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stringlengths 6
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O14344 | MSAFKPYTEALEVLKKYEKKDGLSIDDLIRHNFQGGLTFNDFLILPGYIDFVPNNVSLETRISRNIVLKTPFMSSPMDTVTEDQMAIYMALLGGIGVIHHNCTPEEQAAMVRKVKKYENGFILDPVVFSPQHTVGDVLKIKETKGFSGIPITENGKLRGKLVGIVTSRDVQFHKDTNTPVTEVMTPREELITTAEGISLERANEMLRKSKKGKLPVVDKDDNLVALLSLTDLMKNLHFPLASKTSDTKQLMVAAAIGTRDDDRTRLALLAEAGLDAVVIDSSQGNSCFQIEMIKWIKKTYPKIDVIAGNVVTREQTASLIAAGADGLRVGMGSGSACITQEVMACGRPQATAIAQVAEFASQFGIGVIADGGIQNVGHMVKSLSLGATAVMMGGLLAGTTESPGEYYVREGQRYKSYRGMGSIAAMEGTGVNKNASTGRYFSENDAVRVAQGVSGLVVDKGSLLRFLPYLYTGLQHALQDIGTKSLDELHEAVDKHEVRFELRSSAAIREGDIQGFATYEKRLY | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 57026
Sequence Length: 524
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.205
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Q4L385 | MWENKFAKESLTFDDVLLIPAASDVLPNDADLSVELSERIKLNIPVISAGMDTVTESKMAIAMARQGGLGVIHKNMGIEEQAEEVQKVKRSENGVITNPFYLTPDESVYEAEALMGKYRISGVPIVSDKESRELVGILTNRDLRFIEDFSIKISDVMTKENLITAPVGTTLDEAETILQEHKIEKLPLVENGRLEGLITIKDIEKVLEFPHAAKDAHGRLLAAAAIGTSKDTEIRAQKLVEAGVDALIIDTAHGHSSGVIQEVKKMKEKYPEITIVAGNVATAEATRALFEAGADVVKVGIGPGSICTTRVVAGVGVPQITAIYDCATEARKFGKAIIADGGIKFSGDIIKALAAGGHAVMLGSLLAGTEESPGATEVFQGRQYKVYRGMGSLGAMEKGSNDRYFQEDKTPRKFVPEGIEGRTAYKGPLQDTIYQLMGGVRAGMGYTGSPDLKTLRDEAQFTRMGPAGLAESHPHNVQITKESPNYSF | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Mass (Da): 52577
Sequence Length: 488
Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
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P05701 | MMNEHSIDTDNRKANNALYLFIIIGLIPLLCIFVVYYKTPDALLLRKIATSTENLPSITSSYNPLMTKVMDIYCKTAPFLALILYILTFKIRKLINNTDRNTVLRSCLLSPLVYAAIVYLFCFRNFELTTAGRPVRLMATNDATLLLFYIGLYSIIFFTTYITLFTPVTAFKLLKKRQ | Function: This protein is able to protect a cell, which harbors the plasmid ColA encoding colicin A, against colicin A.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20464
Sequence Length: 178
Subcellular Location: Cell inner membrane
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P22426 | MTSNKDKNKKANEILYAFSIIGIIPLMAILILRINDPYSQVLYYLYNKVAFLPSITSLHDPVMTTLMSNYNKTAPVMGILVFLCTYKTREIIKPVTRKLVVQSCFWGPVFYAILIYITLFYNLELTTAGGFFKLLSHNVITLFILYCSIYFTVLTMTYAILLMPLLVIKYFKGRQ | Function: This protein is able to protect a cell, which harbors the plasmid ColB encoding colicin B, against colicin B.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20186
Sequence Length: 175
Subcellular Location: Cell inner membrane
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P08701 | MNRKYYFNNMWWGWVTGGYMLYMSWDYEFKYRLLFWCISLCGMVLYPVAKWYIEDTALKFTRPDFWNSGFFADTPGKMGLLAVYTGTVFILSLPLSMIYILSVIIKRLSVR | Function: This protein is able to protect a cell, which harbors the plasmid ColIa-CA53 encoding colicin Ia, against colicin Ia.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13283
Sequence Length: 111
Subcellular Location: Cell membrane
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P08702 | MKLDISVKYLLKSLIPILIILTVFYLGWKDNQENARMFYAFIGCIISAITFPFSMRIIQKMVIRFTGKEFWQKDFFTNPVGGSLTAIFELFCFVISVPVVAIYLIFILCKALSGK | Function: This protein is able to protect a cell, which harbors the plasmid IncI1 ColIb-P9 encoding colicin Ib, against colicin Ib.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13219
Sequence Length: 115
Subcellular Location: Cell membrane
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P29681 | MKPVALILVFLAISQARVLNLPKEAIDIPVAIVEDKEPPVALSLVKEEVKAEEVKPEEVKPIAQEEKAKDLKEEVKPEIKPEIKEQPKPDIKDEIKEDLKADIKEELKEKIEEQINELPNAKPLELKEKSLEAEEKPQEIKEEVQQPEIKKEATEIKEEPAQNILKSLPAEETVVVPAEELSPNPVEQEQSENQDAAHPQVRQATQATPTQQSTTQGNFVQQLIQNSPIGQFLNQFQPQPAAAAAPAAAQVQADDAAAAAPATPAPTVPGFLNPQAAITSAQQAVQNAAQSAVNATTQAFQGIQQFASNLGNQFQNTLSSLTGQQQQAVSTTPRPPGPIQQFVNNVFGGNNNATAAAPPAQQSGNPLQGIINFLGGNRPQNAPAAAPATQATEKPAVDDKIDPANDEVGEFVPESDNELRASGENIDDSFEDAGVPSNEVIVVNDDAGEEGNAVQNHPVATDAVAL | Function: Probably has an essential role in embryogenesis, induces morphogenesis of imaginal disks, and may participate in multimolecular aggregates.
Sequence Mass (Da): 49809
Sequence Length: 466
Domain: The regions 203-253, 256-333 and 335-377 are thought to contain either alpha helical or beta pleated sheet motifs.
Subcellular Location: Secreted
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Q8JIR8 | MHLKTGLIFLAICLALQVQGSREIPSKTNHGEAKQLADASGSDKTERTTKRSRVSTIRRIFDMAKHRTKRSPFFSTGVKICPQESVKQILASHQAYYRLRVCQEAVWEAFRIFLDRIPDTSEYQNWVTACQRETFCIFDIGKNFSNSQEHLEIIQRRVKHRTFQERKDEISTDKTGGKKLEDIPSVSTGPPSASLSTYTLVPNGTLLNEIVNETKTPVKELGTNTVPELPAEQMVEFSVTLTDQEYTAELSDPNSPQYRQLAAKFQLQMQKIFEKLPGFKEIHVLGFKQKKEKDGSSSTIARYMVNFERDGSEIKSTADDISTIGSNKVENEKVPLSAKEEREISATKLTVTDLQQLVATALHEDRSLPVDLGTLRFTDEPIKPSSDFDNDIQGMVTIPLAGPDLDDTISAELPLVYPSPITVDQTRDIFVDEFTTGITDLSREIGGPEDFDSNFITSEPAFPTKPSREPPHDRSPDTEDITTDYQRFTVPFSALVSTDSPAKPEDSYLPPPADESDSNDLITDESPTEQVITPAVYTTGSFTLPTFLQATDKDTEAEMKKELVGVTEPLFKEADRDSLSGQAVKMMDELESSGDDILVTTSTYKTLPFLIGSSDLFATQPEVTFAAALPPDQTLLPTVTSPFYSHSVVIDQSPEVPDTLMPAAASALPDRASTGVQDIAAELDGAGVKSTAVLDEAEHGSGYISVQTTEPAEVTQAPTLKYVTTSSMTTAAKGKELVVFFSLRVTNMHFSDDLFNRSSQEYKALEQQFMQLLLPYLQSNLTGFKQLEILNFRNGSVIVNSKMKFARTVPYNITEAVHCVLEDFCDAAAQHLNLEIDSYSLDIEPADQADPCKFMACDEFSKCIMNEWTKEADCLCKPGYASQDGLPCRSLCEMEPHLCDNGGKCELVPGRGAVCRSPDQFTEPGLTS | Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein . May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix (By similarity).
PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic acid).
Sequence Mass (Da): 102684
Sequence Length: 928
Subcellular Location: Cell projection
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Q17R60 | MYLETRRAIFVFWIFLQVQGTKDISINIYHSETKDIDNPPRNETTESTEKMYKMSTMRRIFDLAKHRTKRSAFFPTGVKVCPQESMKQILDSLQAYYRLRVCQEAVWEAYRIFLDRIPDTGEYQDWVSICQQETFCLFDIGKNFSNSQEHLDLLQQRIKQRSFPDRKDEISAEKTLGEPGETIVISTDVANVSLGPFPLTPDDTLLNEILDNTLNDTKMPTTERETEFAVLEEQRVELSVSLVNQKFKAELADSQSPYYQELAGKSQLQMQKIFKKLPGFKKIHVLGFRPKKEKDGSSSTEMQLTAIFKRHSAEAKSPASDLLSFDSNKIESEEVYHGTMEEDKQPEIYLTATDLKRLISKALEEEQSLDVGTIQFTDEIAGSLPAFGPDTQSELPTSFAVITEDATLSPELPPVEPQLETVDGAEHGLPDTSWSPPAMASTSLSEAPPFFMASSIFSLTDQGTTDTMATDQTMLVPGLTIPTSDYSAISQLALGISHPPASSDDSRSSAGGEDMVRHLDEMDLSDTPAPSEVPELSEYVSVPDHFLEDTTPVSALQYITTSSMTIAPKGRELVVFFSLRVANMAFSNDLFNKSSLEYRALEQQFTQLLVPYLRSNLTGFKQLEILNFRNGSVIVNSKMKFAKSVPYNLTKAVHGVLEDFRSAAAQQLHLEIDSYSLNIEPADQADPCKFLACGEFAQCVKNERTEEAECRCKPGYDSQGSLDGLEPGLCGPGTKECEVLQGKGAPCRLPDHSENQAYKTSVKKFQNQQNNKVISKRNSELLTVEYEEFNHQDWEGN | Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein (By similarity). May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 89387
Sequence Length: 797
Subcellular Location: Cell projection
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Q94F00 | MGRSLIFSGNMSLRISHLPRSSLPLQNPISGRTVNRTFRYRCTRILSNSFKSTTRLQTKAVLSEVSDQTRYPRIGAKTTGTISPAHLLEVVELAAKTGAEVVMEAVNKPRNITYKGLSDLVTDTDKASEAAILEVVKKNFSDHLILGEEGGIIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLYRGNPAAASVVEFVGGPMCWNTRTFSATAGGGALCNGQKIHVSKTDAVERALLITGFGYEHDDAWSTNMELFKEFTDVSRGVRRLGAAAVDMCHVALGIAESYWEYRLKPWDMAAGVLIVEEAGGAVTRMDGGKFSVFDRSVLVSNGVLHPKLLERIAPATENLKSKGIDFSLWFKPEDYHTEL | Function: Phosphatase acting preferentially on D-myoinositol 1-phosphate (D-Ins 1-P).
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 40445
Sequence Length: 371
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
Subcellular Location: Plastid
EC: 3.1.3.25
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P83891 | XVGDLKTPAILRVTNAYLFN | Function: Binds DNA.
PTM: Phosphorylated.
Sequence Mass (Da): 2217
Sequence Length: 20
Subcellular Location: Cytoplasm
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P9WJ98 | MVPAGLCAYRDLRRKRARKWGDTVTQPDDPRRVGVIVELIDHTIAIAKLNERGDLVQRLTRARQRITDPQVRVVIAGLLKQGKSQLLNSLLNLPAARVGDDEATVVITVVSYSAQPSARLVLAAGPDGTTAAVDIPVDDISTDVRRAPHAGGREVLRVEVGAPSPLLRGGLAFIDTPGVGGLGQPHLSATLGLLPEADAVLVVSDTSQEFTEPEMWFVRQAHQICPVGAVVATKTDLYPRWREIVNANAAHLQRARVPMPIIAVSSLLRSHAVTLNDKELNEESNFPAIVKFLSEQVLSRATERVRAGVLGEIRSATEQLAVSLGSELSVVNDPNLRDRLASDLERRKREAQQAVQQTALWQQVLGDGFNDLTADVDHDLRTRFRTVTEDAERQIDSCDPTAHWAEIGNDVENAIATAVGDNFVWAYQRSEALADDVARSFADAGLDSVLSAELSPHVMGTDFGRLKALGRMESKPLRRGHKMIIGMRGSYGGVVMIGMLSSVVGLGLFNPLSVGAGLILGRMAYKEDKQNRLLRVRSEAKANVRRFVDDISFVVSKQSRDRLKMIQRLLRDHYREIAEEITRSLTESLQATIAAAQVAETERDNRIRELQRQLGILSQVNDNLAGLEPTLTPRASLGRA | Function: Participates in the development of tolerance to both isoniazid and ethambutol. May function through a MDR-pump like mechanism, although it does not appear to directly transport isoniazid from the cell (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70083
Sequence Length: 640
Subcellular Location: Cell membrane
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F1QR98 | MLCLQESGDCLRDQMRYMMRSLQDLKHLRRSCVAPPVGPPVRLRACKQLIAQRERRARLRISDASEASSYDSACCLSSSLEEEESASDPSAVSSPSSERSLEFDSGYSEASWQDEGVVLRRTKNIRVSSTACLRTNQLSNTRARPKSTSDACLESWTSFETASDPEDWTTSLLTRGRNRQPLVLGDNSFADLIHNWMDLPECPEQTELKHSSGRSFAKDFLVNIKRRIAGFSRSADGRRKSSDVTKLSKSIVPTKRLSCQIDVQHKMPFFYKSHTGLNELDTDYYQFSALMKSGSRTPIVCNDIIGYI | Function: Inhibitor of the serine/threonine-protein kinase pak4/pak5 (By similarity). Acts by binding pak4/pak5 in a substrate-like manner, inhibiting the protein kinase activity (By similarity). Required for the proper migration of neural crest cells during embryonic development, probably by inhibiting pak4/pak5 .
Sequence Mass (Da): 34700
Sequence Length: 308
Domain: Contains 2 Inka boxes (also named iBox or inca box). The Inka boxes bind and inhibit PAK4 by binding a substrate-like manner.
Subcellular Location: Nucleus
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F1QPR4 | MLCVRNSGECFRDHMRHMMRSLQDLKQIREPDDQSKCSYVTRARQKRIKQREQLSRLRISDVSDTSTYDSACCLASPLEEEEDQENHAERLAQGSPSSIKSLDFDSGYSEASWQDEGVVLRRTRNVRVSSSACVRTNRIRPKSTSDACLERWTSFEASDPTDWTTSLLTRGRNRQPLVLGDNSFADLIKNWMDLPECPDSAELKPSRKTAFLVNMRRKIAGISKGLEERRSAEAKRMSCPVGFQPPKPFFHQSHTSLHPMGTDFYQFSSVMKSGSRQPIICNDVIGYI | Function: Inhibitor of the serine/threonine-protein kinase pak4/pak5. Acts by binding pak4/pak5 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 32880
Sequence Length: 288
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner.
Subcellular Location: Nucleus
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Q96EL1 | MDMHSARLDSFLSQLRWELLCGRDTGSPSMPGPLQPTSQTGPDVQPSHQLRASGALEEDSVCCVEEEEEEEEEAVVTEDRDAALGGPREHALDWDSGFSEVSGSTWREEELPVSQRPAPSAQPLRRQCLSVSGLPMPSRAPVASVPPVHHPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPETGSEGGDGGGHRARARPPQFLLGLSEQLRRRLARARRTAMAGKRLSCPPRPEPELPADVSRFAALMSCRSRQPIICNDVSYL | Function: Inhibitor of the serine/threonine-protein kinase PAK4 . Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity .
Sequence Mass (Da): 31574
Sequence Length: 287
Domain: Contains 2 Inka boxes (also named iBox or inca box) . The Inka boxes bind and inhibit PAK4 by binding a substrate-like manner .
Subcellular Location: Nucleus
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Q9CX62 | MHSARLDSFLSQLRWELLCARDTGSPPMSGPLQPKPRTDQNVQPKRQFRASDVLEEDSVCCVEEEEEEGLVAEDKGLPLGCPREHALDWDSGFSEVSGSTWREEEPSVPQRQAPRERPPHSQRFSVSDIPMRSRAAVTNIPPAHRPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPEATSEGSDGDVPRARARPPQFLLGLSEQLRRRLARARRTAMASKRLSCPPRSEPDLPADISRFAALMNCRSRQPIIYNDVSYL | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 31804
Sequence Length: 282
Domain: Contains 2 Inka boxes (also named iBox or inca box). The Inka boxes bind and inhibit PAK4 by binding a substrate-like manner.
Subcellular Location: Nucleus
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Q9NTI7 | MTMESREMDCYLRRLKQELMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALEQLEISGGGPVPGSPEGPRTQCEHPCWEGGRGPARPTVCSPSSQPSLGSSTKFPSHRSVCGRDLAPLPRTQPHQSCAQQGPERVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDLPELEKGGEKGETGGAREPKGEKGQPQELGRRFALTANIFKKFLRSVRPDRDRLLKEKPGWVTPMVPESRTGRSQKVKKRSLSKGSGHFPFPGTGEHRRGENPPTSCPKALEHSPSGFDINTAVWV | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 32759
Sequence Length: 297
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner.
Subcellular Location: Nucleus
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Q80VY2 | MTKESKDMDCYLRRLKQELMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALEQLEISGGTPTFSCPESSQEQPECPRWQGSGGPAGPAAWTSSSQPSFDSSPKLPCRRSVCGKELAVLPKTQLPEEHQSCTQQGTEWVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDLPELEKGGEKGETGGSIEPKGEKGQSRELGRKFALTANIFRKFLRSVRPDRDRLLKEKPGWMTPMVSESRAGRSKKVKKRSLSKGSGRFPFSSTGEPRHIETPATSSPKALEPSCRGFDINTAVWV | Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Sequence Mass (Da): 33233
Sequence Length: 300
Domain: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner.
Subcellular Location: Nucleus
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P0DJM0 | MRKKRYVWLKSILVAILVFGSGVWINTSNGTNAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFYNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLNDQAWTNAPVNYKANVSIPNTVKNVTGALIAPATISDGGSYTEPDITWNLPSYTNEVSYTFSQPVTIGKGTTTFSGTVTQPLKAIFNVKFHVDGKETTKEVEAGNLLTEPAKPVKEGHTFVGWFDAQTGGTKWNFSTDKMPTNDINLYAQFSINSYTATFDNDGVTTSQTVDYQGLLQEPTAPTKEGYTFKGWYDAKTGGDKWDFATSKMPAKNITLYAQYSANSYTATFDVDGKSTTQAVDYQGLLKEPKAPTKAGYTFKGWYDEKTDGKKWDFATDKMPANDITLYAQFTKNPVAPPTTGGNTPPTTNNGGNTTPPSANIPGSDTSNTSTGNSASTTSTMNAYDPYNSKEASLPTTGDSDNALYLLLGLLAVGTAMALTKKARASK | Function: Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells . Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin-2 function as receptors . Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA .
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 86493
Sequence Length: 800
Domain: Consists of an N-terminal cap, a leucine-rich repeat domain (LRR), and an Ig-like interrepeat domain.
Subcellular Location: Secreted
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P0DQD3 | MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVSTPIKQIFPDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLTNLKNLGWLFLDENKIKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLKEVYTVSYDVDGTVIKTKVEAGTRITAPKPPTKQGYVFKGWYTEKNGGHEWNFNTDYMSGNDFTLYAVFKAETTEKTVNLTRYVKYIRGNAGIYKLPREDNSLKQGTLASHRCKALTVDREARNGGKLWYRLKNIGWTKAENLSLDRYDKMEYDKGVTAYARVRNASGNSVWTKPYNTAGAKHVNKLSVYQGKNMRILREAKTPITTWYQFSIGGKVIGWVDTRALNTFYKQSMEKPTRLTRYVSANKAGESYYKVPVADNPVKRGTLAKYKNQKLIVDCQATIEGQLWYRIRTSSTFIGWTKAANLRAQK | Cofactor: Binds 2 Ca(2+) ions; binding site 1 has a 10-fold higher affinity binding site 2 . Loss of Ca(2+)-binding has no measurable effect on host receptor activation or invasion by Listeria, suggesting ion-binding is fortuitous .
Function: Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells (Probable) . Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB in human, green monkey, mouse and dog cell lines . Downstream adapter proteins GAB1 and CBL are phosphorylated in response to InlB, which also causes cell colony scattering . InlB binding to mammalian cells is saturable and inhibited by EDTA; InlB-coated beads can be taken up by host cells . Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) might act as an InlB receptor, leading to activation of PI3-kinase in green monkey cells . Stimulation of Tyr-phosphorylation by InlB is antagonized by C1QBP, showing that potentiation of MET signaling via the GW domains is not mediated by C1QBP; the exact role of C1QBP remains to be determined . Stimulation of Tyr-phosphorylation of MET by InlB is potentiated by the InlB GW domains and glycosaminoglycans such as heparin; exogenously added InlB, or hepatocyte growth factor (HGF) will also substitute for bacterial InlB, suggesting InlB promotes bacterial invasion by mimicking the hormone HGF . May stimulate phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3-kinase) in green monkey cells, has less effect in humans as PI3-kinase is constitutively and highly expressed in Caco cells (Probable). Binds heparin; C1QBP and heparin seem to bind to the GW domains .
Sequence Mass (Da): 71221
Sequence Length: 630
Domain: Has an N-terminal region with 8 leucine-rich repeats (LRR) and has 3 GW repeats in the C-terminus (Probable). Residues 241-319 form an Ig-like region, followed by a 72 residue-long flexible B repeat region (Probable). The GW repeats mediate non-covalent binding of the protein to lipoteichoic acid (LTA) on the bacterial membrane . The GW domain mediates binding to host complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) and to heparin; heparin binding dissociates InlB from the bacterial surface . The LRR domain forms a curved tube, the N-terminus of which has a cap that binds 2 Ca(2+) ions . The LRR domain alone (31-241) binds mammalian MET and stimulates its Tyr-phosphorylation; the LRR plus Ig-like region (31-321) are required for receptor dimerization, and the GW domains, especially GW2 and GW3, potentiate MET activation .
Subcellular Location: Secreted
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P71451 | MLKKNNWLQNAVIAMLVLIVGLCINMGSGTKVQAESIQRPTPINQVFPDPGLANAVKQNLGKQSVTDLVSQKELSGVQNFNGDNSNIQSLAGMQFFTNLKELHLSHNQISDLSPLKDLTKLEELSVNRNRLKNLNGIPSACLSRLFLDNNELRDTDSLIHLKNLEILSIRNNKLKSIVMLGFLSKLEVLDLHGNEITNTGGLTRLKKVNWIDLTGQKCVNEPVKYQPELYITNTVKDPDGRWISPYYISNGGSYVDGCVLWELPVYTDEVSYKFSEYINVGETEAIFDGTVTQPIKN | Function: A virulence enhancer that has at least 2 dissociable functions in infection; it impairs translocation of host transcription factor NF-kappa-B to the nucleus and antagonizes the function of the Tuba dynamin-binding protein, promoting bacterial spreading . Perturbs the morphology of host cell junctions by impairing host DNMBP (Tuba) and WASL interaction, altering cortical tension at the cell junctions and allowing bacteria to more efficiently form bacteria-filled cell protrusions which promote bacterial spreading within infected host tissue . Down-regulates the host inflammation response usually induced by Listeria infection. Interacts with host I-kappa-B kinase alpha (IKKA, CHUK), which prevents IKKA from phosphorylating NF-kappa-B inhibitor alpha (IKBA, NFKBIA) and thus delays degradation of phospho-IKBA. Translocation of host transcription factor p65 (a subunit of NF-kappa-B, RELA) into the nucleus is impaired, which prevents activation of NF-KB-regulated genes . Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis .
Sequence Mass (Da): 33192
Sequence Length: 297
Domain: Consists of the cap domain (residues 35-76) and LRR repeat region (77-213) and an Ig-like region (207-297), where the latter 2 overlap slightly . The LRR repear region interacts via its concave face with host DNMBP (Tuba) .
Subcellular Location: Secreted
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Q5B7I9 | MEKTQTPSLTPDELSARSSTPFEEREEEEEVHYVGHLKFSFIFVGLCLSVFQVALSLQDIGWYGSAYLFTDCAFQLVFGRLYSMLPVKIVYLGALLLFEIGSIICATAPNSIALILGRTIAGIGAGGILSGALTILSQSVPRAKVAVFNGILGAVNGIAFICGPLLAGGIINGTTWRWIFYINPIISAPTFFITVFLLKLDPPKTNVKTWRGRIAMLDLPAFTLFLGSILCLILALLWGGKEYSWKNARIIVLFILFGVIMLAFMLVQKRKGDDALVPMRILCQRSIAFGMFFSFCTSGTGFILEYYLPIWLQVIKDLSVISSAVKLLPIIAAAVVFTTLCGILTPVIGHYVPFMIIATMLLSVGMGLLSTLEYTSPIRHVLGFQVPAGVGLGCALQQTLVAAQTILPMNDIPIGVSLIVLAQTLGGTIALSAADTIYTGTLSSSISSRFPQINRETVLTTGNREIRNLVPAESLSVIMDLCNKAIVKTWYLSIGLAAASIIGVLGMEWRRVTPPKK | Function: MFS efflux transporter; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB . The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB . The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu . Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B . InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA . The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides . The MFS efflux transporter inpD may contribute to fellutamide resistance as well .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56019
Sequence Length: 517
Subcellular Location: Cell membrane
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Q5B7I7 | MAKETRFYPYTSNGGATLGVSGPDFAILAGDTRSTAGYNINTRYEPKVFTIQDARDRSIVISVIGFAADGRALKERLDAIVAMYKYQHGKNIGLRACAQRVSTMLYEKRFFPYQLQTMVAGIDADGQGAIYYYDPAGCIEKRSHCAAGEASSLMLPFLDSQAPRLQPLSLQTAQQLVRDAYTGATERHIEVGDHLQMLVVTREGVSEQLVDLKKD | Function: Proteasome subunit beta type-6; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB . The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB . The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu . Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B . InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA . The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides . The MFS efflux transporter inpD may contribute to fellutamide resistance as well .
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23725
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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Q5B7I6 | MRILFFHGHTQTGPVFERKTVRLREHIQRAYPGSTFFFPTGPIAYKVSDRLDYLSEIQRERSDNFKDPDLIETHAWFRLFEDDPPRGLLESLDIAAEILRVEGPFDGVICFSQGSVVGSMMASLLEGPRRRQRFDEYAASFPGAVRYPKSYKNINHPPLKFGITYGAYMGTSPVFNAFYSEPLIETPFLHFMGEFDPVVPSEMVAAVDKAQIGGSRRRKVMHPGAHAIPVGDRYHEAVVDFIRSACETSPTYFDLPSDEVPLLSYNDTPEQTPFQTPLLTPSLSSAVSTTSIPSSEATILATRRLDQWEKSRSPRSNIRPRSTRRTVFSGRRSTSSSAESSAASQHSDHFEATRTPTSSTSTVQMIEPTVNKEPNLAVRVVEDDTIVSGSEYEGEGWQELLLSDLLNEMLRRHGRPGRFYFVPDGEGGRLENGMRLN | Function: Esterase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB . The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB . The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu . Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B . InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA . The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides . The MFS efflux transporter inpD may contribute to fellutamide resistance as well .
Sequence Mass (Da): 49125
Sequence Length: 437
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.2.-
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P21327 | MSDILQELLRVSEKAANIARACRQQETLFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKENMENKFPGLGKKIFGEESNEFTNDLGEKIIMRLGPTEEETVALLSKVLNGNKLASEALAKVVHQDVFFSDPALDSVEINIPQDILGIWVDPIDSTYQYIKGSADITPNQGIFPSGLQCVTVLIGVYDIQTGVPLMGVINQPFVSQDLHTRRWKGQCYWGLSYLGTNIHSLLPPVSTRSNSEAQSQGTQNPSSEGSCRFSVVISTSEKETIKGALSHVCGERIFRAAGAGYKSLCVILGLADIYIFSEDTTFKWDSCAAHAILRAMGGGMVDLKECLERNPDTGLDLPQLVYHVGNEGAAGVDQWANKGGLIAYRSEKQLETFLSRLLQHLAPVATHT | Function: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Sequence Mass (Da): 43965
Sequence Length: 400
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
EC: 3.1.3.57
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C4M633 | MQTSLFEFANVLITAVKEASYSISKFKEEVEIKYKSDGSEVTQVDTQSQQIIFSIIKNKYPTINIIGEEDVENGIPDNQLPTITQLSFGSLENKIININDIIIYVDPLDGTDCYTHKQYDSVCVLVGVTYKGKPMIGIVSKPFYNNEITFAIENYISSISLQPLNDKIIFVCSKKNDIQHLIKSFPDPYEVKYKGGSGAKMMAIIHQEADIYYHPLIQSCTWDTLAAQVILEAQGGIVCDIYGNPLCYPSSKKESMRHKKGVLCLSPRAKKYLPYMLSISKTILL | Cofactor: Binds 3 Mg(2+) per subunit.
Function: Catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate . Is also able to convert 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP but with less efficiency .
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Sequence Mass (Da): 32051
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 3.1.3.57
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P49441 | MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEALARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQCVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRRNGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGAAGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT | Function: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Catalytic Activity: 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Sequence Mass (Da): 43998
Sequence Length: 399
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
EC: 3.1.3.57
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Q8A7J9 | MKRPSFLPVLIGTGFGSGFSPFAPGTAGALLASIIWIALYFLLPFTALLWTTAALVVLFTFAGIWAANKLESCWGEDPSRVVVDEMVGVWIPLLAVPDNDRWYWYVIAAFALFRIFDIVKPLGVRKMENFKGGVGVMMDDVLAGVYSFILIAVARWVIG | Function: May be responsible for the conversion of phosphatidylinositol phosphate diacylglycerol (PIP-DAG) to phosphatidylinositol diacylglycerol (PI-DAG), making it a key enzyme in the inositol glycerophospholipid biosynthesis pathway.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17480
Sequence Length: 159
Subcellular Location: Membrane
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C8AW47 | MSKHAVVQFGVVYALLFPGVFGFVPSPTNVSVVCHNFVNVLYWNYSNPTEQTKFAIKVEPYESPSQTVDTSQTYLDISSYSTDVEDDYLVLLTAHDGQEKSEDVSIRFTYSKDYFDENKHKYKCSLDFPAVNTSVHKDVIEVSFQHPFKLYKQEIMKEEFTYKITHDEQMVKYSCFEDEDLCNAEVHFNQSVAGQCVELKLEGVIAGIPSYTYSNVCVPQPTPETDKTGIIAALIGGATVVLFIIMGFVWLLWRKWSNIPQMPQGLWCIISKQSHTMLLSQPEPTDICPVTSQGPLNYLTEEDQSVSARDDTGADPPVVSEEGMAGEDSQGLGCSSDYDRPKFL | Function: Receptor which shows binding specificity for the cytokine ifng1 (interferon gamma 1).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38670
Sequence Length: 344
Subcellular Location: Cell membrane
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Q9VBB3 | MAANIAAAAAAAQEVDPVLKKAIKLLHSSNPTSAAELRLLLDEALKARFGPEKSLTNNMTPRMLEDEANFSGRAATPPQQPINADEIINLTNSPDKEPSDSVDTIADSDDGLSAVGIVNTGDTGDFGDLNCCVCGEMVFTATNRLIECSKCGAMYHQECHKPPITKEEAADDQEQNWQCDTCCNKPTSSGRTTSSAAAVTPTVFIADEPMPLTSKAKSSVASSRSSNSSNSSSPFYRPEPSSSTNASSSSSSKHGHKSSSSSSSKSHKEERSSKSTAASSLSAIGGMEKHNSSGTSSRRSGSSTKSSSKSSSSKHHESGSSSKRRSKQ | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 . Required for the normal expression of the Integrator complex component IntS1 . May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Sequence Mass (Da): 34334
Sequence Length: 328
Domain: The PHD-type zinc finger is not required for 3'-end snRNA processing.
Subcellular Location: Nucleus
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Q9VEX5 | MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIVSDTAAHIVNTWRPSTQNMAHVMNAMLIVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADFGTDELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPSKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISPLLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGATYETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSLCITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRVVPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLPHFLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLESLQSLRAAYGDAPLKSEPGASLLRTYTESPLSPERLEPISSVGASGSSSSNSLLKASKRRMSSCGQRSLLDIISSAERSQSNKRLDFSGRLCTPLGQVAKLYPDFGTKDKDTVTTGASITPNVKEESVRS | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1 and U5 . Plays a role as a regulator of spermatogenesis . Crucial regulator of the mitotic cell cycle and development . Required for the correct dynein-dynactin perinuclear localization important for nucleus-centrosome coupling that occur upon meiotic progression of primary spermatocytes . Plays a role in sperm motility and fertility . May have a role in the PNG/PLU/GNU pathway .
PTM: Phosphorylated.
Sequence Mass (Da): 75728
Sequence Length: 689
Subcellular Location: Nucleus
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Q39041 | MASSDALLPISAREEEPLCPYTRLPMADPNQETHGPRRRRPFKGLLAVSFGLLFIAFYVALIATHDGSRSNDEGIDETETITSRARLAGVSEKRNDGLWKLSGDRNTPAFEWNNSMLSWQRTAFHFQPEQNWMNDPNGPLFYKGWYHFFYQYNPNAAVWGDIVWGHAVSRDLIHWVHLPIAMVADQWYDSNGVWTGSATFLPDGSIVMLYTGSTDKAVQVQNLAYPEDPNDPLLLKWVKFPGNPVLVPPPGILPKDFRDPTTAWKTSEGKWRITIGSKLNKTGISLVYDTIDFKTYEKLDTLLHRVPNTGMWECVDFYPVSKTAGNGLDTSVNGPDVKHIVKASMDDTRFDHYAVGTYFDSNGTWIPDDPTIDVGMTASLRYDYGKFYASKSFYDQNKGRRVLWSWIGESDSEASDVQKGWSSLQGIPRTVVLDTKTGKNLVQWPVEEIKSLRLSSKQFDLEVGPGSVVPVDVGSAAQLDIEAEFEINKESLDKIIGNASVVAEAEEFSCEKSGGSTVRGALGPFGFSVLATESLSEQTPVYFYVAKGKDSELKTFFCTDTSRSSVANDVVKPIYGSVVPVLKGEKLTMRILVDHSIVEAFGQGGRTCITSRVYPTTAIYGAAKLFLFNNALDATVTASFTVWQMNSAFIHPYSDEAVRALSRT | Function: Possible role in the continued mobilization of sucrose to sink organs . Regulates root elongation .
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 73844
Sequence Length: 664
Domain: The LCPYTRL domain (18-24) is critical for trafficking from the trans-Golgi network to the prevacuolar compartment and from the prevacuolar compartment to the central vacuole . The PRRRRP domain (36-41) is involved in sorting to the vacuole . At least two Arg are needed for correct delivery and the presence of two neighboring Pro seems to contribute to the sorting efficiency .
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Vacuole
EC: 3.2.1.26
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Q9FXA8 | MSAIYLLRKISTKTPSRFHRSLFFSTFSKDSPPDLSRTTSIRHLSSSQRFVSSSIYCFPQSKILPNRFSEKTTGISVRQFSTSVETNLSDKSFERIHVQSDAILERIHKNEEEVETVSIGSEKVVREESEAEKEAWRILENAVVRYCGSPVGTVAANDPGDKMPLNYDQVFIRDFVPSALAFLLKGEGDIVRNFLLHTLQLQSWEKTVDCYSPGQGLMPASFKVRTVALDENTTEEVLDPDFGESAIGRVAPVDSGLWWIILLRAYGKITGDFSLQERIDVQTGIKLIMNLCLADGFDMFPTLLVTDGSCMIDRRMGIHGHPLEIQSLFYSALRCSREMLSVNDSSKDLVRAINNRLSALSFHIREYYWVDIKKINEIYRYKTEEYSTDATNKFNIYPEQIPPWLMDWIPEQGGYLLGNLQPAHMDFRFFTLGNFWSIVSSLATPKQNEAILNLIEAKWDDIIGNMPLKICYPALEYDDWRIITGSDPKNTPWSYHNSGSWPTLLWQFTLACMKMGRPELAEKALAVAEKRLLADRWPEYYDTRSGKFIGKQSRLYQTWTVAGFLTSKLLLANPEMASLLFWEEDYELLDICACGLRKSDRKKCSRVAAKTQILVR | Function: Mitochondrial invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development and floral transition. May generate glucose as a substrate for mitochondria-associated hexokinase, contributing to mitochondrial reactive oxygen species homeostasis.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 70437
Sequence Length: 616
Subcellular Location: Mitochondrion
EC: 3.2.1.26
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P29000 | MATQCYDPENSASRYTLLPDQPDSGHRKSLKIISGIFLSVFLLLSVAFFPILNNQSPDLQIDSRSPAPPSRGVSQGVSDKTFRDVAGASHVSYAWSNAMLSWQRTAYHFQPQKNWMNDPNGPLYHKGWYHLFYQYNPDSAIWGNITWGHAVSKDLIHWLYLPFAMVPDQWYDINGVWTGSATILPDGQIMMLYTGDTDDYVQVQNLAYPANLSDPLLLDWVKFKGNPVLVPPPGIGVKDFRDPTTAWTGPQNGQWLLTIGSKIGKTGVALVYETSNFTSFKLLDGVLHAVPGTGMWECVDFYPVSTKKTNGLDTSYNGPGVKHVLKASLDDNKQDHYAIGTYDLGKNKWTPDNPELDCGIGLRLDYGKYYASKTFYDPKKERRVLWGWIGETDSESADLQKGWASVQSIPRTVLYDKKTGTHLLQWPVEEIESLRVGDPTVKQVDLQPGSIELLRVDSAAELDIEASFEVDKVALQGIIEADHVGFSCSTSGGAASRGILGPFGVIVIADQTLSELTPVYFYISKGADGRAETHFCADQTRSSEAPGVGKQVYGSSVPVLDGEKHSMRLLVDHSIVESFAQGGRTVITSRIYPTKAVNGAARLFVFNNATGASVTASVKIWSLESANIQSFPLQDL | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70097
Sequence Length: 636
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Membrane
EC: 3.2.1.26
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P80065 | MDTYHFLPSRDLEHASSYTPRPDSPETRHEPDPDRSKTNRRPIKIVSSVLLSTLILSFVIFLLVNPNVQQVVRKKVSKNSNGEDRNKASKSPEMLGPPSRGVSQGVSEKSFRQATAEPSYPWTNDMLSWQRTSFHFQPQENWMNDPNGPLFHMGWYHLFYQYNPDSAIWGNITWGHAISRDLINWLHLPFAMQPDQWYDINGVWTGSATVLPDGKIVMLYTGDTDDLVQVQNLAYPANLSDPLLLDWIKYPDNPVMFPPPGIGSTDFRDPTTAWIGRDGKWRITIGSKVNKTGISLMYKTTDFITYELLDNLLHAVPGTGMWECVDFYPVSVTGSNGLDTSVNGPGVKHVLKSSLDDDRHDYYALGTYDPINDKWTPDNPELDVGIGLRLDYGKYYASKTFYDQDKERRLLWGWIGETDSESADLLKGWASVQSIPRTVVFDKKTGTNILQWPVKEVESLRSRSYEIDDVELKPGSLVPLKISSAAQLDIVASFEVDEEAFKGTYEADASYNCTASEGAAGRGILGPFGILVLADDPLSELTPVYFYIAKGVDGNAKTYFCADQSRSSTASDVDKEVYGSDVPVLHGESLSMRLLVDHSIVESFAQGGRTVITSRVYPTRAIYSAARVFLFNNATGVSVTASVKAWQMASATLKPFPFDQL | Function: May participate in the regulation of the hexose level in mature tissues and in the utilization of sucrose stored in vacuoles.
PTM: N-glycosylated; high-mannose and high-xylose complex glycans.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 73864
Sequence Length: 661
Subcellular Location: Membrane
EC: 3.2.1.26
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F8DT27 | MFNFNASRWTRAQAMKVNKFDLTTSMPEIGTDFPIMRDDLWLWDTWPLRDINGNPVSFKGWNVIFSLVADRNIPWNDRHSHARIGYFYSKDGKSWVYGGHLLQESANTRTAEWSGGTIMAPGSRNQVETFFTSTLFDKNGVREAVAAVTKGRIYADSEGVWFKGFDQSTDLFQADGLFYQNYAENNLWNFRDPHVFINPEDGETYALFEANVATVRGEDDIGEDEIGPVPANTVVPKDANLCSASIGIARCLSPDRTEWELLPPLLTAFGVNDQMERPHVIFQNGLTYLFTISHDSTYADGLTGSDGLYGFVSENGIFGPYEPLNGSGLVLGGPASQPTEAYAHYIMNNGLVESFINEIIDPKSGKVIAGGSLAPTVRVELQGHETFATEVFDYGYIPASYAWPVWPFPDRRK | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 46100
Sequence Length: 413
Subcellular Location: Secreted
EC: 3.2.1.26
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P42412 | MAEIRKLKNYINGEWVESKTDQYEDVVNPATKEVLCQVPISTKEDIDYAAQTAAEAFKTWSKVAVPRRARILFNFQQLLSQHKEELAHLITIENGKNTKEALGEVGRGIENVEFAAGAPSLMMGDSLASIATDVEAANYRYPIGVVGGIAPFNFPMMVPCWMFPMAIALGNTFILKPSERTPLLTEKLVELFEKAGLPKGVFNVVYGAHDVVNGILEHPEIKAISFVGSKPVGEYVYKKGSENLKRVQSLTGAKNHTIVLNDANLEDTVTNIVGAAFGSAGERCMACAVVTVEEGIADEFMAKLQEKVADIKIGNGLDDGVFLGPVIREDNKKRTLSYIEKGLEEGARLVCDGRENVSDDGYFVGPTIFDNVTTEMTIWKDEIFAPVLSVIRVKNLKEAIEIANKSEFANGACLFTSNSNAIRYFRENIDAGMLGINLGVPAPMAFFPFSGWKSSFFGTLHANGKDSVDFYTRKKVVTARYPAPDFN | Function: Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively.
Catalytic Activity: 3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH
Sequence Mass (Da): 53453
Sequence Length: 487
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7.
EC: 1.2.1.-
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P42413 | MSYLLRKPQSHEVSNGVKLVHEVTTSNSDLTYVEFKVLDLASGSSYTEELKKQEICIVAVTGKITVTDHESTFENIGTRESVFERKPTDSVYISNDRAFEITAVSDARVALCYSPSEKQLPTKLIKAEDNGIEHRGQFSNKRTVHNILPDSDPSANSLLVVEVYTDSGNWSSYPPHKHDQDNLPEESFLEETYYHELDPGQGFVFQRVYTDDRSIDETMTVGNENVVIVPAGYHPVGVPDGYTSYYLNVMAGPTRKWKFYNDPAHEWILER | Function: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
Catalytic Activity: 5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate
Sequence Mass (Da): 30706
Sequence Length: 271
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 4/7.
EC: 5.3.1.30
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Q5KYR2 | MSRLIIPSHSPNEEGNVVRVTPESVGWEYVGFEVYVLAKGQTLRKETKDQEACLVLLKGKANISTKLERWEQIGLRMDVFEKVPPYSVYVPANDVYEVEAMTDVEVAVCLAPGKGTYPARLIPPSEVGVEIRGAGNIERRVHNILPESQPADSLLVVEVFTPEGNWSSYPPHKHDQDNLPHESYLEETYYHKINPGHGFMVQRVYTDDRSIDETMVVKNGDVVLVPKGYHPVSAPPGYEGYYLNVMAGPVRTWKFHNDPDHDWVMESKLAAKQKEK | Function: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
Catalytic Activity: 5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate
Sequence Mass (Da): 31186
Sequence Length: 276
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 4/7.
EC: 5.3.1.30
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Q9X7U5 | MSELLGVAVLGAGHMGADHIRRVDQVVSGARVAAVADPDAERAKEAVGGIGGTGRITVHTDVEAALDAPGVEAVLIASPGEAHEEALLAAFARGLPVLCEKPMAPNSAGALRVVEAEARLGRRLAQIGFMRRYDAEYRQLKSLLDGGRLGRPLMLHCVHRNVSSPPHFTSAMLINSSVSHEIDAARWLLGQELSAVTVLRPRPSAGAPEGLLDPQLVLFETEGGAVVDVEVFVNCGFGYEVRCEAVCEAGSARIGAAHTMMVTAAGGAREEVPQDYLVRFADAYDREVQSWVDATRRGLVTGPGTWDGYAAAAVAEAGVRALDTGVRTPVDMAPRPSLHDRA | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36020
Sequence Length: 342
EC: 1.1.1.18
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Q9WYP5 | MRIGVIGLGRIGTIHAENLKMIDDAILYAISDVREDRLREMKEKLGVEKAYKDPHELIEDPNVDAVLVCSSTNTHSELVIACAKAKKHVFCEKPLSLNLADVDRMIEETKKADVILFTGFNRRFDRNFKKLKEAVENGTIGKPHVLRITSRDPAPPPLDYIRVSGGIFLDMTIHDFDMARYIMGEEVEEVFADGSVLVDEEIGKAGDVDTAVVVLRFKSGALGVIDNSRRAVYGYDQRIEVFGSKGRIFADNVRETTVVLTDEQGDRGSRYLYFFLERYRDSYLEELKTFIKNVKSGEPPAVSGEDGKMALLLGYAAKKSLEEKRSVKLEEVIG | Function: Catalyzes the NAD(+)-dependent oxidation of myo-inositol (MI) to 2-keto-myo-inositol (scyllo-inosose), and thus probably functions in a myo-inositol degradation pathway together with IolM, IolN and IolO. Has no activity with scyllo-inositol and much reduced activity (78-fold lower catalytic efficiency) with 1D-chiro-inositol.
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 37485
Sequence Length: 334
Pathway: Polyol metabolism; myo-inositol metabolism.
EC: 1.1.1.18
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P42419 | MKLCFNEATTLENSNLKLDLELCEKHGYDYIEIRTMDKLPEYLKDHSLDDLAEYFQTHHIKPLALNALVFFNNRDEKGHNEIITEFKGMMETCKTLGVKYVVAVPLVTEQKIVKEEIKKSSVDVLTELSDIAEPYGVKIALEFVGHPQCTVNTFEQAYEIVNTVNRDNVGLVLDSFHFHAMGSNIESLKQADGKKIFIYHIDDTEDFPIGFLTDEDRVWPGQGAIDLDAHLSALKEIGFSDVVSVELFRPEYYKLTAEEAIQTAKKTTVDVVSKYFSM | Cofactor: Binds 1 divalent metal cation per subunit. Can use Mn(2+), Fe(2+) or Co(2+).
Function: Involved in the reversible interconverion of 2-keto-myo-inositol (2KMI, inosose or 2,4,6/3,5-pentahydroxycyclohexanone) to 1-keto-D-chiro-inositol (1KDCI or 2,3,5/4,6-pentahydroxycyclohexanone).
Catalytic Activity: scyllo-inosose = scyllo-inosine
Sequence Mass (Da): 31656
Sequence Length: 278
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA.
EC: 5.3.99.11
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Q5WKY5 | MGFVPMAPLLADAKKDSYAIGQFNINGLQWAKAILAGAESQQSPVIAAASDRLIDYLGGFQTVVAMMGALTDELGITVPVVLHLDHGLSIERCKKAVDAGFSSVMFDGSHYPINENIDMTKEVVAYAHAHNVSVEGEVGTVGGMEDGLMAEIKYADVEECQRFVCETNVDALAAALGSVHGKYKGEPKLGFNEMAAISASTNVPLVLHGASGIPDEQLQRAIKLGHAKININTECMIAWSDACRTTFAEQETAFEPRLLLQEGLAMVQATVEKKIKQFGAANKAAGSASLQRR | Function: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Catalytic Activity: 6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate
Sequence Mass (Da): 31239
Sequence Length: 293
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 6/7.
EC: 4.1.2.29
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P42420 | MAFVSMKELLEDAKREQYAIGQFNINGLQWTKAILQAAQKEQSPVIAAASDRLVDYLGGFKTIAAMVGALIEDMAITVPVVLHLDHGSSAERCRQAIDAGFSSVMIDGSHQPIDENIAMTKEVTDYAAKHGVSVEAEVGTVGGMEDGLVGGVRYADITECERIVKETNIDALAAALGSVHGKYQGEPNLGFKEMEAISRMTDIPLVLHGASGIPQDQIKKAITLGHAKININTECMVAWTDETRRMFQENSDLYEPRGYLTPGIEAVEETVRSKMREFGSAGKAAKQQVG | Function: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Catalytic Activity: 6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate
Sequence Mass (Da): 31372
Sequence Length: 290
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 6/7.
EC: 4.1.2.29
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Q9WYP3 | MRAVRLHAKWDPRPEFKLGPKDIEGKLTWLGSKVWRYPEVRVEEVPEPRIEKPTEIIIKVKACGICGSDVHMAQTDEEGYILYPGLTGFPVTLGHEFSGVVVEAGPEAINRRTNKRFEIGEPVCAEEMLWCGHCRPCAEGFPNHCENLNELGFNVDGAFAEYVKVDAKYAWSLRELEGVYEGDRLFLAGSLVEPTSVAYNAVIVRGGGIRPGDNVVILGGGPIGLAAVAILKHAGASKVILSEPSEVRRNLAKELGADHVIDPTKENFVEAVLDYTNGLGAKLFLEATGVPQLVWPQIEEVIWRARGINATVAIVARADAKIPLTGEVFQVRRAQIVGSQGHSGHGTFPRVISLMASGMDMTKIISKTVSMEEIPEYIKRLQTDKSLVKVTMLNE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of scyllo-inosose (2-keto-myo-inositol) to 3-dehydro-scyllo-inosose (diketo-inositol), and thus probably functions in a myo-inositol degradation pathway together with IolG, IolN and IolO. Has no activity on myo-inositol, D-chiro-inositol and 1-keto-D-chiro-inositol.
Catalytic Activity: NAD(+) + scyllo-inosose = 3-dehydro-scyllo-inosose + H(+) + NADH
Sequence Mass (Da): 43317
Sequence Length: 395
Pathway: Polyol metabolism; myo-inositol metabolism.
EC: 1.1.1.-
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Q9WYP4 | MERPTGVYFQTMTMKQIRERLKQCDLIIIPVGSTENHGPNAPTGEDTFLVTRMAEQVALKTGCTVAEPIWYGYHPYHHIGMPGTVPVKDEAFIDYLVSVIAGFWNTGFRKQILLNGHGQEFVIPIAIHKFAKIFQVPAIIINLNWYHAIQDKFKTKEEGGPYETPFIHADEVETSWSLALFPEFMHQEWAVDTEPKGFLPEGHIDKAGNLLHRPIAWYGHVGGGPIEVVAYPEGVVGKATLASAEKAKEGVEALLDYLEKLVRDIMERFPAGKLPPAEMLSQRPKEELEALTKEPLTEGWRNLYTAGNLWG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the ring-opening hydrolysis of 3-dehydro-scyllo-inosose (diketo-inositol) to 5-dehydro-L-gluconate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolO.
Catalytic Activity: 3-dehydro-scyllo-inosose + H2O = 5-dehydro-L-gluconate + H(+)
Sequence Mass (Da): 34947
Sequence Length: 311
Pathway: Polyol metabolism; myo-inositol metabolism.
EC: 3.7.1.-
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Q9WYP7 | MKLSLVISTSDAAFDALAFKGDLRKGMELAKRVGYQAVEIAVRDPSIVDWNEVKILSEELNLPICAIGTGQAYLADGLSLTHPNDEIRKKAIERVVKHTEVAGMFGALVIIGLVRGRREGRSYEETEELFIESMKRLLELTEHAKFVIEPLNRYETDFINTIDDALRILRKINSNRVGILADTFHMNIEEVNIPESLKRAGEKLYHFHVADSNRWAPGCGHFDFRSVFNTLKEIGYNRYVSVECLPLPGGMEEAAEIAFKTLKELIIKLT | Cofactor: Binds 1 divalent metal cation per subunit. Mn(2+) is the most efficient metal cofactor, but can also use other divalent metal cations such as Ni(2+), Mg(2+), and, to a lesser extent, Co(2+) and Zn(2+), but not Ca(2+), Cu(2+), and Fe(2+).
Function: Catalyzes the reversible epimerization between 5-keto-L-gluconate (5-dehydro-L-gluconate) and D-tagaturonate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolN . Is not active on the enantiomer 5-keto-D-gluconate . Was also shown to be a nonphosphorylated sugar isomerase with broad substrate specificity in vitro . Is able to catalyze the reversible C3-epimerization of L-ribulose to L-xylulose, D-ribulose to D-xylulose, D-psicose to D-fructose, and D-tagatose to D-sorbose, with a substrate preference for ketopentoses rather than ketohexoses . Also catalyzes the aldose-ketose isomerization reaction from either D-erythrose or D-threose to D-erythrulose . Exhibits no activity for C4-epimerization of D-tagatose to D-fructose .
Catalytic Activity: 5-dehydro-L-gluconate = keto-D-tagaturonate
Sequence Mass (Da): 30464
Sequence Length: 270
Pathway: Polyol metabolism; myo-inositol metabolism.
EC: 5.1.3.-
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O34718 | MNKQGNQMSFLRTIILVSTFGGLLFGYDTGVLNGALPYMGEPDQLNLNAFTEGLVTSSLLFGAALGAVFGGRMSDFNGRRKNILFLAVIFFISTIGCTFAPNVTVMIISRFVLGIAVGGASVTVPAYLAEMSPVESRGRMVTQNELMIVSGQLLAFVFNAILGTTMGDNSHVWRFMLVIASLPALFLFFGMIRMPESPRWLVSKGRKEDALRVLKKIRDEKRAAAELQEIEFAFKKEDQLEKATFKDLSVPWVRRIVFIGLGIAIVQQITGVNSIMYYGTEILRNSGFQTEAALIGNIANGVISVLATFVGIWLLGRVGRRPMLMTGLIGTTTALLLIGIFSLVLEGSPALPYVVLSLTVTFLAFQQGAISPVTWLMLSEIFPLRLRGLGMGVTVFCLWMVNFAVSFTFPILLAAIGLSTTFFIFVGLGICSVLFVKRFLPETKGLSLEQLEENFRAYDHSGAKKDSGAEVIG | Function: Major myo-inositol uptake transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51633
Sequence Length: 473
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA.
Subcellular Location: Cell membrane
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Q9UHH9 | MSPAFRAMDVEPRAKGVLLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRKFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGIVDIVDNSDCEPKSKLLRWTTNKKHHVLETEKTPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYTVEKKGNISSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTSRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGSGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLERQESYRFYSSSLLVIYDGKERPEVVLDSDAEDLEDLSEESADESAGAYAYKPIGASSVDVRMIDFAHTTCRLYGEDTVVHEGQDAGYIFGLQSLIDIVTEISEESGE | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 49186
Sequence Length: 426
Pathway: Phospholipid metabolism; phosphatidylinositol metabolism.
Subcellular Location: Nucleus
EC: 2.7.4.-
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Q9R0U1 | MSPAFRTMDVEPRTKGILLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRRFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGPVDIVDNSDCEPKSKLLRWTNKKHHVLETEKSPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYSVEKKGTVSSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTCRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGTGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLERQESYRFYSSSLLVIYDGKEWPEVTLDSDAEDLEDLSEESADESAGAYAYKPLGASSVDVRMIDFAHTTCRLYGEDSVVHEGQDAGYIFGLQSLIDIVTEISEESGE | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 49164
Sequence Length: 425
Pathway: Phospholipid metabolism; phosphatidylinositol metabolism.
Subcellular Location: Nucleus
EC: 2.7.4.-
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Q96PC2 | MVVQNSADAGDMRAGVQLEPFLHQVGGHMSVMKYDEHTVCKPLVSREQRFYESLPLAMKRFTPQYKGTVTVHLWKDSTGHLSLVANPVKESQEPFKVSTESAAVAIWQTLQQTTGSNGSDCTLAQWPHAQLARSPKESPAKALLRSEPHLNTPAFSLVEDTNGNQVERKSFNPWGLQCHQAHLTRLCSEYPENKRHRFLLLENVVSQYTHPCVLDLKMGTRQHGDDASEEKKARHMRKCAQSTSACLGVRICGMQVYQTDKKYFLCKDKYYGRKLSVEGFRQALYQFLHNGSHLRRELLEPILHQLRALLSVIRSQSSYRFYSSSLLVIYDGQEPPERAPGSPHPHEAPQAAHGSSPGGLTKVDIRMIDFAHTTYKGYWNEHTTYDGPDPGYIFGLENLIRILQDIQEGE | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4.
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 46417
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 2.7.4.21
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Q8BWD2 | MVVRHSSDKGKIGVGVPLEPFLHQVGGHLSVLQYDAYTVCKPLVSQEQKFYESLPLAMKCFTPKYKGTITVRLRRDSRGHLGLVANPLKENLEPFQVSPESRAVALWQTLQQTTGSESSPCPLTQLARSLKESAAKVLLRSDCHLSTQASPLVESEDGSQVERKGFNPWGLHCHQAHLTRLCSQYPEDKRHRFLLLENVVSQYKQPCILDLKMGTRQHGDDASEEKKARHMKKCAQSTSACLGVRICGMQVYQTDQKSFLCKDKYYGRKLSVEGFRQALSQFLHDGTRLRAELLEPILRRLQALLTVIRSQSSYRFYSSSVLIIYDGEPPQTTQGSTSGGVTSGDPAKVDVRMIDFAHTTFKGSWNEHTTYEGPDPGYIFGLENLIGILRDIQEGE | Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity).
Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP
Sequence Mass (Da): 44418
Sequence Length: 396
Subcellular Location: Cytoplasm
EC: 2.7.4.21
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Q83RJ4 | MSIMLPINNNFSLSQNSFYNTISGTYADYFSAWDKWEKQALPGENRNEAVSLLKECLINQFSELQLNRLNLSSLPDNLPPQITVLEITQNALISLPELPASLEYLDACDNRLSTLPELPASLKHLDVDNNQLTMLPELPALLEYINADNNQLTMLPELPTSLEVLSVRNNQLTFLPELPESLEALDVSTNLLESLPAVPVRNHHSEETEIFFRCRENRITHIPENILSLDPTCTIILEDNPLSSRIRESLSQQTAQPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSTSAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQVTDEVLALRLSENGSQLHHS | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Synthesizes a 'Lys-48'-linked ubiquitin chain, which requires non-covalent binding between ubiquitin and the host ubiquitin-conjugating enzyme UBE2D1.
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme UBE2D3 and ubiquitin.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 64943
Sequence Length: 571
Domain: The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins.
Subcellular Location: Secreted
EC: 2.3.2.27
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Q8VSC3 | MLPINNNFSLPQNSFYNTISGTYADYFSAWDKWEKQALPGEERDEAVSRLKECLINNSDELRLDRLNLSSLPDNLPAQITLLNVSYNQLTNLPELPVTLKKLYSASNKLSELPVLPPALESLQVQHNELENLPALPDSLLTMNISYNEIVSLPSLPQALKNLRATRNFLTELPAFSEGNNPVVREYFFDRNQISHIPESILNLRNECSIHISDNPLSSHALPALQRLTSSPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYPQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLPENGSQLHHS | Function: Effector E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell . Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), a ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG . Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection . Mediates polyubiquitination of host U2AF1, leading to its proteasomal degradation . Catalyzes 'Lys-48'-linked polyubiquitination and subsequent degradation of a subset of host guanylate-binding proteins (GBP1, GBP2, GBP4 and GBP6), thereby suppressing host cell defense . In contrast, host GBP3 and GBP7 are not ubiquitinated by IpaH9.8 . Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme .
PTM: Autoubiquitinated (in vitro) . Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 61979
Sequence Length: 545
Domain: The LRR (leucine-rich repeat) repeats are involved in substrate recognition with target proteins.
Subcellular Location: Secreted
EC: 2.3.2.27
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A7MB64 | MALGLFRVCLVVVTAIINHPLLFPRENTTVPENEEEIIRQMQAHQEKLQLEQLRLEEEMARLAADKEAEKEALERVAEEGQQQNESRTAWDLWSTLCMILFLVIEVWRQDHQDAPSPECLGSDEDELPDLEGAPLRGLTLPNRATLDHFYERCIRGATADAARTREFVEGFVDDLLEALRSLCSRDSDMEVEDFIGVDSMYENWQVNKPLLCDLFVPFMPPEPYHFHPELWCSSRSVPLDRQGYGQIKVVRADEDTLGCICGKTKLGEDMLCLLHGRNNVVHHGSKAADPLCAPNSPYLDTMRVMKWFQTALTRAWHRIEHKYEFDLAFGQLDTPGSLKIRFRSGKFMPFNLIPVIQCDDSDLYFVSHLAREPGGGTRASSTDWLLSFAVYERHFLRVTSKALPEGACHLSCLQIASFLLSKQSRLTGPSGLGSYHLKTALLHLLLARRPADWKAEQLDARLHELLCFLEKSLLEKKLQHFFIGNRKVPQAMGLPEAVRRAEPLNLFRPFVLQRSLYRKTVDSFYEMLKNAPALISEYSLHIPSDHASLPPKTVIL | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63432
Sequence Length: 556
Subcellular Location: Cell membrane
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Q567X9 | MQGAIARVCMVVVAAILNHPLLFPNENTTVPEQDEDLLARMKEHQEKLEAEQKRLEQEISQNETSVIGDQDGYGWYFWSALCLVIFFTIEVCRQDLISAEIPDPAEDEDGDCSTGYHSAKSIALDRGTLNNFCKTRFFPYTNESGRVREFIEGFADDLLEALRSICDLKADLEVEDFAGIGSMFESWRVSKPPTCDLIVPFSPPQPLRFQFELWCDPSTEIPLDLQGCGRIQLIKPGGNGTDCLCGSIDLGDDMLCLLHNRNECEVLEDDALPELLCARDTTYLSKGQIMRWFQISVSKAWGKISHKYDFELAFRNLDFPGALKIKFPSGKTVVLNLTPAVQFENTDAYLISHFPSDTSNSSDTHWQLSLSVYEKNLLKHLAKSLPTNSCHIHCLQIVAFLHKKQTTLTGRSAFCNYHIKTALLHLLLSKRPAMWQPQNLDSRLRDLLSFLQQSLEEKKLYHALVGNPRIPVEILVPKIIRTAEPINLYRPLVLQRHVYAKMEEHFEEMVRNTSVLVQEYTPHFSNGHVRHEFSSAEQI | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 61362
Sequence Length: 539
Subcellular Location: Cell membrane
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Q8IWB1 | MAMGLFRVCLVVVTAIINHPLLFPRENATVPENEEEIIRKMQAHQEKLQLEQLRLEEEVARLAAEKEALEQVAEEGRQQNETRVAWDLWSTLCMILFLMIEVWRQDHQEGPSPECLGGEEDELPGLGGAPLQGLTLPNKATLGHFYERCIRGATADAARTREFLEGFVDDLLEALRSLCNRDTDMEVEDFIGVDSMYENWQVDRPLLCHLFVPFTPPEPYRFHPELWCSGRSVPLDRQGYGQIKVVRADGDTLSCICGKTKLGEDMLCLLHGRNSMAPPCGDMENLLCATDSLYLDTMQVMKWFQTALTRAWKGIAHKYEFDLAFGQLDSPGSLKIKFRSGKFMPFNLIPVIQCDDSDLYFVSHLPREPSEGTPASSTDWLLSFAVYERHFLRTTLKALPEGACHLSCLQIASFLLSKQSRLTGPSGLSSYHLKTALLHLLLLRQAADWKAGQLDARLHELLCFLEKSLLQKKLHHFFIGNRKVPEAMGLPEAVLRAEPLNLFRPFVLQRSLYRKTLDSFYEMLKNAPALISEYSLHVPSDQPTPKS | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62060
Sequence Length: 547
Subcellular Location: Cell membrane
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Q3TNL8 | MAMELFRVCLVVVTAIINHPLLFPRENATIPENEEEIIRKMQEHQEKLRLEQLRLEEEVSRLEAEKEALRQVEEEQQQLEAHTAWDLWTTLCMVLFLIIEVLRQNHQEGTFPECLGGDEDELSGLGGTLLQGLPLPNRATLDHFYEHCIRSTTGDATRTQEFVEGFVDDLLEALRSTYNGKTDMELEDFIGVGSMYENWQVERPLRCHLFIPFIPPEPYSFHPEFWCSSLSTPLERQGYGQIKVTLADGNPLGCVCGKAKLEEDMLCLLYGKNRGAWPSSAGCGEMEGLLCSRESSYLDVMQVMKWFQMALTRAWHRIAHKYEFDLAFGELDTPGSLKIKFRSGKSMPFILTPVIQCNDSDLYFILQLPKEPCGGGPASSAHWLLSFAVYEREFLRMTGKALPEGACHLSCLQIASFLLSKQTRLTGPSGLSDYHLKTALLHLLLSRQASDWKASKLDVRLQDLFCFLERSLLEKKLYHFFMGNHKVPEALGLPEVVRRAEPLNLFRPFVLQRTLYRNTVDSFYEMLKNAPALISEYSLHVPSVRASPPPKAVVS | Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63238
Sequence Length: 555
Subcellular Location: Cell membrane
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P05154 | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP | Function: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.
PTM: N- and O-glycosylated. N-glycosylation consists of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated with core 1 or possibly core 8 glycans. Further modified with 2 sialic acid residues.
Sequence Mass (Da): 45675
Sequence Length: 406
Domain: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
Subcellular Location: Secreted
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P70458 | MRFFPILCLVLFISHGVASRRHSHSKKKKAKESSVGAVGPPSSKDFAFRLYRALVSESPGQNVFFSPLSVSMSLGMLSLGAGLKTKTQILDGLGLSLQQGQEDKLHKGFQQLLQRFRQPSDGLQLSLGSALFKDPAVHIRDDFLSAMKTLYMSDTFSTNFGNPEIAKKQINNYVAKQTKGKIVDFIKDLDSTHVMIVVNYIFFKAKWQTAFSETNTHKMDFHVTPKRTTQVPMMNREDGYSYYLDQNISCTVVGIPYQGNAIALFILPSEGKMKQVEDGLDERTLRNWLKMFTKRRLDLYLPKFSIEATYKLENVLPKLGIQDVFTTHADLSGITDHTNIKLSEMVHKSMMEVEESGTTAAAITGAIFTFRSARPSSLKIEFTRPFLLTLMEDSHILFVGKVTRP | Function: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid (By similarity).
PTM: N-glycosylated; glycans consist of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated; further modified with 2 sialic acid residues. Proteolytically cleaved at the N-terminus; inhibits slightly the heparin- and thrombomodulin-enhanced rates of thrombin inhibition (By similarity).
Sequence Mass (Da): 45600
Sequence Length: 405
Domain: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
Subcellular Location: Secreted
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Q94ID3 | MTELNFHLLPIISDRFTTTTTTSPSFSSHSSSSSSLLSFTKRRRKHQPLVSSIRMEQSRSRNRKDKVVVILGATGAGKSRLSVDLATRFPSEIINSDKIQVYEGLEITTNQITLQDRRGVPHHLLGVINPEHGELTAGEFRSAASNVVKEITSRQKVPIIAGGSNSFVHALLAQRFDPKFDPFSSGSCLISSDLRYECCFIWVDVSETVLYEYLLRRVDEMMDSGMFEELSRFYDPVKSGLETRFGIRKAIGVPEFDGYFKEYPPEKKMIKWDALRKAAYDKAVDDIKRNTWTLAKRQVKKIEMLKDAGWEIERVDATASFKAVMMKSSSEKKWRENWEEQVLEPSVKIVKRHLVQN | Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP, ADP and AMP. Adenine, adenosine, isopentenylpyrophosphate and 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBDP) are not used as substrates.
Catalytic Activity: AMP + dimethylallyl diphosphate = diphosphate + N(6)-(dimethylallyl)adenosine 5'-phosphate
Sequence Mass (Da): 40765
Sequence Length: 357
Subcellular Location: Plastid
EC: 2.5.1.112
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Q15306 | MNLEGGGRGGEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSIFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLEDPQMSMSHPYTMTTPYPSLPAQQVHNYMMPPLDRSWRDYVPDQPHPEIPYQCPMTFGPRGHHWQGPACENGCQVTGTFYACAPPESQAPGVPTEPSIRSAEALAFSDCRLHICLYYREILVKELTTSSPEGCRISHGHTYDASNLDQVLFPYPEDNGQRKNIEKLLSHLERGVVLWMAPDGLYAKRLCQSRIYWDGPLALCNDRPNKLERDQTCKLFDTQQFLSELQAFAHHGRSLPRFQVTLCFGEEFPDPQRQRKLITAHVEPLLARQLYYFAQQNSGHFLRGYDLPEHISNPEDYHRSIRHSSIQE | Function: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes (By similarity).
PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21 production.
Sequence Mass (Da): 51772
Sequence Length: 451
Subcellular Location: Nucleus
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Q64287 | MNLETGSRGSEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSVFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLDDTQMAMGHPYPMTAPYGSLPAQQVHNYMMPPHDRSWRDYAPDQSHPEIPYQCPVTFGPRGHHWQGPSCENGCQVTGTFYACAPPESQAPGIPIEPSIRSAEALALSDCRLHICLYYRDILVKELTTTSPEGCRISHGHTYDVSNLDQVLFPYPDDNGQRKNIEKLLSHLERGLVLWMAPDGLYAKRLCQSRIYWDGPLALCSDRPNKLERDQTCKLFDTQQFLSELQVFAHHGRPAPRFQVTLCFGEEFPDPQRQRKLITAHVEPLLARQLYYFAQQNTGHFLRGYELPEHVTTPDYHRSLRHSSIQE | Function: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes.
PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21 production.
Sequence Mass (Da): 51577
Sequence Length: 450
Subcellular Location: Nucleus
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Q13568 | MNQSIPVAPTPPRRVRLKPWLVAQVNSCQYPGLQWVNGEKKLFCIPWRHATRHGPSQDGDNTIFKAWAKETGKYTEGVDEADPAKWKANLRCALNKSRDFRLIYDGPRDMPPQPYKIYEVCSNGPAPTDSQPPEDYSFGAGEEEEEEEELQRMLPSLSLTEDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLAPPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISPHMLPLTDLEIKFQYRGRPPRALTISNPHGCRLFYSQLEATQEQVELFGPISLEQVRFPSPEDIPSDKQRFYTNQLLDVLDRGLILQLQGQDLYAIRLCQCKVFWSGPCASAHDSCPNPIQREVKTKLFSLEHFLNELILFQKGQTNTPPPFEIFFCFGEEWPDRKPREKKLITVQVVPVAARLLLEMFSGELSWSADSIRLQISNPDLKDRMVEQFKELHHIWQSQQRLQPVAQAPPGAGLGVGQGPWPMHPAGMQ | Function: Transcription factor that plays a critical role in innate immunity by activating expression of type I interferon (IFN) IFNA and INFB and inflammatory cytokines downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (By similarity). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction downstream of the TLR-activated, MyD88-dependent pathway (By similarity). Key transcription factor regulating the IFN response during SARS-CoV-2 infection .
PTM: Phosphorylation of serine and threonine residues by IKBKB in a C-terminal autoinhibitory region, stimulates dimerization, transport into the nucleus, assembly with the coactivator CBP/EP300 and initiation of transcription.
Sequence Mass (Da): 56044
Sequence Length: 498
Subcellular Location: Cytoplasm
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Q08DD6 | MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPIAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLVAPNLIERQKKVKLFCLETFLSDLIAHQKGQIEKQPPFEIYLCFGEEWPDGKPQERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPAPSMQLPTTLPAQ | Function: Probable DNA-binding transcriptional activator. It is a key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity).
PTM: Phosphorylated. Phosphorylation status depends on the cell cycle and is a signal for ubiquitination and proteasome-mediated degradation.
Sequence Mass (Da): 53105
Sequence Length: 467
Subcellular Location: Nucleus
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O14896 | MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPMAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLVAPNLIERQKKVKLFCLETFLSDLIAHQKGQIEKQPPFEIYLCFGEEWPDGKPLERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPTPSMQLPPALPPQ | Function: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development (By similarity). Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity).
PTM: Phosphorylated. Phosphorylation status depends on the cell cycle and is a signal for ubiquitination and proteasome-mediated degradation.
Sequence Mass (Da): 53130
Sequence Length: 467
Subcellular Location: Nucleus
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Q92985 | MALAPERAAPRVLFGEWLLGEISSGCYEGLQWLDEARTCFRVPWKHFARKDLSEADARIFKAWAVARGRWPPSSRGGGPPPEAETAERAGWKTNFRCALRSTRRFVMLRDNSGDPADPHKVYALSRELCWREGPGTDQTEAEAPAAVPPPQGGPPGPFLAHTHAGLQAPGPLPAPAGDKGDLLLQAVQQSCLADHLLTASWGADPVPTKAPGEGQEGLPLTGACAGGPGLPAGELYGWAVETTPSPGPQPAALTTGEAAAPESPHQAEPYLSPSPSACTAVQEPSPGALDVTIMYKGRTVLQKVVGHPSCTFLYGPPDPAVRATDPQQVAFPSPAELPDQKQLRYTEELLRHVAPGLHLELRGPQLWARRMGKCKVYWEVGGPPGSASPSTPACLLPRNCDTPIFDFRVFFQELVEFRARQRRGSPRYTIYLGFGQDLSAGRPKEKSLVLVKLEPWLCRVHLEGTQREGVSSLDSSSLSLCLSSANSLYDDIECFLMELEQPA | Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters . Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (By similarity). Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages (By similarity) .
PTM: Acetylation inhibits its DNA-binding ability and activity.
Sequence Mass (Da): 54278
Sequence Length: 503
Subcellular Location: Nucleus
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P70434 | MAEVRGVQRVLFGDWLLGEVSSGQYEGLQWLNEARTVFRVPWKHFGRRDLDEEDAQIFKAWAVARGRWPPSGVNLPPPEAEAAERRERRGWKTNFRCALHSTGRFILRQDNSGDPVDPHKVYELSRELGSTVGPATENREEVSLSNALPTQGVSPGSFLARENAGLQTPSPLLSSDAGDLLLQVLQYSHILESESGADPVPPQAPGQEQDRVYEEPYAAWQVEAVPSPRPQQPALTERSLGFLDVTIMYKGRTVLQAVVGHPRCVFLYSPMAPAVRTSEPQPVIFPSPAELPDQKQLHYTETLLQHVSPGLQLELRGPSLWALRMGKCKVYWEVGSPMGTTGPSTPPQLLERNRHTPIFDFSTFFRELEEFRARRRQGSPHYTIYLGFGQDLSAGRPKEKTLILVKLEPWVCKAYLEGVQREGVSSLDSSSLGLCLSSTNSLYEDIEHFLMDLGQWP | Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses . Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner . Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.
PTM: Acetylation inhibits its DNA-binding ability and activity.
Sequence Mass (Da): 51222
Sequence Length: 457
Subcellular Location: Nucleus
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Q02556 | MCDRNGGRRLRQWLIEQIDSSMYPGLIWENEEKSMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVATAGCVNEVTEMECGRSEIDELIKEPSVDDYMGMIKRSPSPPEACRSQLLPDWWAQQPSTGVPLVTGYTTYDAHHSAFSQMVISFYYGGKLVGQATTTCPEGCRLSLSQPGLPGTKLYGPEGLELVRFPPADAIPSERQRQVTRKLFGHLERGVLLHSSRQGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTSQFFRELQQFYNSQGRLPDGRVVLCFGEEFPDMAPLRSKLILVQIEQLYVRQLAEEAGKSCGAGSVMQAPEEPPPDQVFRMFPDICASHQRSFFRENQQITV | Function: Transcription factor that specifically binds to the upstream regulatory region of type I interferon (IFN) and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) . Can both act as a transcriptional activator or repressor (By similarity). Plays a negative regulatory role in cells of the immune system (By similarity). Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes (By similarity). Required for the development of plasmacytoid dendritic cells (pDCs), which produce most of the type I IFN in response to viral infection (By similarity). Positively regulates macroautophagy in dendritic cells . Acts as a transcriptional repressor of osteoclast differentiation factors such as NFATC1 and EEIG1 (By similarity).
PTM: Ubiquitinated . Ubiquitination by TRIM21 in macrophages, a process that is strongly increased upon interferon gamma stimulation, leds to the enhanced transcriptional activity of target cytokine genes (By similarity). Ubiquitination leads to its degradation by the proteasome .
Sequence Mass (Da): 48356
Sequence Length: 426
Subcellular Location: Nucleus
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P23611 | MCDRNGGRRLRQWLIEQIDSSMYPGLIWENDEKTMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVAPAGCMSEVPEMECGRSEIEELIKEPSVDEYMGMTKRSPSPPEACRSQILPDWWVQQPSAGLPLVTGYAAYDTHHSAFSQMVISFYYGGKLVGQATTTCLEGCRLSLSQPGLPKLYGPDGLEPVCFPTADTIPSERQRQVTRKLFGHLERGVLLHSNRKGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTNQFIRELQQFYATQSRLPDSRVVLCFGEEFPDTVPLRSKLILVQVEQLYARQLVEEAGKSCGAGSLMPALEEPQPDQAFRMFPDICTSHQRPFFRENQQITV | Function: Transcription factor that specifically binds to the upstream regulatory region of type I interferon (IFN) and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) . Can both act as a transcriptional activator or repressor . Plays a negative regulatory role in cells of the immune system . Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes . Required for the development of plasmacytoid dendritic cells (pDCs), which produce most of the type I IFN in response to viral infection . Positively regulates macroautophagy in dendritic cells (By similarity). Acts as a transcriptional repressor of osteoclast differentiation factors such as NFATC1 and EEIG1 .
PTM: Ubiquitinated . Ubiquitination by TRIM21 in macrophages, a process that is strongly increased upon interferon gamma stimulation, leds to the enhanced transcriptional activity of target cytokine genes . Ubiquitination leads to its degradation by the proteasome (By similarity).
Sequence Mass (Da): 48237
Sequence Length: 424
Subcellular Location: Nucleus
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Q00978 | MASGRARCTRKLRNWVVEQVESGQFPGVCWDDTAKTMFRIPWKHAGKQDFREDQDAAFFKAWAIFKGKYKEGDTGGPAVWKTRLRCALNKSSEFKEVPERGRMDVAEPYKVYQLLPPGIVSGQPGTQKVPSKRQHSSVSSERKEEEDAMQNCTLSPSVLQDSLNNEEEGASGGAVHSDIGSSSSSSSPEPQEVTDTTEAPFQGDQRSLEFLLPPEPDYSLLLTFIYNGRVVGEAQVQSLDCRLVAEPSGSESSMEQVLFPKPGPLEPTQRLLSQLERGILVASNPRGLFVQRLCPIPISWNAPQAPPGPGPHLLPSNECVELFRTAYFCRDLVRYFQGLGPPPKFQVTLNFWEESHGSSHTPQNLITVKMEQAFARYLLEQTPEQQAAILSLV | Function: Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.
PTM: (Microbial infection) Ubiquitinated by Herpes simplex virus 2 E3 ubiquitin ligase ICP22.
Sequence Mass (Da): 43696
Sequence Length: 393
Subcellular Location: Cytoplasm
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A6NK06 | MMLKSITESFATAIHGLKVGHLTDRVIQRSKRMILDTLGAGFLGTTTEVFHIASQYSKIYSSNISSTVWGQPDIRLPPTYAAFVNGVAIHSMDFDDTWHPATHPSGAVLPVLTALAEALPRSPKFSGLDLLLAFNVGIEVQGRLLHFAKEANDMPKRFHPPSVVGTLGSAAAASKFLGLSSTKCREALAIAVSHAGAPMANAATQTKPLHIGNAAKHGIEAAFLAMLGLQGNKQVLDLEAGFGAFYANYSPKVLPSIASYSWLLDQQDVAFKRFPAHLSTHWVADAAASVRKHLVAERALLPTDYIKRIVLRIPNVQYVNRPFPVSEHEARHSFQYVACAMLLDGGITVPSFHECQINRPQVRELLSKVELEYPPDNLPSFNILYCEISVTLKDGATFTDRSDTFYGHWRKPLSQEDLEEKFRANASKMLSWDTVESLIKIVKNLEDLEDCSVLTTLLKGPSPPEVASNSPACNNSITNLS | Function: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response . Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages . Involved in antimicrobial response of innate immune cells; ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages by generating itaconate, leading to alkylation of proteins, such as TFEB . Involved in antiviral response following infection by flavivirus in neurons: ACOD1-mediated itaconate production inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). Plays a role in the embryo implantation (By similarity).
Catalytic Activity: cis-aconitate + H(+) = CO2 + itaconate
Sequence Mass (Da): 52628
Sequence Length: 481
Subcellular Location: Mitochondrion
EC: 4.1.1.6
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P54987 | MMLKSVTESFAGMIHGLKVNHLTDGIIRRSKRMILDSLGVGFLGTGTEVFHKVTQYSKIYSSNTSSTVWGRPDFRLPPTYAAFVNGVAVHSMDFDDTWHPATHPSGAVLPVLTALSEALPQIPKFSGLDLLLAFNVGIEVQGRLMHFSKEAKDIPKRFHPPSVVGTLGSAAAASKFLGLSLTKCREALAIAVSHAGAPIANAATQTKPLHIGNAAKHGMEATFLAMLGLQGNKQILDLGSGFGAFYANYSPEDLPSLDSHIWLLDQQDVAFKSFPAHLATHWVADAAAAVRKHLVTPERALFPADHIERIVLRIPDVQYVNRPFPDSEHEARHSFQYVACASLLDGSITVPSFHSQQVNRPQVRELLKKVKLEHPPDNPPSFDTLYCEISITLKDGTTFTERSDTFYGHWRKPLSQEDLRNKFRANASKMLCRDTVESLITVVEKLEDLEDCSVLTRLLKGPSVQDEASKLSSMSSFDHTTLPRFTNI | Function: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response . Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages . Involved in antimicrobial response of innate immune cells; ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages by generating itaconate, leading to alkylation of proteins, such as TFEB . Involved in antiviral response following infection by flavivirus in neurons: ACOD1-mediated itaconate production inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes . Plays a role in the embryo implantation .
Catalytic Activity: cis-aconitate + H(+) = CO2 + itaconate
Sequence Mass (Da): 53758
Sequence Length: 488
Subcellular Location: Mitochondrion
EC: 4.1.1.6
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A5F9G0 | MSRFNPSPVSLSVTLGLMFSASAFAQDATKTDETMVVTAAGYAQVIQNAPASISVISREDLESRYYRDVTDALKSVPGVTVTGGGDTTDISIRGMGSNYTLILVDGKRQTSRQTRPNSDGPGIEQGWLPPLQAIERIEVIRGPMSTLYGSDAIGGVINIITRKDQQQWSGNVQLSTVVQENRASGDEQSANFFVTGPLSDALSLQVYGQTTQRDEDEIEHGYGDKSLRSLTSKLNYQLNPDHQLQLEAGVSAQDRENNVGKSAQSSGCRGTCSNTDNQYRRNHVAVSHQGDWQGVGQSDTYLQYEENTNKSREMSIDNTVFKSTLVAPIGEHMLSFGVEGKHESLEDKTSNKISSRTHISNTQWAGFIEDEWALAEQFRLTFGGRLDHDKNYGSHFSPRVYGVWNLDPLWTVKGGVSTGFRAPQLREVTPDWGQVSGGGNIYGNPDLQPETSINKELSLMYSTGSGLAASLTAFHNDFKDKITRVACPANICTAGPNQWGATPTYRVNIDEAETYGAEATLSLPITESVELSSSYTYTHSEQKSGNFAGRPLLQLPKHLFNANLSWQTTDRLNSWANLNYRGKEMQPEGGASNDDFIAPSYTFIDTGVTYALTDTATIKAAVYNLFDQEVNYAEYGYVEDGRRYWLGLDIAF | Function: Involved in the initial step of iron uptake by binding ferric vibriobactin, an iron chelatin siderophore that allows V.cholerae to extract iron from the environment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71641
Sequence Length: 652
Subcellular Location: Cell outer membrane
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Q3IFI3 | MKLPIYLDYAATTPVDERVAKEMMQCLTMDGNFGNPASRSHRFGWQAEEVVDQARTDVADLINADPREIVFTSGATESNNLAIKGAAQFYKKKGKHIITAKTEHKAVIDTCRELERQGFEVTYMDVEENGLLDLQKLADTMRDDTVLVSIMHVNNELGVIQDIATIGEMCRERKIMFHVDAAQSAGKVLIDVQQLKVDFMSFSGHKVYGPKGVGALYVRRKPRARLEAQMHGGGHERGMRSGTLATHQLVGMGTAFRVAKQDFEKDHAHISALRKRLIDGIMSDMEEVYFNGTQDQSVPGIVNISFNFVEGESLLMAVKDIAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFSIGRFTTEEEIDYTVELMKNSIGRLREMSPLWEMHQEGIDLDSVEWAHH | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 45214
Sequence Length: 405
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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Q1RHY6 | MNTQLNNLILPIYMDYQATTPLDPRVMEAMLPYFTTKFGNPHSHSHSFGWEAENAVEEARGDIAKLIGAEAKEIIFTSGATESNNLAIKGIAKFYGNKKNHIITVVSEHKCVLDACRHLEQEGVKVTYLPIKPNGIIDLEVLKNAITDQTMLVSVMAVNNEIGVIQPLKEIGKICREKGVFFHSDSAQGFGKVPIDVNECNIDLASISGHKIYGPKGIGALYVRKKPRVRITPLINGGGQERGMRSGTLPTPLIVGLGTAANIAYNEMEKDTKHVNHLFDKFLDAINSQISEVYLNGDKDQRYKGNLNLSFAGVEGESIILAIKDLAVSSGSACTSASLEPSYVLRSMGVDEELAHTSIRFGIGRFTTEQEIDYAVKLICSKINKLRDLSPLWEMMQEGIDLKKIKWATH | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 45189
Sequence Length: 410
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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Q4UL77 | MNPQLNNPNLPIYMDYQATTPLDPRVMEAMLPYFTTKFGNPHSRSHSFGWEAENAVEEARSRVARLIGADTKEIIFTSGATESNNLAIKGIAKFYGNKKNHIITVVSEHKCVLDACRHLEQEGIKITYLPIKPNGIIDLETLKNAITDQTMLVSVMAVNNEIGVVQPLKEIGKICRERGVFFHSDIAQGFGKIPIDVNEFNIDLASISGHKIYGPKGIGALYVRKKPRVRVTPLINGGGQERGMRSGTLPTPLIVGLGMAAEIAYSVMEKDTKHVNYLFDRFLNNIHNRISEVYLNGDKNQRYKGNINLSFAGVEGESIILAIKDLAVSSGSACTSASLEPSYVLRSMGIGEELAHTSIRFGIGRFTTEQEVDYAVDLICSKIDKLRELSPLWEMVQEGIDLKKIKWATH | Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 45477
Sequence Length: 410
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.7
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Q2FXJ2 | MNKHHPKLRSFYSIRKSTLGVASVIVSTLFLITSQHQAQAAENTNTSDKISENQNNNATTTQPPKDTNQTQPATQPANTAKNYPAADESLKDAIKDPALENKEHDIGPREQVNFQLLDKNNETQYYHFFSIKDPADVYYTKKKAEVELDINTASTWKKFEVYENNQKLPVRLVSYSPVPEDHAYIRFPVSDGTQELKIVSSTQIDDGEETNYDYTKLVFAKPIYNDPSLVKSDTNDAVVTNDQSSSVASNQTNTNTSNQNISTINNANNQPQATTNMSQPAQPKSSTNADQASSQPAHETNSNGNTNDKTNESSNQSDVNQQYPPADESLQDAIKNPAIIDKEHTADNWRPIDFQMKNDKGERQFYHYASTVEPATVIFTKTGPIIELGLKTASTWKKFEVYEGDKKLPVELVSYDSDKDYAYIRFPVSNGTREVKIVSSIEYGENIHEDYDYTLMVFAQPITNNPDDYVDEETYNLQKLLAPYHKAKTLERQVYELEKLQEKLPEKYKAEYKKKLDQTRVELADQVKSAVTEFENVTPTNDQLTDLQEAHFVVFESEENSESVMDGFVEHPFYTATLNGQKYVVMKTKDDSYWKDLIVEGKRVTTVSKDPKNNSRTLIFPYIPDKAVYNAIVKVVVANIGYEGQYHVRIINQDINTKDDDTSQNNTSEPLNVQTGQEGKVADTDVAENSSTATNPKDASDKADVIEPESDVVKDADNNIDKDVQHDVDHLSDMSDNNHFDKYDLKEMDTQIAKDTDRNVDKDADNSVGMSSNVDTDKDSNKNKDKVIQLNHIADKNNHTGKAAKLDVVKQNYNNTDKVTDKKTTEHLPSDIHKTVDKTVKTKEKAGTPSKENKLSQSKMLPKTGETTSSQSWWGLYALLGMLALFIPKFRKESK | Function: Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 100947
Sequence Length: 895
Domain: The NEAT 1 domain binds with higher affinity than the NEAT 2 domain haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin.
Subcellular Location: Secreted
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A7I1V2 | MKDITLVLLAAGDSTRFKAPFKKQWIRIGEIPLWQYVAKDLSQKCDFSDIIIVANEKEISYMKKIERNFKYAKGGKLRQNSLANALKKVKSEFVFVSDTARAEISKDLIGRLINECEKFDCVSPFLGVVDTTYLGRNQIDRNDLKLIQTPQISRANLLKKALESNEIFTDDSAAVAFAGGKLGFVEGDEKARKITFTSDLAHFDFTPASGTIFTGNGFDVHAFAKGEFITLGGVKIPCEYSLVGHSDADAAIHALMDAILGACGLGDIGELFPDTDDSFKGIDSKILLQKVVNFVHLLGFKIINADITIIAQKPKISPYKEKMCEILSEILQTSRVNVKASTTEKLGFVGRVEGVAAIASANLGYFDWRKF | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 40914
Sequence Length: 371
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q9PM68 | MSEMSLIMLAAGNSTRFNTKVKKQFLRLGNDPLWLYATKNLSSFYPFKKIVVTSSNITYMKKFTKNYEFIEGGDTRAESLKKALELIDSEFVMVSDVARVLVSKNLFDRLIENLDKADCITPALKVADTTLFDNEALQREKIKLIQTPQISKTKLLKKALDQNLEFTDDSTAIAAMGGKIWFVEGEENARKLTFKEDLKKLDLPTPSFEIFTGNGFDVHEFGENRPLLLAGVQIHPTMGLKAHSDGDVLAHSLTDAILGAAGLGDIGELYPDTDMKFKNANSMELLKQAYDKVREIGFELINIDICVMAQSPKLKDFKQAMQSNIAHTLDLDEFRINVKATTTEKLGFIGRKEGMAVLSSVNLKYFDWTRL | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 41690
Sequence Length: 371
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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Q9A7I5 | MTFSVVIVAAGSGTRAGPGQAKQWRVLAGRPVLRWSVEAFLAAGAAEVVVVTTADGEAFLPRMLEGLQGWRSTLGGATRALSVQAGLAALSERPGAEPVMIHDAARPFVSRNVILALLGALSDADLALPALAVADTLKRQPTGEAAQTVSREHLWRAQTPQAARRDTLIAAYAAWTHGEPTDDAQVVEAAGGRIALTAGDPLLTKLTYPEDFAMAEHLAGVARVTRVGQGFDAHRWGPGEEVWLCGVAIKHDETLVGHSDADAGLHALTDAILGAIGEGDIGDHFPPTDPKWKGAASDQFLKHAVDLVTAKGGALVNVDVTLICERPKIKPHRQAMRERLAEILSIPVDRVSVKATTTEKMGFTGRGEGLAASAVVAVETPA | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 40049
Sequence Length: 382
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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A5CTY4 | MSHDPVVPSAPATDGGATDGPRLGVVVVAAGSGTRLGAGIPKALVEVGGVTLLARSLSSVLGLAEEAHVVVVAPDTHLAETSAVVDAVAGAARGSVAVVVGGATRQGSVRAGLAALVGSVDTVLVHDAARALTPTDLFAAVARAVRAEGAGVVPGLPVTDTVKRVDPAGECLGTVDRSDLVGVQTPQGFPRAALDAAYARAAAEHTDDAALFQASGGRVRVIPGDALAFKVTTAWDLRRAEELVARDAGAGSASSRLRSGIGTDVHAVDASQPLWLAGLHWPGEAGLAGHSDGDAVSHAMCDALLSAAGLGDIGGIFGTDDPELDGAHGEVFLRRTAELVRDAGYRIVNVAVQVMAVRPKLSPRRAEAERILSAAVGAPVSLAGTTTDGLGFTGRGDGVAAVATALVERL | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 40906
Sequence Length: 410
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
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B1GYT4 | MKNAAIIAAAGSGKRFGSRVSKQFLNLSGKPVFLWSVEAFASIKSFKQIIVVVPSDMVEFLSLKYKTGFVCATGGNERFDSVKNGLALVGDDIDFIAVHDASRPLISKKDILLVLEKAAKTKVAVAVEKAKDTVKLVSADGYILKTLDRTILRNAQTPQIFKTELLKRAYSRKMSAGTTDDSQLVENLKIKVSAVETKFLNFKITTKQDFELAEKILKS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 24065
Sequence Length: 219
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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Q2J542 | MGEGHRLPVASPRVAAIVPAAGRGERLGGGTPKALRALGGRPMLVRTVESLRRSRLVTQIVVAAPPTLVDAVAQLLGGDVYVIAGGAERVDSVRRALRAVDDDVSVVLVHDAARPLTPPELVDAVAAAVLDGHPAVIPVVPLADTVKEVDADGRVVRTPPRDGLRAVQTPQGFRRDVLSAAYALEDIAVTDDAGLVEALGVPVTTIPGAQEAFKVTRPADLVLAEALLARCDPADDARSAEARSAEARSEEPQFAGARSTDARSGG | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 27498
Sequence Length: 266
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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Q8R6H2 | MYSSNSEIKKKVTFILAAAGQGKRMNLNSPKQFLDYRGEPLFYSSLKLAFENKNINDIIIITNKENLNFMVKYCQNKNLFSKVKYIVEGGSERQYSIYNAIKKIKDTDIVIIQDAARPFLKDKYIEESLKILNDDCDGAIIGVKCKDTIKIIDENGIVLETPNRDNLIMVHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKIKIIYGDYDNIKITVQEDLKFLK | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26491
Sequence Length: 231
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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Q9KUJ2 | MNNMTAIVPAAGVGSRMQADRPKQYLTLLDKTVLEHTVEHLLEHPLIEHVVVAVSADDPYFANLPLAHHPRVIRVDGGKERADSVLSALEYVCQHRLSEWVLVHDAARPCVTHADITQLITTALAHPIGAILASPVRDTMKRGDHLQQIVHTVDRTALWHALTPQMFRAQSLRERLFAALQQQVTITDEASAFEWRGEKPALVAGRADNLKITQPEDLALAEFYLSRNKEKS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25902
Sequence Length: 232
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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Q8PLR8 | MTGSIWAIVPAAGRGTRFGGPLPKQYLQAGGQPLMAYTLAALAAHPALAGIMVAIAPGDADWPGWTAVQSKPVLTCLGGATRAASVLSGLLALPESVRADDFVLVHDAARPNLALADLDRLLEIGRGDPVGAILAAPVRDTLKRAGDDGGIDGTEPRERLWRALTPQLFRRHQLIRGLTEASAAGVEVTDEAMAMERIGLRPLLVEGAEDNFKVTTPADLARFEFELANRDCGPGTRDPESAHPQSSVSASAFSGPGSRAPGPEEI | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 27793
Sequence Length: 266
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
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Q6AAD6 | MTVTVRVSAKVNLALGVGGLAPDGFHPLATVFEAICIYDEVAVTRRDDSRITLTVSGEDADQVPTDETNLAWRAVELVREEFASEWGKRGHGADIHIDKSIPVAGGMAGGSADAAGALMAAAALCRLPYSPEELQPLAAQLGSDVPFCLTGGVALGRGRGDRLAPVICRGRHRWVFATSNQGLSTPAVYRRFDELGGTPGGETVPNDLISALTRGDLDAVAASLSNDLQAAAIDLRPELEEVLTVGREVGALTALVSGSGPTCAFLVRDTAGAKKVSAAVSNLPQVHRTRTARGPAAGAQLLPGPVGSFA | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32024
Sequence Length: 310
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q11VT3 | MISFPNAKINLGLSVLSKRPDGYHNIETCFYPIPWNDMLEIIPAKETVFTSSGNNIPGTSASNLCLKTYTLLKEKYPLSPVHIHLHKRIPIGAGLGGGSSDAAFTCKLLNDVFALKLSAAEMEDIVRPVGSDCAFFIENTSILAHEKGDYFSHPGIVNLSGKWIYLIHPGIHVATKEAYDGVVPNTDRKPIGDILKQPLSVWKAELVNDFERSVFEKYPAIKTLKEQMYKQGAAYAAMSGSGSTVFGIFNTKPETFHENTSNIQSCIAPL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29635
Sequence Length: 270
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q3Z9E9 | MLTLLAPAKVNLSLEVLYRRNDGYHELRSIIQSLSLCDRLSFSPAKTVQISSDSPDWQAEHSLVSKAVALFSEKCGQGRGVNLTIAKRIPLVSGLGGDSSCAAAVLKGLNKLWGCGYPRWRLMELGAELGSDVPFFMMGGTAMMEGRGETVTPLPTLNQMWAVLLVPEIEMPPDKTAALYRNLHADSFSSGEISDKLLEDICQGKLSYSSCFNVFEKIAFTLFPDLAKYRWQFLEAGAYQIFLAGAGPTLFTLLKDKNMAEKIYHNLCQKGHQAYLVSTLGPLD | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31235
Sequence Length: 284
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q9RR89 | MTHQPSPVIHHHFAPAKINLGLSVLGVRENGYHDLHSLMVPLTVGDELEIRPAGALTLRVEGADLPTDERNLVYRAARAYLDAAGAAGGADLVLHKRLPLASGLGGGSSDAASTLLALAELYPAPDHRPVDLPALALTLGADVPFFLLGGAALAEGVGERLTPVDDLPPVHLVLANAGAEVSAGDAYRWLDETGDFSGKLRLEAMRLALARGVEVPYFNSLQAGVLARVPSVLTTLEALADAGLHSVLMSGSGATCFGLAHDAAQAQAAAAALAQRCPGWWVTAAQVRLPLSDNSGGRT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30919
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q251V5 | MIRNQVEMFAYAKINLALAITGRRPDGYHELESVMQSIGIYDRIRVTLAEGGIQCSCGEWSGPENLAYRAAEAFLSGLGSSQGIHIDIEKNIPVQAGLGGGSADAAAALQALNKLFKEPYTEEELKSFAAQLGADVAFCLKGGTQWATGVGEELKGLPHAPKINLVLIKPDQGVNTAEAYRAFDQEGKFSHLDYAGWQEALASGRAESLIPLLYNDLEPASMKLLPEIAWVKEELMKQNGCLGALMSGSGSAVFGIVQTEEQAEKIAAIWRERNYHVWVTHTMERGNIYG | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31504
Sequence Length: 290
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q6AJL6 | MDRNEGELAQVATRLHMRAPAKVNLSLQVLSRRADGYHDLATHMQKVSLYDELELCLTKQSGVSLVCSDGDIPLDEKNLAVRAALAYLARSSRVGQRGVRISLEKNIPVGAGLGGGSSDAGTVLRGLNQLLDNEFSEEELIEMARPLGADVPFFASEMSAAFATGIGDILQPLESTKEFDFILVNPGIFISTKEIFERFSLTLSPKRNIFARPFRVHERASLLDYMHNDLEEIVSDLCPAIDEMKSLLEANGASAVMMSGSGSTVFGVFQRSVGQKKINQVCKVLSCKYGEKVFAVQAV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32616
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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A4J0P1 | MGIRLKAHGKINLTLDVLDRRPDGYHEVEMIMQSISLHDVLEIEEQSKEISLTVSGISVTAEEDNLVLKAARLLQQVAGTGAGAKIHLQKNIPVAAGLAGGSTDAAATLKGLNALWGLGLSQEQLRQLATQLGADVPFCLAGGTAIARGIGEKLTTLEPAPPFGIILVKPSFGVSTAEVYQGLRLEHLGKRPNTEAMVKALKERDLGQVARELANVLESVTLRMHPKLEQIKEILRQIGCTGVLMSGSGPTVFGLTENREKAAELISGLPQAGCHVLAAWMV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29982
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q72BQ8 | MNDAVTLRSGCKVNLDLHITSRRDDGYHEIDSLFLPLEEPHDELVVTVGDAPGITVTCAIQGIDPTRNTVTRAYDAYAEASGFRPPLRVELRKGVPHGAGLGGGSANAAAILNHLESIAPHPLGRETLCRLAARIGADVPFFIHAVPCRASGIGEIITPVAWPYKGFTLLLACPQVQVSTAWAYGALDAAEEKQLRVRGCLTTGGVADRNSFSRESWLHNSFEPVVFASHPELRSLKEALLRHGAAAALMSGSGASVFALFRRREDAEAAFEQLKGHGIRVYQHLL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30819
Sequence Length: 286
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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A2BWR1 | MTKLSTTKICVKSPAKINLHLEIIGKREDGYHELAMIMQNIDLFDYIEFENNQIGDIELKSNNKDLSLKDDNLIIKAANYVKDISKKKDLGANIFLKKNIPIGAGLAGGSSNAAATIIGLNKLWDLDLDNETMLSLSSKLGSDVPFFINGGCQFCFGRGEILENYNSKFDYGVILLKNPNISISTADTYKKYSKEYCSNFLTESEKTNDIRNDLRINGFNDLNSSNQIIKVKNDLQIIVEKENDSVKKALYLLSNLQNCLSFSMSGSGPTCFALFKDINKANEVFEQNHKMFNNNGFEAWVCKLINSGITFL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 34941
Sequence Length: 312
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
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Q46L57 | MVPSKANEDFLIANAHAKINLHLEVLGIRSDGFHELAMVMQSINLSDQLKMIKRVDNTINLKSNNKEISNGDDNLIIKAAKLLRNKVENQELGVDIELEKNIPIGAGLAGGSTDAAATLLGLNKLWKLNLKIDELENLSKEIGSDIPFCISGGRQICFGRGEILEKLKFDQIQLGLVLVKDPSIQVSTPVAYKKYKEQFGESYLEDDRDFEIKRNSIRSIDWSDQSLFDNRKEIQNDLQKSIRPMTPEVEKSLNLLSSLPDSRLVSMSGSGPSCFALFQNYDQANKVLKEHVNEFERAGLSAWACSMMSNGVELRNEFT | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 35688
Sequence Length: 319
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
|
P42805 | MSVRLSLPAPAKLNLFLHILGRRDDGYHELQTLFQFLDHGDELHFEARQDGQVRLHTEIAGVPHDSNLIVRAARGLQEASGSPQGVDIWLDKRLPMGGGIGGGSSDAATTLLALNHLWQLGWDEDRIAALGLRLGADVPVFTRGRAAFAEGVGEKLTPVDIPEPWYLVVVPQVLVSTAEIFSDPLLTRDSPAIKVRTVLEGDSRNDCQPVVERRYPEVRNALILLNKFVSARLTGTGGCVFGSFPNKAEADKVSALLPDHLQRFVAKGSNISMLHRKLETLV | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30843
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
EC: 2.7.1.148
|
Q9CAK8 | MATSSTQLLLSSSSLFHSQITKKPFLLPATKIGVWRPKKSLSLSCRPSASVSAASSAVDVNESVTSEKPTKTLPFRIGHGFDLHRLEPGYPLIIGGIVIPHDRGCEAHSDGDVLLHCVVDAILGALGLPDIGQIFPDSDPKWKGAASSVFIKEAVRLMDEAGYEIGNLDATLILQRPKISPHKETIRSNLSKLLGADPSVVNLKAKTHEKVDSLGENRSIAAHTVILLMKK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP. Is essential for chloroplast development.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 24812
Sequence Length: 231
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Subcellular Location: Plastid
EC: 4.6.1.12
|
Q5NYK0 | MKAPFRIGQGFDVHALVPGRALIVGGVHIPFERGLLGHSDADVLLHALTDALLGAAGLGDIGRLFPDTDAAHAGADSRVLLREAFAAVRAAGFGVVNVDATVICRAPRILPHAPAMVANIAADLGIDAAAVNIKGKTTEKLGFTGRGEGIAAQVVALLMRHGDET | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Mass (Da): 16909
Sequence Length: 165
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
EC: 4.6.1.12
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