKTAWIGPEYNEAPGLNPNLSVNPEALLHRLNYQRAYKTEFEIDCLWRANQAGAAGHKAAQAAFLTGKSECDVYRDFLAASGQLSNQEPYPGIVALNENAAVLHYEKKNPLKPDAMRTLLIDAGAAYGGYASDITRTYTAGSGLFAELIERVNTLQLSIAAQAVHGKAFSELHQATLAGVANILHETRICSLSVEAQLDKRIPQVFFPHGLGHLLGLQVHDVGGHQQDKTGTLRKPDESAPFLRLTRTLEKDMVITIEPGLYFIPMLLDNMVKNIAGHGCDLDLIETLKPYGGIRIEDNVVVQEGRSRNLTREAFSALLA | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
Catalytic Activity: H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline
Sequence Mass (Da): 48837
Sequence Length: 438
EC: 3.4.13.9
|
B9EAD7 | MKEKLIDRLTSYVVIDTQSDASSTTTPSTDKQWNLLNQLKQEIEQLGLETDIDEYGYLFATLPSNTNKDVPVIGLLAHVDTATDFTGTNVNPQIIQSYDGNDITLKSGLKIETAKFPELSLYKGHTLITTDGTTLLGADNKAGIAEIMTAIEYLIAHPEIKHGKIRFGFTPDEEIGRGPHKFDVERFACDFAYTIDGGRRGELQYESFNAAGVNVTFNGVNVHPGSAKDKMVNALNLAVRFQSSLPANEVPEHTEGYEGFFHLMELNGNVERAQLSYIIRDHSREQFEARKVKMHEIITSIQNEYGEQAAHIEINDQYYNMGEKITPHPQLIDIPLEVMKSLNIEPIVEPIRGGTDGSQLSYMGLPTPNLFTGGENYHGPYEYVSVDDMERAVMNIVGILQKFEEKA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45438
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 3.4.11.4
|
Q6D4E3 | MDKLLDRFLNYVSFDTQSKSGVRQVPSTDGQLKLARALQQELLELGFEQIVLSKQGCLTAALPSNVAWSVPAIGFISHMDTSPDFSGKNVNPQILENYRGGDIALGVGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLKKSQLPHGDIRIAFTPDEEIGKGAQFFDVKAFNAQWAYTVDGGGVGELEYENFNAASVQVKIVGNNVHPGSAKGVMVNALTLASRYHQHVPESESPEQTEGYQGFYHLHSMKGSVERADLHYIVRDFDRNGFEQRKQTMLDIAEKVGAGLHPDCYIEVTITDTYYNMREQVEQHPHIIALAQQAMRDCSIEPNMKPIRGGTDGAHLSFQGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVSVIMRIAELTALRAKP | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45106
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 3.4.11.4
|
P84516 | MSRAPTLAAAAAVAAVVLICSSSTATAADGNARQPPLAPGLSFDFYKRSCPKAESIVRSFVQDAVRRDVGLAAGLLRLHFHDCFVQGCDASVLLDGSATGPGEQQAPPNLTLRPTAFKAINDIHDRLHKECGGTVVSCSDVLALAARDSVVVSGGPSYKVPLGRRDSASFATQQDVLSGLPPPTAAVPALLAVLSKINLDATDLVALSGGHTIGLGHCTSFEDRLFPRPDPTLNATFAGQLRRTCPAKGTDRRTPLDVRTPNAFDNKYYVNLVNREGLFTSDQDLFSNARTRALVDKFARSQRDFFDQFAFSVVKMGQIKVLTGTQGQIRTNCSARNAAGTTMLPWSVSVVEEAADESLGVF | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue (By similarity). Has a high preference for hydroxycinnamates as substrates. Substrate preference is ferulic acid > p-coumaric acid > N-acetyl tyrosine methyl ester > N-acetyl-tyrosine > tyrosine > catechol > Gly-Tyr-Gly. May be involved in the formation of diferulate linkages in the plant cell wall .
PTM: The proportions of glycoforms I and II are 35% and 65% respectively.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 38452
Sequence Length: 362
Subcellular Location: Secreted
EC: 1.11.1.7
|
P86103 | DNTAKEKDSPANLSLRTCAAGDNAEQPLDPSRNTFDNAYYIALQRQAGVLFSDQSLFTSAR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 6665
Sequence Length: 61
Subcellular Location: Secreted
EC: 1.11.1.7
|
P86014 | VSCADILTMATRQFDNVYYKNLQQGK | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 3007
Sequence Length: 26
Subcellular Location: Secreted
EC: 1.11.1.7
|
P25625 | MRLAVVVTLLVHCFLVTCSPGDNLDEFIDCTYACEYNRRCPNSQINYIDPETNMFHDIEFFDTPPLYSKLLFWDCISDCDYQCQHIITRWRIDEEEEIYQFHGKWPFLRVLGTQEFFSTIFSIGNFIPHYKGFVKFSRIIREEGDRRRKNSRSILIWNYLYVTVAGMLAWTASSVFHCRDLIITEKLDYFFAGLTVLTGFHAIFARMTSMFLYPKIAQAFTASVAAIFALHILRLYVDWSYTYNMRFNIFFGVLQYILLIMLSCQNYHALQKQKLMGEFKKTAYSSFKRQIFKLCVIPILLVIVTTMAMSLELFDFFSYEWQIDAHALWHLCTIWPSWVLYDFFLEDYAYWGNRQLY | Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for efficient transport of GPI-anchor proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42541
Sequence Length: 357
Subcellular Location: Endoplasmic reticulum membrane
|
Q42580 | MANAKPFCLLGFFCLLLQLFSIFHIGNGELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVKIIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEMIKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSVGRVHCVNLVHRLYPTIDPTLDPSYALYLKKRCPSPTPDPNAVLYSRNDRETPMVVDNMYYKNIMAHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYVN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 36741
Sequence Length: 327
EC: 1.11.1.7
|
Q7F1U0 | MASATNSSLSLMLLVAAAMASVASAQLSATFYDTSCPNALSTIKSVITAAVNSEARMGASLLRLHFHDCFVQGCDASVLLSGQEQNAGPNVGSLRGFSVIDNAKARVEAICNQTVSCADILAVAARDSVVALGGPSWTVLLGRRDSTTASEALANTDLPAPSSSLAELIGNFSRKGLDATDMVALSGAHTIGQAQCQNFRDRIYNETNIDSAFATQRQANCPRPTGSGDSNLAPLDTTTPNAFDNAYYSNLLSNKGLLHSDQVLFNGGSADNTVRNFASNAAAFSSAFTTAMVKMGNISPLTGTQGQIRLSCSKVNS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: AH2 + H2O2 = A + 2 H2O
Sequence Mass (Da): 32890
Sequence Length: 317
Subcellular Location: Secreted
EC: 1.11.1.-
|
Q9ZV04 | MANKSLEIRFLFPLVLFLVVKLLCVDGKGFNNNGHKIRKGRWEGKLKMNFYHNSCPGAEDIVRQIVWKKVEANRSLAPKLLRVHYHDCFVRGCDASLLLDSVAGKAVSEKEARPNLSLSGFEIIDEIKYILEKRCPNTVSCADILTLAARDAVSYEFERPLWNVFTGRVDGRVSLATEAARDLPSAGANFTTLQKLFAESDLDVVDLVALSGAHTIGIAHCGVFGRRLLNFTGKGDTDPSLNPSYASFLKSECSDKSLRLNPSAVVGMDPTGPLAFDSGYFVSLLKNKGLFTSDAALLTDPSAAHIASVFQNSGAFLAQFGRSMIKMSSIKVLTLGDQGGEIRKNCRLVN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 38237
Sequence Length: 350
Subcellular Location: Secreted
EC: 1.11.1.7
|
O80822 | MGVYLGKYCYIMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAILESDQRLWSDAETNAVVKKYASRLRGLLGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKVN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 35886
Sequence Length: 328
Subcellular Location: Secreted
EC: 1.11.1.7
|
O22862 | MVMIHIFLTVMVVGGVSLFPETAEAIVMGPSMQKLTWHYYKVYNTCENAENFVRHQVEIFYKNDKSIAPKLLRLLYSDCFVSGCDASVLLEGPNSEKMAPQNRGLGGFVLIDKIKIVLEQRCPGVVSCADILNLATRDAVHLAGAPSYPVFTGRRDGLTSDKQTVDLPSPSISWDQAMSYFKSRGLNVLDMATLLGSHSMGRTHCSYVVDRLYNYNKTGKPSPTMNKYFLSEMAKQCPPRTRKGQTDPLVYLNPDSGSNHSFTSSFYSRILSNKSVLEVDQQLLYNDDTKQISKEFSEGFEDFRKSFALSMSKMGAINVLTKTEGEIRKDCRHIN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress (Probable). The enzyme activity has to be proved.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 37568
Sequence Length: 335
Subcellular Location: Secreted
EC: 1.11.1.7
|
Q43735 | MAASKRLVVSCLFLVLLFAQANSQGLKVGFYSKTCPQLEGIVKKVVFDAMNKAPTLGAPLLRMFFHDCFVRGCDGSVLLDKPNNQGEKSAVPNLSLRGFGIIDDSKAALEKVCPGIVSCSDILALVARDAMVALEGPSWEVETGRRDGRVSNINEVNLPSPFDNITKLISDFRSKGLNEKDLVILSGGHTIGMGHCPLLTNRLYNFTGKGDSDPSLDSEYAAKLRKKCKPTDTTTALEMDPGSFKTFDLSYFTLVAKRRGLFQSDAALLDNSKTRAYVLQQIRTHGSMFFNDFGVSMVKMGRTGVLTGKAGEIRKTCRSAN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34950
Sequence Length: 321
Subcellular Location: Secreted
EC: 1.11.1.7
|
Q9SS67 | MKIATFSVLLLLLFIFPVALAQLKFKFYSESCPNAETIVENLVRQQFARDPSITAALTRMHFHDCFVQGCDASLLIDPTTSQLSEKNAGPNFSVRGFELIDEIKTALEAQCPSTVSCSDIVTLATRDAVFLGGGPSYVVPTGRRDGFVSNPEDANEILPPPFISVEGMLSFFGNKGMNVFDSVALLGAHTVGIASCGNFVDRVTNFQGTGLPDPSMDPTLAGRLRNTCAVPGGFAALDQSMPVTPVSFDNLFFGQIRERKGILLIDQLIASDPATSGVVLQYASNNELFKRQFAIAMVKMGAVDVLTGSAGEIRTNCRAFN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34537
Sequence Length: 321
Subcellular Location: Secreted
EC: 1.11.1.7
|
Q9LSP0 | MKPKSKVAESTAASCFLVMSLLCSCIIGDQMETNNEGLSYSYYEKTCPKVEEIVRSSLSSMFILDPTSPAALLRLMFHDCQVQGCDASILLEPIRDQQFTELDSAKNFGIRKRDLVGSIKTSLELECPKQVSCSDVIILAARDAVALTGGPLISVPLGRKDSLSTPSKHVADSELPPSTADVDTTLSLFANKGMTIEESVAIMGAHTIGVTHCNNVLSRFDNANATSENMDPRFQTFLRVACPEFSPTSQAAEATFVPNDQTSVIFDTAYYDDAIAGRGNLRIDSEIGADPRTRPFVEAFAADQDRFFNAFSSAFVKLSSYKVLTGNEGVIRSVCDKVD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 36807
Sequence Length: 339
Subcellular Location: Secreted
EC: 1.11.1.7
|
Q9LV48 | MSTAPSPGTTPSPSPPSPPTNSTTTTPPPAASSPPPTTTPSSPPPSPSTNSTSPPPSSPLPPSLPPPSPPGSLTPPLPQPSPSAPITPSPPSPTTPSNPRSPPSPNQGPPNTPSGSTPRTPSNTKPSPPSDSSDGLSTGVVVGIAIGGVAILVILTLICLLCKKKRRRRHDDEAAYYVPPPPPSGPKAGGPYGGQQQYWQQQNASRPSDNHVVTSLPPPKPPSPPRKPPPPPPPPAFMSSSGGSDYSDLPVLPPPSPGLVLGFSKSTFTYEELSRATNGFSEANLLGQGGFGYVHKGILPSGKEVAVKQLKAGSGQGEREFQAEVEIISRVHHRHLVSLIGYCMAGVQRLLVYEFVPNNNLEFHLHGKGRPTMEWSTRLKIALGSAKGLSYLHEDCNPKIIHRDIKASNILIDFKFEAKVADFGLAKIASDTNTHVSTRVMGTFGYLAPEYAASGKLTEKSDVFSFGVVLLELITGRRPVDANNVYVDDSLVDWARPLLNRASEEGDFEGLADSKMGNEYDREEMARMVACAAACVRHSARRRPRMSQIVRALEGNVSLSDLNEGMRPGHSNVYSSYGGSTDYDTSQYNDDMIKFRKMALGTQEYGTTGEYSNPTSDYGLYPSGSSSEGQATREMEMGKIKKTGQGYSGPSL | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69272
Sequence Length: 652
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LK03 | MSSAPPPGGTPSPPPQPLPIPPPPQPLPVTPPPPPTALPPALPPPPPPTALPPALPPPPPPTTVPPIPPSTPSPPPPLTPSPLPPSPTTPSPPLTPSPTTPSPPLTPSPPPAITPSPPLTPSPLPPSPTTPSPPPPSPSIPSPPLTPSPPPSSPLRPSSPPPPSPATPSTPPRSPPPPSTPTPPPRVGSLSPPPPASPSGGRSPSTPSTTPGSSPPAQSSKELSKGAMVGIAIGGGFVLLVALALIFFLCKKKRRRDNEAPPAPIDGVPYGGQQQQNASRRSDHVVMSVPPPKSPSSAPPRPPHFMSSGSSGDYDSNYSDQSVLPPPSPGLALGLGIYQGTFNYEELSRATNGFSEANLLGQGGFGYVFKGMLRNGKEVAVKQLKEGSSQGEREFQAEVGIISRVHHRHLVALVGYCIADAQRLLVYEFVPNNTLEFHLHGKGRPTMEWSSRLKIAVGSAKGLSYLHENCNPKIIHRDIKASNILIDFKFEAKVADFGLAKIASDTNTHVSTRVMGTFGYLAPEYASSGKLTEKSDVFSFGVVLLELITGRRPIDVNNVHADNSLVDWARPLLNQVSELGNFEVVVDKKLNNEYDKEEMARMVACAAACVRSTAPRRPRMDQVARVLEGNISPSDLNQGITPGHSNVYGSSGGSTDYDSSQDNEGMNKFRKVGLETQDLYSNPISEYDLYPSWSSTDGQTTQGKATGNIKRPGQGYG | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75380
Sequence Length: 717
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q1PEM5 | MARSNRCVPQNSSIVQIPIEEVFKTQLKSRWQQITMSSASSPPPPQVFVPEPLFSEPPPPPKAPVNVSLSPPPPPRSPSTSTPPRLGNRNPPPPASPSGQEPTTPTMTPGFSLSPPSPSRLSTGAVVGISIGGGVFVLTLIFFLCKKKRPRDDKALPAPIGLVLGIHQSTFTYGELARATNKFSEANLLGEGGFGFVYKGILNNGNEVAVKQLKVGSAQGEKEFQAEVNIISQIHHRNLVSLVGYCIAGAQRLLVYEFVPNNTLEFHLHGKGRPTMEWSLRLKIAVSSSKGLSYLHENCNPKIIHRDIKAANILIDFKFEAKVADFGLAKIALDTNTHVSTRVMGTFGYLAPEYAASGKLTEKSDVYSFGVVLLELITGRRPVDANNVYADDSLVDWARPLLVQALEESNFEGLADIKLNNEYDREEMARMVACAAACVRYTARRRPRMDQVVRVLEGNISPSDLNQGITPGHSNTVSVRLDARAVRVKPHGEMDSRWGRFKRTAQRYGGDSL | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56081
Sequence Length: 513
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9ZNQ8 | MASSPESAPPTNSTSSPSPPSNTNSTTSSPPAPSPPSPTPPQGDSSSSPPPDSTSPPAPQAPNPPNSSNNSPSPPSQGGGGERGNGGNNGGNDTPPSRGSPPSPPSRSNGDNGGSRSSPPGDTGGSRSDNPPSSGGSSGGGGGGRSNTNTAIIVGVLVGAGLLMIVLIIVCLRRKKKRKDSFYPEPMKGNQYQYYGNNNNNNASQNYPNWHLNSQGQNQQSTGGWGGGGPSPPPPPRMPTSGEDSSMYSGPSRPVLPPPSPALALGFNKSTFTYQELAAATGGFTDANLLGQGGFGYVHKGVLPSGKEVAVKSLKAGSGQGEREFQAEVDIISRVHHRYLVSLVGYCIADGQRMLVYEFVPNKTLEYHLHGKNLPVMEFSTRLRIALGAAKGLAYLHEDCHPRIIHRDIKSANILLDFNFDAMVADFGLAKLTSDNNTHVSTRVMGTFGYLAPEYASSGKLTEKSDVFSYGVMLLELITGKRPVDNSITMDDTLVDWARPLMARALEDGNFNELADARLEGNYNPQEMARMVTCAAASIRHSGRKRPKMSQIVRALEGEVSLDALNEGVKPGHSNVYGSLGASSDYSQTSYNADMKKFRQIALSSQEFPVSDCEGTSSNDSRDMGTKSPTPPK | Function: Required during abscisic acid (ABA)-mediated activation of Ca(2+) channels. Regulates ABA signaling pathways. Modulates the expression of genes related to cell elongation and ABA signaling during root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 66652
Sequence Length: 633
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q8GX23 | MADSPVDSSPAPETSNGTPPSNGTSPSNESSPPTPPSSPPPSSISAPPPDISASFSPPPAPPTQETSPPTSPSSSPPVVANPSPQTPENPSPPAPEGSTPVTPPAPPQTPSNQSPERPTPPSPGANDDRNRTNGGNNNRDGSTPSPPSSGNRTSGDGGSPSPPRSISPPQNSGDSDSSSGNHPQANIGLIIGVLVGAGLLLLLAVCICICCNRKKKKKSPQVNHMHYYNNNPYGGAPSGNGGYYKGTPQDHVVNMAGQGGGNWGPQQPVSGPHSDASNLTGRTAIPSPQAATLGHNQSTFTYDELSIATEGFAQSNLLGQGGFGYVHKGVLPSGKEVAVKSLKLGSGQGEREFQAEVDIISRVHHRHLVSLVGYCISGGQRLLVYEFIPNNTLEFHLHGKGRPVLDWPTRVKIALGSARGLAYLHEDCHPRIIHRDIKAANILLDFSFETKVADFGLAKLSQDNYTHVSTRVMGTFGYLAPEYASSGKLSDKSDVFSFGVMLLELITGRPPLDLTGEMEDSLVDWARPLCLKAAQDGDYNQLADPRLELNYSHQEMVQMASCAAAAIRHSARRRPKMSQIVRALEGDMSMDDLSEGTRPGQSTYLSPGSVSSEYDASSYTADMKKFKKLALENKEYQSSEYGGTSEYGLNPSASSSEEMNRGSMKRNPQL | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70902
Sequence Length: 670
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LS95 | MAEGQSPENSPPSPTPPSPSSSDNQQQSSPPPSDSSSPSPPAPPPPDDSSNGSPQPPSSDSQSPPSPQGNNNNDGNNGNNNNDNNNNNNGNNNNDNNNGNNKDNNNNGNNNNGNNNNGNDNNGNNNNGNNNDNNNQNNGGGSNNRSPPPPSRNSDRNSPSPPRALAPPRSSGGGSNSSGNNEPNTAAIVGIVAGAGLLFLVMILFCVCCCRKKKKKHQMPYYAGNGYATGKGDQYQQQQYNNQSDHVMNLSQQYPGSNGNNNWMNSPPPPPPGSWQPSPPPPPPPVSGGMNGNSSDFSSNYSGPHGPSVPPPHPSVALGFNKSTFTYDELAAATQGFSQSRLLGQGGFGYVHKGILPNGKEIAVKSLKAGSGQGEREFQAEVDIISRVHHRFLVSLVGYCIAGGQRMLVYEFLPNDTLEFHLHGKSGKVLDWPTRLKIALGSAKGLAYLHEDCHPRIIHRDIKASNILLDESFEAKVADFGLAKLSQDNVTHVSTRIMGTFGYLAPEYASSGKLTDRSDVFSFGVMLLELVTGRRPVDLTGEMEDSLVDWARPICLNAAQDGDYSELVDPRLENQYEPHEMAQMVACAAAAVRHSARRRPKMSQIVRALEGDATLDDLSEGGKAGQSSFLGRGSSSDYDSSTYSADMKKFRKVALDSHEYGASSEYGNTSEYGLDPSSSSSEEIRRGGANNNKTTPSRDH | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74687
Sequence Length: 700
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9XI96 | MAEGQSPENSPPAPPPPSPPSPPSSNDQQTTSPPPSDNQETTSPPPPSSPDIAPPPQQQQESPPPPLPENSSDGSSSSSPPPPSDSSSQSQSPPPPSTSPPQQSDNNGNKGNNNENNKGNDGSSGDGGNKNMSHTPPPPSKTSDHSSHSQPRSLAPPTSNSGSNSSSNDGLNIGAVIGLVAAAGILFIVMILLCVCCFRKKKKKSKLDQMPYYGSNAYPAGKTGGDQYYNQNAATQQQQHYNQNDHIVNLPPPPGSMGTNWVSSPPPPPPGNWQPMPSPPAPVSGGANVIQSGEMSSNFSSGPYAPSLPPPHPSVALGFNNSTFTYEELASATQGFSKDRLLGQGGFGYVHKGILPNGKEIAVKSLKAGSGQGEREFQAEVEIISRVHHRHLVSLVGYCSNAGGQRLLVYEFLPNDTLEFHLHGKSGTVMDWPTRLKIALGSAKGLAYLHEDCHPKIIHRDIKASNILLDHNFEAKVADFGLAKLSQDNNTHVSTRVMGTFGYLAPEYASSGKLTEKSDVFSFGVMLLELITGRGPVDLSGDMEDSLVDWARPLCMRVAQDGEYGELVDPFLEHQYEPYEMARMVACAAAAVRHSGRRRPKMSQIVRTLEGDASLDDLDDGVKPKQSSSGGEGSSDYEMGTYGAEMRKFRKVTLESRDYGASSEYGATSEYGLDPSSSSSEEMHIGGSTSKTTTTNRGI | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74329
Sequence Length: 699
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9FFW5 | MSLVPPLPILSPPSSNSSTTAPPPLQTQPTTPSAPPPVTPPPSPPQSPPPVVSSSPPPPVVSSPPPSSSPPPSPPVITSPPPTVASSPPPPVVIASPPPSTPATTPPAPPQTVSPPPPPDASPSPPAPTTTNPPPKPSPSPPGETPSPPGETPSPPKPSPSTPTPTTTTSPPPPPATSASPPSSNPTDPSTLAPPPTPLPVVPREKPIAKPTGPASNNGNNTLPSSSPGKSEVGTGGIVAIGVIVGLVFLSLFVMGVWFTRKRKRKDPGTFVGYTMPPSAYSSPQGSDVVLFNSRSSAPPKMRSHSGSDYMYASSDSGMVSNQRSWFSYDELSQVTSGFSEKNLLGEGGFGCVYKGVLSDGREVAVKQLKIGGSQGEREFKAEVEIISRVHHRHLVTLVGYCISEQHRLLVYDYVPNNTLHYHLHAPGRPVMTWETRVRVAAGAARGIAYLHEDCHPRIIHRDIKSSNILLDNSFEALVADFGLAKIAQELDLNTHVSTRVMGTFGYMAPEYATSGKLSEKADVYSYGVILLELITGRKPVDTSQPLGDESLVEWARPLLGQAIENEEFDELVDPRLGKNFIPGEMFRMVEAAAACVRHSAAKRPKMSQVVRALDTLEEATDITNGMRPGQSQVFDSRQQSAQIRMFQRMAFGSQDYSSDFFDRSQSHSSWGSRDQSRFVP | Function: Could be involved in the negative regulation of root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72390
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9SX31 | MATTPVQPPVSNSPPVTSPPPPLNNATSPATPPPVTSPLPPSAPPPNRAPPPPPPVTTSPPPVANGAPPPPLPKPPESSSPPPQPVIPSPPPSTSPPPQPVIPSPPPSASPPPALVPPLPSSPPPPASVPPPRPSPSPPILVRSPPPSVRPIQSPPPPPSDRPTQSPPPPSPPSPPSERPTQSPPSPPSERPTQSPPPPSPPSPPSDRPSQSPPPPPEDTKPQPPRRSPNSPPPTFSSPPRSPPEILVPGSNNPSQNNPTLRPPLDAPNSTNNSGIGTGAVVGISVAVALVVFTLFGIFVWCLRKREKRLSAVSGGDVTPSPMSSTARSDSAFFRMQSSAPVGASKRSGSYQSQSGGLGNSKALFSYEELVKATNGFSQENLLGEGGFGCVYKGILPDGRVVAVKQLKIGGGQGDREFKAEVETLSRIHHRHLVSIVGHCISGDRRLLIYDYVSNNDLYFHLHGEKSVLDWATRVKIAAGAARGLAYLHEDCHPRIIHRDIKSSNILLEDNFDARVSDFGLARLALDCNTHITTRVIGTFGYMAPEYASSGKLTEKSDVFSFGVVLLELITGRKPVDTSQPLGDESLVEWARPLISHAIETEEFDSLADPKLGGNYVESEMFRMIEAAGACVRHLATKRPRMGQIVRAFESLAAEDLTNGMRLGESEVFNSAQQSAEIRLFRRMAFGSQNYSTDFFSHSSYNSRDANV | Function: Could be involved in the negative regulation of root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75128
Sequence Length: 708
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
A0A452E9Y6 | MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKLLDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHVTKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism . Shows antibacterial properties against several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species . Inhibits the growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor . Does not have anti-fungal activity towards C.albicans and Pythium species . May protect the udder from infection and may promote growth in newborns . May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 80366
Sequence Length: 712
Subcellular Location: Secreted
EC: 1.11.1.7
|
P22079 | MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDENYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism . Shows antibacterial properties against Pseudomonas aeruginosa . The lactoperoxidase-SCN(-)-H2O2 system shows antibacterial properties against Burkholderia cepacia and Haemophilus influenzae in vitro . Present in mammary and salivary gland secretions and may contribute to airway host defense against infection . May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 80288
Sequence Length: 712
Subcellular Location: Secreted
EC: 1.11.1.7
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.