ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P49587 | MDSSNYFHDCKTMLSEHNESIESSNNDINGKQKEHIKKGNSENQDVDPDTNPDAVPDDDDDDDDNSNDESEYESSQMDSEKNKGSIKNSKNVVIYADGVYDMLHLGHMKQLEQAKKLFENTTLIVGVTSDNETKLFKGQVVQTLEERTETLKHIRWVDEIISPCPWVVTPEFLEKYKIDYVAHDDIPYANNQKKKKKKKSKGKSFSFDEENEDIYAWLKRAGKFKATQRTEGVSTTDLIVRILKNYEDYIERSLQRGIHPNELNIGVTKAQSIKMKKNLIRWGEKVTDELTKVTLTDKPLGTDFDQGVENLQVKFKELFKIWKNASNKLITDFTRKLEATSYLTSIQNIIDYEIENDDYASSNFDDETSS | Function: Controls phosphatidylcholine synthesis.
Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 42630
Sequence Length: 370
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
EC: 2.7.7.15
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O74975 | MGEEGIKINDTHKRRIDEVEPSEKEDNVERQTKKYNFEIDEPEEQEKKDEKEDDKEESPSKSLEEISQSVSPVEEEPRDVRFKELSTPFSYPINDPPEGRPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITPEFLEEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARGVNRKELNVSLFKKNELDLRHHIKVLRDTLRNHWVSTTRDLKADIKSFLSMATTDYQLQKNPLHGSSEPSSPGPTGFLGGINRWMQRRSSSHYDLPRVGNEIAASSSSATEENH | Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 41751
Sequence Length: 362
Subcellular Location: Nucleus
EC: 2.7.7.15
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P13259 | MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNELKKQNQRQRKQNFLDDPFTRKLIREASPATEFANEFTGENSTAKSPDDNGNLFSQEDDEDTNSNNTNTNSDSDSNTNSTPPSEDDDDNDRLTLENLTQKKKQSAN | Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 49406
Sequence Length: 424
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Subcellular Location: Membrane
EC: 2.7.7.15
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Q55BZ4 | MSTTTNKKPIRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLTEEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDHLQNVSGEQTSPLGGVNPNVLHKQSPYTSLSHFLPTTRKIVQFSEGRSPKPNDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYKEVKHTEGLTATEIVKRIIDNRLQYEARNRKKEAKEINFIEQSN | Function: Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway.
Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 40301
Sequence Length: 360
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
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Q99447 | MIRNGRGAAGGAEQPGPGGRRAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKTEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLEAARQQAAQPLGERDGDF | Function: Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway . Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis .
Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 43835
Sequence Length: 389
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
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Q922E4 | MIRNGHGAASAAGLKGPGDQRIVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKPPHPTPAGDTLSSEVSSQCPGGQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKTEIVPDRDGSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLEATKQQEAPPGGEID | Function: Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway . Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis .
Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 45235
Sequence Length: 404
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
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Q9XT54 | MSAKDERAREILKGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSAEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV | Function: Promotes the release of prenylated target proteins from cellular membranes (By similarity). Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (By similarity). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (By similarity). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17362
Sequence Length: 150
Subcellular Location: Cytoplasm
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O43924 | MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV | Function: Promotes the release of prenylated target proteins from cellular membranes . Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location . Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E . Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17420
Sequence Length: 150
Subcellular Location: Cytoplasm
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Q9N2V9 | MGDRSGVGGEEGEKSVLGASAHSQAGRRQQHTPAARRGAQRAPAATAAAASRPVFAMRWCCGGSYSENGGGGGGSRGAPPTPLLTVAATSSSTAHDTFGPMQVKMLKTAVIVTEGTGESVLLDSLRASGWICTVSFPTQATSDVESICPLAVFIDLRVPHPSQIAKDVSSVSTEEVLIVSIAEKHISEKRRRALAQSNIIHHVTWNTRDVVLFDYVGRLANRIRALPALFAVLDETDQAVEICDEQRVVQYVNRAYENVTGCIRSEVIGQPESEMRRKSLPRARGEEERRRSCDWKFIRVPFANNSQFVYMKRSNTTGDTAAIFRDVSLKSLKSQTGGIEAPISEVLTMLRDVSARVDGEPAQTIKDAMKVLSSHELYAPSINRFRDADRIATQYYDGLIRLHHPARQRKRSVVDAHREKRGSHGERRRVSADVKNALENDNCWKFDILHLEKVSDHHALSQVGMKVFERWKVCDVLGCSDDLLHRWILSIEAHYHAGNTYHNATHAADVLQATSFFLDSPSVAVHVNESHAVAALLAAAVHDLDHPGRGNAYLINTRQSLAILYNDNSILENHHIALAFQLTLQHNANVNIFSSLSREEFIQMRHAMVEMVLATDISRHFEYLAKFNKMHVTDVPEEQRDTNSLTICDMLVKCADISNPAREWGLCQRWAHRIVEEYFEQTREEKEKGLPVTMEVFDRNTCNVPITQCGFIDMFAREAFATFTEFAKLGELSDQLESNYEKWKVMTSQWTPTHNTNLVL | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 84881
Sequence Length: 760
EC: 3.1.4.17
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P04085 | MRTLACLLLLGCGYLAHVLAEEAEIPREVIERLARSQIHSIRDLQRLLEIDSVGSEDSLDTSLRAHGVHATKHVPEKRPLPIRRKRSIEEAVPAVCKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACATTSLNPDYREEDTGRPRESGKKRKRKRLKPT | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).
Sequence Mass (Da): 24043
Sequence Length: 211
Domain: The long form contains a basic insert which acts as a cell retention signal.
Subcellular Location: Secreted
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P20033 | MRTWACLLLLGCGYLAHALAEEAEIPRELIERLARSQIHSIRDLQRLLEIDSVGAEDALETSLRAHGSHAINHVPEKRPVPIRRKRSIEEAVPAVCKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACATSNLNPDHREEETGRRRESGKNRKRKRLKPT | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB.
Sequence Mass (Da): 24102
Sequence Length: 211
Domain: The long form contains a basic insert which acts as a cell retention signal.
Subcellular Location: Secreted
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P13698 | MRIWAWILLLSVCCSYLSPSLGEEAEIPQELIERLAHSEIRSISDLQRLLDIDSVGGGEDASAANIRSQKHDFHHNRLVPEKRSVPSRRKRSVEEAVPAICKTRTVIYEIPRSQIDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRIHHRSVKVAKVEYVRKKPKLKEVLVRLEEHLECTCTANSNSDYREEETGFFTSPALVLTGRTRETGKKQKRKKLKPT | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).
Sequence Mass (Da): 25720
Sequence Length: 226
Domain: The long form contains a basic insert which acts as a cell retention signal.
Subcellular Location: Secreted
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Q9NRA1 | MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERIITVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYFPSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLIRYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSKVTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.
PTM: Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG.
Sequence Mass (Da): 39029
Sequence Length: 345
Subcellular Location: Cytoplasm
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Q9GZP0 | MHRLIFVYTLICANFCSCRDTSATPQSASIKALRNANLRRDESNHLTDLYRRDETIQVKGNGYVQSPRFPNSYPRNLLLTWRLHSQENTRIQLVFDNQFGLEEAENDICRYDFVEVEDISETSTIIRGRWCGHKEVPPRIKSRTNQIKITFKSDDYFVAKPGFKIYYSLLEDFQPAAASETNWESVTSSISGVSYNSPSVTDPTLIADALDKKIAEFDTVEDLLKYFNPESWQEDLENMYLDTPRYRGRSYHDRKSKVDLDRLNDDAKRYSCTPRNYSVNIREELKLANVVFFPRCLLVQRCGGNCGCGTVNWRSCTCNSGKTVKKYHEVLQFEPGHIKRRGRAKTMALVDIQLDHHERCDCICSSRPPR | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix (By similarity).
PTM: Activated by proteolytic cleavage. Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after Arg-247 or Arg-249 by urokinase plasminogen activator gives rise to the active form.
Sequence Mass (Da): 42848
Sequence Length: 370
Subcellular Location: Secreted
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Q05957 | MAPPNGTTNGETEVATQGSYTAVSTGRKTTMHRLIEEHGSVLMPGVQDALSAAVVEKTGFHAAFVSGYSVSAAMLGLPDFGLLTTTEVVEATRRITAAAPNLCVVVDGDTGGGGPLNVQRFIRELISAGAKGVFLEDQVWPKKCGHMRGKAVVPAEEHALKIAAAREAIGDSDFFLVARTDARAPHGLEEGIRRANLYKEAGADATFVEAPANVDELKEVSAKTKGLRIANMIEGGKTPLHTPEEFKEMGFHLIAHSLTAVYATARALVNIMKILKEKGTTRDDLDQMATFSEFNELISLESWYEMESKFKNFTPKAT | Cofactor: Binds 1 Mg(2+) ion per subunit. Can bind other divalent cations such as Mn(2+), Fe(2+) and Co(2+).
Function: Catalyzes cleavage of the C(2)-C(3) bond in oxaloacetate and in (2R)-alkyl malate derivatives to form oxalate and acetate, and alkyl carboxylates and R-ketocarboxylates, respectively.
Catalytic Activity: H2O + oxaloacetate = acetate + H(+) + oxalate
Sequence Mass (Da): 34180
Sequence Length: 318
EC: 3.7.1.1
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P77836 | MRMVDLIEKKRDGHALTKEEIQFIIEGYTKGDIPDYQMSALAMAIFFRGMNEEETAELTMAMVHSGDTIDLSRIEGIKVDKHSTGGVGDTTTLVLGPLVASVGVPVAKMSGRGLGHTGGTIDKLESVPGFHVEITNDEFIDLVNKNKIAVVGQSGNLTPADKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGVGAFMKDLNDAKALAKAMVDIGNRVGRKTMAIISDMSQPLGYAIGNALEVKEAIDTLKGEGPEDFQELCLVLGSHMVYLAEKASSLEEARHMLEKAMKDGSALQTFKTFLAAQGGDASVVDDPSKLPQAKYIIELEAKEDGYVSEIVADAVGTAAMWLGAGRATKESTIDLAVGLVLRKKVGDAVKKGESLVTIYSNREQVDDVKQKLYENIRISATPVQAPTLIYDKIS | Cofactor: Binds 1 K(+) ion per subunit.
Function: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.
Catalytic Activity: phosphate + uridine = alpha-D-ribose 1-phosphate + uracil
Sequence Mass (Da): 46332
Sequence Length: 433
EC: 2.4.2.2
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Q8CNH8 | MRMIDIIEKKRDGKSLTKEEIEFFVNGYTHEEVPDYQASSLAMAIFFQDMNDEERAALTMSMVNSGEKIDLSDINGIKVDKHSTGGVGDTTTLVLAPLVAAVGVPVAKMSGRGLGHTGGTIDKLESVKGFNVEISEKDFIKLVNDNQVAVIGQSGNLTPADKKLYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGSGAFMKTLDDAEALAHAMVRIGNNVGRNTMAIISDMSQPLGNAIGNALELKEAISTLKGNGPKDLTELVLTLGSQMVVLAEQATSLDEARQMLIDAIKTGKALNKFKTFLSNQGGDDSIVDSPEKLPSAKYQVEFKAKKDGYITEIIANEIGVASMMLGAGRQTKEDVIDLGVGIVLNKKVGEHVEKGENILTIHTNTKEIDDILYKLDNSITIESKGEAPTLIHKIITE | Cofactor: Binds 1 K(+) ion per subunit.
Function: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.
Catalytic Activity: phosphate + uridine = alpha-D-ribose 1-phosphate + uracil
Sequence Mass (Da): 46360
Sequence Length: 433
EC: 2.4.2.2
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Q6MNY2 | MDGDNKTYTIYILSDSTGETAATMIRAALVQYTTKDVNIIRCKNVRTDTQAEAVIEECFERRGMLAYTVASQGLRAKIREMASGKGIPYFDLLGPLLSTLDTFFGQHSEDTVGALRAVDERYFKRIEAIEYTVKHDDGKTFAELDKADIVLVGISRTSKTPLSIFLSHKGWKVANVPLVLDTPLPEELFKIDQRRIVGLIIDMDSLQRIRKSRLEKFGQDPGGSYASMSHIAKEIEYAEKIFKVNRRWPVFNVTERALEETASEIVRIIAARLGLPDSVIF | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31643
Sequence Length: 281
EC: 2.7.11.32
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Q9AC59 | MGPFGARASPEAGQVVKQPLTDDPQESLAQGESERLPPRFATYFHIHLVSDSTGETLNAMARAVCARFTDILPIEHIYALVRSTRQLDRALEEIAGAPGVVMHTIVDPGLRAALEEGCRKLEMPCIAALDPVISAMSRYLGARISTRVGAQHALTNDYFDRIEALDYAIAHDDGQGGQDLTQADVILVGVSRTSKTPTCIYLAHRGVRAANVPLVPGRPPPPELFELKNTLIVGLITSPDRLIQIRRNRLLSLKENRESDYVDADAVRQEIIAARRLFERQNWPVIDITRRSVEETAAAVINLLSGGRGKVEVLG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 34495
Sequence Length: 315
EC: 2.7.11.32
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A9WG10 | MSDQPVSQTAPPLYIVSGGAGAVGEQVARLTLSQFEGAEVPLIIIPNVRDLSQIAEVVERAAHQNGTILHTLMEPSLRRELMRLARERGVAEIDLVGSVLSRLATVLRKEPLGKPGLYQPRRSAYFERLDAIEYTVAHDDGNKPHELHQADIVLVGISRVGKTPLSMYLAVLGWKVANVPLVREVPLPAELFQVDPRRVIGLIVEAEQITARRRWRQRRMGVSIGGNYTSLDAAYDEVEWARRTFRQHGWTTINVTDKSIEESADEIITLISRRFSQLP | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]
Sequence Mass (Da): 31182
Sequence Length: 279
EC: 2.7.11.32
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Q940L5 | MTLESYAGDVHTVPQSENSMEERGGGELFVPPLNFAMVDNGIFRSGFPEPVSFSFLQSLRLKSIIYLCPEAYPEVNREFAKSNGIQVFQFGIERCKEPFVNIPDEVIREALQVLLDTENHPVLIHCKSGKHRTGCLVGCVRKIQRWCLSSIFDEYQRFAAAKARISDQRFMELFDISNLKHTPLSFSCSKRYTNTIDY | Function: Probable tyrosine-protein phosphatase that acts as negative regulator of defense responses against the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 22640
Sequence Length: 198
EC: 3.1.3.48
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P80093 | MPQIGLVSAVNLRVQGNSAYLWSSRSSLGTDSQDGCSQRNSLCFGGSDSMSHRLKIRNPHSITRRLAKDFRPLKVVCIDYPRPELDNTVNYLEAAFLSSSFRSSPRPTKPLEIVIAGAGLGGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDDDGDWYETGLHIFFGAYPNMQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEALPAPLNGILAILKNNEMLTWPEKVKFAIGLLPAMLGGQSYVEAQDGISVKDWMRKQGVPDRVTDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVEHIESKGGQVRLNSRIKKIELNEDGSVKCFILNDGSTIEGDAFVFATPVDIFKLLLPEDWKEIPYFQKLEKLVGVPVINVHIWFDRKLKNTSDNLLFSRSPLLSVYADMSVTCKEYYDPNKSMLELVFAPAEEWVSRSDSEIIDATMKELAKLFPDEISADQSKAKILKYHVVKTPRSVYKTVPGCEPCRLLQRSPVEGFYLAGDYTKQKYLASMEGAVLSGKLCAQAIVQDYELLVGRSQRKLAETSVV | Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis.
Catalytic Activity: 15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65062
Sequence Length: 582
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Plastid
EC: 1.3.5.5
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Q40406 | MSIVGLVSVVCPSGGIKKRYFSKGLDNFQGFRSSECLGIQLQVPVPFYSGIRQSPRATSLQVVCKDCPRPELEGAVNFLEAAQLSASFRSSPRPEKGLEVVVVGAGLAGLSTAKYLADAGHKPILLESRDVLGGKIAAWKDKDGDWYETGLHIFFGAYPNVQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEVLPAPLNGIWAILRNNEMLTWPEKVRFAIGLLPAMVGGQAYVEAQDGLTVTEWMRRQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHIQSLGGRAQLNSRLQKIELNPDGTVKHFVLGNGNIITGDAYVVAAPVDILKLLLPQEWREIPYFQKLDKLVGVPVINVHIWFDRKLKNTYDHLLFTRSPLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWISRSDSEIIERTMKELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTNQKYLASMEGAVLSGKLCAQSIVQDYELLVRRSKKASTAEMTVV | Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis.
Catalytic Activity: 15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63791
Sequence Length: 570
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Plastid
EC: 1.3.5.5
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A2XDA1 | MDTGCLSSMNITGTSQARSFAGQLPTHRCFASSSIQALKSSQHVSFGVKSLVLRNKGKRFRRRLGALQVVCQDFPRPPLENTINFLEAGQLSSFFRNSEQPTKPLQVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKIAAWKDEDGDWYETGLHIFFGAYPNIQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPETLPAPLNGIWAILRNNEMLTWPEKVKFALGLLPAMVGGQAYVEAQDGFTVSEWMKKQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHVRSLGGEVRLNSRIQKIELNPDGTVKHFALTDGTQITGDAYVFATPVDILKLLVPQEWKEISYFKKLEKLVGVPVINVHIWFDRKLKNTYDHLLFSRSSLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWVGRSDTEIIEATMQELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTKQKYLASMEGAVLSGKLCAQSVVEDYKMLSRRSLKSLQSEVPVAS | Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis. Active with decylplastoquinone (DPQ) as substrate . Also active with other benzoquinones, which are strongly preferred over naphthoquinones as substrates .
Catalytic Activity: 15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64770
Sequence Length: 578
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Plastid
EC: 1.3.5.5
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P26294 | MRVAIAGAGLAGLSCAKYLADAGHTPIVYERRDVLGGKVAAWKDEDGDWYETGLHIFFGAYPNMLQLFKELNIEDRLQWKSHSMIFNQPTKPGTYSRFDFPDIPAPINGVAAILSNNDMLTWEEKIKFGLGLLPAMIRGQSYVEEMDQYSWTEWLRKQNIPERVNDEVFIAMAKALNFIDPDEISATVVLTALNRFLQEKKGSMMAFLDGAPPERLCQPIVEHVQARGGDVLLNAPLKEFVLNDDSSVQAFRIAGIKGQEEQLIEADAYVSALPVDPLKLLLPDAWKAMPYFQQLDGLQGVPVINIHLWFDRKLTDIDHLLFSRSPLLSVYADMSNTCREYEDPDRSMLELVFAPAKDWIGRSDEDILAATMAEIEKLFPQHFSGENPARLRKYKIVKTPLSVYKATPGRQQYRPDQASPIANFFLTGDYTMQRYLASMEGAVLSGKLTAQAIIARQDELQRRSSGRPLAASQA | Function: This enzyme converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene. Also active with phytofluene and 1,2-epoxyphytoene as substrates.
Catalytic Activity: 15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53296
Sequence Length: 474
Pathway: Carotenoid biosynthesis; lycopene biosynthesis.
Subcellular Location: Cell membrane
EC: 1.3.5.5
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Q10177 | MSSQSYYMNDLDDLRSLESSTLNKKDTAINELNPEQNDTRRSTDLLLEDKYGIQTGFSKYWKKCTYGIREYCKFIGPGFLIAVAYIDPGNYSTDLDAGSRFQYKLLFIVFLSNLFAVYLQSLCIRLGSVTGMDLARNCREHYNRYICWSFYVLAEIAIIATDIAEVIGTAVALKILMHIPLVAGVVITILDVLLVLIAWRPEGSMLSVRIFETAVALLVLVVAISFAVVLGRVHIGGAGTVFKGFLPSSTVFSREGLYSSIGILGATVMPHSLFLGSGLVQTRLRDLDVRRGNYTPVGDCSDYRPTHETIKHSLTYSIVEVALSLFTFALFTNSSILIVAGAVFYNTSGADTSDLFSIYDLLKEYVSISCGRLFAVALLFSGMSAGYVCTIAGQIVSEGYINWNLRPWLRRVITRAIAIIPCLVVSAAVGQSGLNQVLNASQVCLSILLPFLTFPLVMFTCSRKVMRVVSDSTNEETGQLIRETHDYSLGWTMTIVTWAIWLFLTALNLLLIVWLGMGVSF | Function: Transports manganese ions into the cell. Regulates cell morphogenesis through control of manganese homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57641
Sequence Length: 521
Subcellular Location: Endoplasmic reticulum membrane
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P9WGM2 | MTGPTTDADAAVPRRVLIAEDEALIRMDLAEMLREEGYEIVGEAGDGQEAVELAELHKPDLVIMDVKMPRRDGIDAASEIASKRIAPIVVLTAFSQRDLVERARDAGAMAYLVKPFSISDLIPAIELAVSRFREITALEGEVATLSERLETRKLVERAKGLLQTKHGMTEPDAFKWIQRAAMDRRTTMKRVAEVVLETLGTPKDT | Function: Member of the two-component regulatory system PdtaR/PdtaS. This two-component system plays an essential role in mycobacterial adaptation to poor nutrient conditions. PdtaR probably acts at the level of transcriptional antitermination rather than transcriptional initiation.
PTM: Phosphorylated and activated by PdtaS.
Sequence Mass (Da): 22669
Sequence Length: 205
Domain: Contains a C-terminal ANTAR domain, which is a RNA binding domain.
Subcellular Location: Cytoplasm
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A0QTP6 | MSTLGDLLAEHTMLPGSAVDHLHAVVGEWQMLSDLSFADYLMWVRRDDGVLVCVAQIRPNTAPTVLLADSVGKLAGPDDLPVVTMAFESGAIGRGSDKAGQGSRTRPGLDVEAVPVRHQGQVVAVLTHQTALAERRLTSPLEGAYLDCANDLLHMLAEGTFPNIGDLAMSRSSPRVGDGFIRLNEGGEVVFASPNAISAYHRMGLNSELDGHNLVAITRPLISDPFEAQELANHIRDSLAGGSSMRMEVDANGAAILLRTLPLVAGGKSLGAAVLIRDVTEVKRRDRALLSKDATIREIHHRVKNNLQTVAALLRLQARRTSNEEAREALIESVRRVTSIALVHDALSMSVDEEVNLDQVVDRILPIMNDVASVDTPIRINRVGNLGVLDADRATALIMVITELVQNAIEHAFDAKTEQGCVTIKAERSARWLDVVVHDDGRGLPVGFSLEKSDRLGLQIVRTLVTAELDGSLGMHDVPSGGTDVVLRVPIGRRSRGAQ | Function: Member of the two-component regulatory system PdtaR/PdtaS. This two-component system plays an essential role in mycobacterial adaptation to poor nutrient conditions. Nutrient deprivation results in increasing intracellular concentrations of cyclic diguanosine monophosphate (c-di-GMP), which binds to the PdtaS sensor and promotes its autophosphorylation, leading to the activation of the signaling cascade. The phosphate group is then transferred to PdtaR.
PTM: Autophosphorylated.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 53695
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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P9WGL4 | MSTLGDLLAEHTVLPGSAVDHLHAVVGEWQLLADLSFADYLMWVRRDDGVLVCVAQCRPNTGPTVVHTDAVGTVVAANSMPLVAATFSGGVPGREGAVGQQNSCQHDGHSVEVSPVRFGDQVVAVLTRHQPELAARRRSGHLETAYRLCATDLLRMLAEGTFPDAGDVAMSRSSPRAGDGFIRLDVDGVVSYASPNALSAYHRMGLTTELEGVNLIDATRPLISDPFEAHEVDEHVQDLLAGDGKGMRMEVDAGGATVLLRTLPLVVAGRNVGAAILIRDVTEVKRRDRALISKDATIREIHHRVKNNLQTVAALLRLQARRTSNAEGREALIESVRRVSSIALVHDALSMSVDEQVNLDEVIDRILPIMNDVASVDRPIRINRVGDLGVLDSDRATALIMVITELVQNAIEHAFDPAAAEGSVTIRAERSARWLDVVVHDDGLGLPQGFSLEKSDSLGLQIVRTLVSAELDGSLGMRDARERGTDVVLRVPVGRRGRLML | Function: Member of the two-component regulatory system PdtaR/PdtaS. This two-component system plays an essential role in mycobacterial adaptation to poor nutrient conditions. Nutrient deprivation results in increasing intracellular concentrations of cyclic diguanosine monophosphate (c-di-GMP), which binds to the PdtaS sensor and promotes its autophosphorylation, leading to the activation of the signaling cascade. The phosphate group is then transferred to PdtaR.
PTM: Autophosphorylated.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 54012
Sequence Length: 501
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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A1AY86 | MSANDRAIETLRREIAKLQTDGAAIARKDAGIRAKLASAMAAQAKAKTAPALRLKQAEASRLEKELMATSKSQADIATKIAKKQSSLSAKLVVQANEAKKADAKAKKNQERVSKTQEEATRKLEAGYRKLTLENQSLEQRLQRELSAMKPTAGPTTNADLTSAPPHDIFISHAWEDKADFVEALAHTLRAAGAEVWYDDFSLRPGDSLRRSIDKGLGSSRFGIVVLSTHFFKKEWPQKELDGLFQLESSGRSRILPIWHKVSKDEVASFSPTMADKLAFNTSTKSVDEIVADLMAIIRD | Function: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide.
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 32902
Sequence Length: 299
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
EC: 3.2.2.6
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C0QBU5 | MTDNRPVIGITMGDPVGIGPEIIVSALDDPFVYTVCRPLVLGDEGVMERAIDLKSARMDVHTTDTPAGGKYCHGTMDIVPLSRLDAATLLAGHPTPGTGKAMIDYITTGVDLAMDGKIQAIATCPITKTAMKLAGSKFHGHTELIADRTHTPRVAMMMAGDRLRVVLVTIHIPLCEVSARLNQAEILATISLTSETLKTKFGIPEPRIAVAGLNPHGGEDGMFGSEELEIIAPAVEQARSKGITVSGPFPPDTLFFNAANHKFDAVVCMYHDQGLIPFKMIHFSDGVNTTLGLPIIRTSVDHGTAYDIAWRGTADPSSLIAAIKMAALQATITGANRINR | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH
Sequence Mass (Da): 36215
Sequence Length: 340
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.262
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C5BR49 | MKIVVDENIPLADALFGDLGEIIRKPGREISSADVAEADALLVRSVTRVNADLLTGSKVKFVGTCTIGTDHLDKEFLAEAGIRFASAPGCNAQGVVQYDLAALAHLGYLARDIRVGIIGCGNVGGSLHRALTGMGVTCVCYDPFLTQDQNADLADWDALFTCDVICVHTPLTRSGPYPTHHMLSTPFFRAMRDGALLLNAGRGEVIDNRALKAYLQGDNSNHLSVVLDVWEGEPAIDAELAPLVKIATPHIAGYSFEGKTNGSLMIYEALAEFLGVNATERSARVAAVKAQAYGAAEPLDADDLVTAILATHPITRDDKALRDQLDQLPAGFDALRKGYPVRREFSHYQLTSAQIPANVTALGFSLDSAK | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 39575
Sequence Length: 370
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q9KQ92 | MKILIDENMPYAQALFSQLGEVILKPGRTLTADDLIDVDALMIRSVTKVNDALLAKANRLKFVGTATAGMDHVDQALLRERGIFFTAAPGCNKVGVAEYVFSVLMVLAQQQGFSVFDKTVGIIGAGQVGSYLAKCLSGIGMKVLLNDPPKQAQGDEREFTELETLLKQADVITLHTPITRGGEWPTHHLIDAAILEQLRSDQILINAARGPVVDNAALKARLQQGDGFTAVLDVFEFEPQVDMELLPLLAFATPHIAGYGLEGKARGTTMIFNSYCEFLGSAHCANPASLLPKAPVPKVYLERAWDEETLRTLTQIIYDVRKDDAQFRREIHQPGAFDLMRKHYWDRREYSAVTLAGGADCHLAPLAKLGFQVEVCDEPTI | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 41865
Sequence Length: 381
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q8D2P6 | MKILIDNNIIFSYSLFKKIGKVNLINSIDINAKNISGFDALIIKSSTNVNENLLKNSNIKFIGSATSGKDHVDVDWLKKNKINFDFAPGCNSVAVAEYVFSSMLYFAYRDKFSLLKKTVGIVGFGNIGKCLNKKLSAIGVKTILCDPILEEKNNIKLKSLNEIVQNSDIITLHVPLTYSGKYPTWHLINKKILLDLKDNCILINTSRGSVIDNNSLLNILKEGKPIRVVLDVWENEPLICSKLLSLIDIGTPHIAGHSLEGKIKGTISIFNSLCNFVGKKNKKYFISSFIDPYEIEYISMKGRIDQSKIYLLSLLSNNILYDDHELRKNFNKKNCFVNLRNSYRKRREWSSLFIKSNNILFSNLLNKIGFNSKFFKEK | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42967
Sequence Length: 378
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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A1JL55 | MKILVDENMPYAEALFQQLGDVQAVPGRPIPLDALAGADALMVRSVTKVNEALLQGTSIRFVGTATAGTDHVDDNWLQQQGIGFSAAPGCNAIAVVEYVFSALMMMAERDGFQLRDKTVGIIGVGNVGSRLNARLQALGVRTLLCDPPRADRGDNERFWPLEKLVREADVLTFHTPLNKNGPYQSLHMADDELLAALPDGRILINACRGAVVDNTALLRALEKGKKLSVVLDVWEPEPELSLPLLARVDIGTPHIAGYTLEGKARGTTQVFEAFSQYLGQPQSVELASLLPQPEFSQLRLNGELDEGKLKRLMHLVYDVRRDDAPLRRVADQSGEFDRLRKHYQERREWSSLCVQCDDAASAELLQKLGFSTQLL | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 41323
Sequence Length: 375
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 1.1.1.290
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Q0ARD7 | MSDDKLIPATPDADAYAKTADANAAEIFDRDEPFALFADWLTEAKKKEPNDANAMALATADASGLPDVRMVLLKDVDADGFVFYTNLESGKGGQLADNPQAALCFHWKSLRRQVRVRGAVEPVSAGEADAYFASRARDSRIGAWASKQSRPLESRFALEKSVAREAARFGLGEVPRPPHWSGFRIRPLSLEFWRDRPFRLHDRMFFDRPDLGSTWTVTRLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24863
Sequence Length: 222
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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O33065 | MAGPDDQHLSGMRVEYGSVEKDGSPDLDTDWLYDGWLTLFCKWIDDAERAGVAEPNAMVLATVANGRPVSRSVLCKGADEAGIIFFTNYDSDKGDDLAATPYASVTFPWYQLGRQVHIRGPVSTVDPQVSEDYWSKRPRGSQLGAWASHQSRPIASRTALLDQLLEVTVRFADSELIPLPPNWGGYLIVPEVVEFWQGRENRVHNRIRVTGGCIERLQP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24388
Sequence Length: 219
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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A1TF46 | MGTSDYLARMRVEYGSVEKDGSSDLDVDWLGPDPATGWVTLLHQWMAEAEQAGAAEPNAMVVATVDDRGRPVTRTVLCKSVDASGVSFYTNYDSEKGRQLAAAPYASATFPWYLVGRQVHVHGAVTKVSAEETADYWSKRPRGSQLGAWASQQSLPIASRAALMQQLTEVTERFADVEEIPVPPHWGGYLIAAEVVEFWQGRENRVHNRIRVCGGQVERLQP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24506
Sequence Length: 222
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q8PI89 | MTDLYAEALATFAALYAEAQNSAELEASAMTVATANVDGRPSARTVLLKAFDARGFVFYTHLDSAKGRDLQTHPQAALLFLWRSLREAGIQVRIEGGVQLVSADESDAYFASRPRMSQIGAWASRQSQALGSREEFDAAIAKVEATFAGREVPRPDGWGGFRVVPQAFEFWYGAKFRLHERWRYEADAASHWSKRMLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 22200
Sequence Length: 199
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
EC: 1.4.3.5
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Q31AB8 | MATLGVNIDHIANVRQARKTVEPDPVQFAFLAELGGADSITVHLREDRRHIQDRDVFLLKETIKTKLNLEMAATEEMLEIAKKTLPDYVTLVPEKREEVTTEGGLDLKSNAQYLKNFVENLKHSNIEVSAFIDPLGEQINYSKEIGFDFIELHTGKYAELSGSEQYKELQRIIESTHLANDLGLVVNAGHGLNYNNVKKIASINNMNELNIGHSIVARALAIGLEKSVREMKSLITSN | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 26638
Sequence Length: 238
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
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Q7V6Q5 | MASLGVNIDHIANVRQARQTVEPDPVPMALLAELGGADGITVHLREDRRHIQDRDLDLLRATVRSRLNLEMAATAEMVGIALKIQPDMVTLVPERRQEVTTEGGLDVAAQQGSLKGMVDQLQVAGIPVSLFVDPVSQQLEAAFKSGARWVELHTGAYAEACWADQSFELARLTEATARARSLGLRVNAGHGLTYQNVEAVAAIEGIEELNIGHTIVARSIAVGLKEAVREMKRLVQNPRREPLFG | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 26648
Sequence Length: 245
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
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Q02HS5 | MTEATRILLGVNIDHVATLRQARGTRYPDPVKAALDAEEAGADGITVHLREDRRHIQERDVRVLKEVLQTRMNFEMGVTEEMLAFAEEIRPAHSCLVPERREELTTEGGLDVAGQEQRIRDAVRRLAAVGSEVSLFIDPDPRQIEASARVGAPAIELHTGRYADAEDPEEQARELQRVREGVALGRSLGLIVNAGHGLHYHNVEPVAAIDGINELNIGHAIVAHALFVGFRQAVAEMKALMLAAATKR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate
Sequence Mass (Da): 27260
Sequence Length: 248
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.6.99.2
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Q5YTE0 | MSAPAAEPQAAPSRPTIGVLALQGDVREHLAALRACGAEPVLVRRVGELEAVDGLVLPGGESTAISKLLQVFDLLDPLRARLRDGMPAFGSCAGMILLASEVLDTRPDAQHLSGIDMTVRRNAFGRQVDSFETDLDFAGLDDGPVRAVFIRAPWVERAGDGVQVLATVPDGPSRGRIVAVRQGNVLATSFHPEVTGDLRVHRMFVDIVRAAGDRAGNVHTPDVQPT | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 23992
Sequence Length: 226
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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A1R728 | MTNPLSDASSRVGSGLRIGVLALQGDFREHIHAVEAAGATGVGIRRPSELDDIDGLIIPGGESTTIDKLSRIFEVRDPLQKRIAEGLPVYGSCAGMILLADEIADPATDLDGNPQQTFGGLDITVRRNAFGRQRESFETDLDFKGLDFSAGESGVDPVHAVFIRGPWVERVGSGVEVLAQVDPDHASHTATLHGVARIVAVRSGQLLATSFHPEVTGEKRVHELFIRMIRGEA | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 24967
Sequence Length: 233
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q6MEN7 | MLIGILALQGDFFKHQEMLHSLGIETIQVKTRNELDFCDALIIPGGESTVMMRQLETTNLKELLVHFAIHKPVFGTCAGLILMSSHVQNSAMMPLGLLHIAVERNAFGRQVDSFQVDVSVYLKPGDEICFPAFFIRAPRIRTSETPVQILASYEGEPILVRQGHHLGASFHPELTVNPSIHLYFLEMVKENLENHKK | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 22159
Sequence Length: 197
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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Q6L1R3 | MKIGVLGIQGDVYEHYTAIRPLKNKYKVEAYIIRSPEEINEMDGIIIPGGESTTITRFLSRYINIINENVRNGMKIMGTCAGAIILSKDTGDPRVHGTGIMDIKIQRNAYGRQIDSFIDAVNIKNIGTFNAVFIRAPVIDDPGKTSVLGEYNGKPVIVENENAIAMTFHPELTGDLRVHEYFLRKVMGN | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 21042
Sequence Length: 189
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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A9WSE8 | MTIGRTLRAGVLALQGDVREHLAALEACGAEAVPIRRASELADLDGLVLPGGESTAIDRLIRAFELSEPLKAFIASGKPVYGSCSGMILLADRIADPALDRDGAPQRTLGGLDVTVRRNAFGRQRDSFETELKFDSLSDSERPVHAVFIRAPWIEQAGSEVEVLAVVRIEGIDRAVAVRSGNLLATSFHPEVLVQESETSELRVHELLVSMMASRLSQDANQAESRK | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Sequence Mass (Da): 24540
Sequence Length: 227
Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
EC: 4.3.3.6
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L0T5T4 | SFAGAEAANASQLQSIARQVRGAVNAVAGQVTGNGGSGNSGTSAAAANPNSDNTASIADRGTSAIMTTASATASSTGVDGGIAATYAVASQWDGGYVANYTITQFGRDFDDRLAVAIHFA | Function: Together with PE9, induces macrophage apoptosis through human Toll-like receptor 4 (TLR4) signaling pathway. Interaction with TLR4 leads to increased levels of phospho-IRF-3, increase in the transcript levels of IFN-beta and pro-apoptotic genes, up-regulation of IL-10, down-regulation of IL-1b and enhanced levels of macrophage apoptosis.
Sequence Mass (Da): 11763
Sequence Length: 120
Domain: The C-terminal domain is required for interaction with TLR4 but not with PE9.
Subcellular Location: Secreted
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Q79FR5 | MSFVTTRPDSIGETAANLHEIGVTMSAHDDGVTPLITNVESPAHDLVSIVTSMLFSMHGELYKAIARQAHVIHESFVQTLQTSKTSYWLTELANRAGTST | Function: Involved in cell wall lipids remodeling and in virulence . Restricts the biofilm growth and is essential for the optimal intracellular survival of M.tuberculosis . Shows esterase activity with a preference for short-chain esters, particularly pNP-acetate (C2) and pNP-butyrate (C4) . Has weaker activity with pNP-octanoate (C8), pNP-laurate (C12) and pNP-myristate (C14) . Shows weak long-chain triacylglycerol (TAG) hydrolase activity in vitro . Not necessary for PPE17 stability or for its localization on the mycobacterial surface .
Catalytic Activity: an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+)
Sequence Mass (Da): 10872
Sequence Length: 100
Subcellular Location: Secreted
EC: 3.1.1.6
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P36497 | MWTQKWHKYYTAQVDENDCGLAALNMILKYYGSDYMLAHLRQLAKTTADGTTVLGLVKAAKHLNLNAEAVRADMDALTASQLPLPVIVHVFKKNKLPHYYVVYQVTENDLIIGDPDPTVKTTKISKSQFAKEWTQIAIIIAPTVKYKPIKESRHTLIDLVPLLIKQKRLIGLIITAAAITTLISIAGAYFFQLIIDTYLPHLMTNRLSLVAIGLIVAYAFQAIINYIQSFFTIVLGQRLMIDIVLKYVHHLFDLPMNFFTTRHVGEMTSRFSDASKIIDALGSTTLTLFLDMWILLAVGLFLAYQNINLFLCSLVVVPIYISIVWLFKKTFNRLNQDTMESNAVLNSAIIESLSGIETIKSLTGEATTKKKIDTLFSDLLHKNLAYQKADQGQQAIKAATKLILTIVILWWGTFFVMRHQLSLGQLLTYNALLAYFLTPLENIINLQPKLQAARVANNRLNEVYLVESEFSKSREITALEQLNGDIEVNHVSFNYGYCSNILEDVSLTIPHHQKITIVGMSGSGKTTLAKLLVGFFEPQEQHGEIQINHHNISDISRTILRQYINYVPQEPFIFSGSVLENLLLGSRPGVTQQMIDQACSFAEIKTDIENLPQGYHTRLSESGFNLSGGQKQRLSIARALLSPAQCFIFDESTSNLDTITEHKIVSKLLFMKDKTIIFVAHRLNIASQTDKVVVLDHGKIVEQGSHRQLLNYNGYYARLIHNQE | Function: Involved in the export process of the bacteriocin pediocin PA-1/AcH. Is also essential for pediocin production.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81652
Sequence Length: 724
Subcellular Location: Cell membrane
EC: 3.4.22.-
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P36955 | MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP | Function: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
PTM: The N-terminus is blocked. Extracellular phosphorylation enhances antiangiogenic activity.
Sequence Mass (Da): 46312
Sequence Length: 418
Domain: The N-terminal (AA 44-121) exhibits neurite outgrowth-inducing activity. The C-terminal exposed loop (AA 382-418) is essential for serpin activity.
Subcellular Location: Secreted
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Q5P5I4 | MTQRLKDKLAVITGGANGIGRAIAERFAVEGADIAIADLVPAPEAEAAIRNLGRRVLTVKCDVSQPGDVEAFGKQVISTFGRCDILVNNAGIYPLIPFDELTFEQWKKTFEINVDSGFLMAKAFVPGMKRNGWGRIINLTSTTYWLKIEAYTHYISTKAANIGFTRALASDLGKDGITVNAIAPSLVRTATTEASALSAMFDVLPNMLQAIPRLQVPLDLTGAAAFLASDDASFITGQTLAVDGGMVRH | Function: Catalyzes the NAD-dependent stereospecific oxidation of (S)-1-phenylethanol to acetophenone in the degradation of ethylbenzene.
Catalytic Activity: (S)-1-phenylethanol + NAD(+) = acetophenone + H(+) + NADH
Sequence Mass (Da): 26662
Sequence Length: 249
EC: 1.1.1.311
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Q9UBV8 | MASYPYRQGCPGAAGQAPGAPPGSYYPGPPNSGGQYGSGLPPGGGYGGPAPGGPYGPPAGGGPYGHPNPGMFPSGTPGGPYGGAAPGGPYGQPPPSSYGAQQPGLYGQGGAPPNVDPEAYSWFQSVDSDHSGYISMKELKQALVNCNWSSFNDETCLMMINMFDKTKSGRIDVYGFSALWKFIQQWKNLFQQYDRDRSGSISYTELQQALSQMGYNLSPQFTQLLVSRYCPRSANPAMQLDRFIQVCTQLQVLTEAFREKDTAVQGNIRLSFEDFVTMTASRML | Function: Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats . In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification . Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium . Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 . Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity).
PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30381
Sequence Length: 284
Subcellular Location: Cytoplasm
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Q641Z8 | MASYPDGQSYPGAAGQVPGPHPGGYYPGPPHGGGQYGSGFPPGGYGAPAPGGPYGYPSAGGTPSGTPGGPYGGGPPGGPYGGGPPGGPYGQAHPSPYGTQPPGPYGQGGVPPNVDPEAYSWFQSVDADHSGYISLKELKQALVNSNWSSFNDETCLMMINMFDKTKTGRIDVVGFSALWKFLQQWKNLFQQYDRDHSGSISSTELQQALSQMGYNLSPQFTQLLVSRYCTRSAIPAMQLDCFIKVCTQLQVLTEAFREKDTAVQGNIRLSFEDFVTMTASRML | Function: Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats. In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification. Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium. Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (By similarity). Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 .
PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30012
Sequence Length: 283
Subcellular Location: Cytoplasm
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Q5PQ53 | MASYPYGQGYHGAAGQPPGAPQTNYYGGQQYGGGVQPAASYGRPAPGAPYGSPPSGGVYGHPVPGSAAPGAPGGPYGGQAPGGPYSVPGSTPYGSQQHGSYGQGAPAGNIPPGVDPEAFSWFQTVDTDHSGYISLKELKQALVNTNWSSFNDETCTMMMNMFDKSNSGRIDMFGFSALWRFIQQWRNLFQQYDRDRSGSINQGELHQALCQMGYQLSPQFVQIVMSRYAQRSAQPGLQLDRFIQICTQLQSMTEAFREKDTGQIGTAKLSYEDFITMTTTRLL | Function: Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Acts as a negative regulator of ER-Golgi transport (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30533
Sequence Length: 283
Subcellular Location: Cytoplasm
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P53238 | MCAKKLKYAAGDDFVRYATPKEAMEETRREFEKEKQRQQQIKVTQAQTPNTRVHSAPIPLQTQYNKNRAENGHHSYGSPQSYSPRHTKTPVDPRYNVIAQKPAGRPIPPAPTHYNNLNTSAQRIASSPPPLIHNQAVPAQLLKKVAPASFDSREDVRDMQVATQLFHNHDVKGKNRLTAEELQNLLQNDDNSHFCISSVDALINLFGASRFGTVNQAEFIALYKRVKSWRKVYVDNDINGSLTISVSEFHNSLQELGYLIPFEVSEKTFDQYAEFINRNGTGKELKFDKFVEALVWLMRLTKLFRKFDTNQEGIATIQYKDFIDATLYLGRFLPH | Function: Calcium-binding protein that is required for polar bud growth and cell wall abscission. Can also bind zinc ions.
Sequence Mass (Da): 38342
Sequence Length: 335
Domain: Binds calcium via its EF-hands.
Subcellular Location: Cytoplasm
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Q7YRH6 | MTRLLGYVDLSEPHFVAAVLAIVFNPLFWNVVARWEHKTRKLSKAFGSPRLACYTLGGAILLLNVLRSHCFTQAMLSQPRMQSLDNPAVYHVGLALLGVGGVFVLSSFLALGFTGTFLGDYFGILKEARVTMFPFSVLDNPMYWGSTAIYLGWAIVHASPTGLLLTALVALIYMVAIVYEEPFTAEIYQQKASQAYKRS | Function: Catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22018
Sequence Length: 199
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
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Q9UBM1 | MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTILLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYEEPFTAEIYRQKASGSHKRS | Function: Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure . Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step . Responsible for approximately 30% of hepatic PC with the CDP-choline pathway accounting for the other 70% (Probable).
PTM: Isoform 2 is N-glycosylated with high-mannose oligosaccharides.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22134
Sequence Length: 199
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum
EC: 2.1.1.17
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Q61907 | MSWLLGYMDPTEPSFVAAVITIVFNPLFWNVVARWEQRTRKLSRAFGSPHLACYSLGICILLLNILRSHCFTQAMMSQPKMEGLDNHTTYFLGLAFLGWGFVFVLSSFYALGFTGTFLGDYFGILKESRVTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVLVAIVYVVALLYEEPFTAEIYRQKATRLHKRS | Function: Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure (Probable). Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step .
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22579
Sequence Length: 199
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
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P83918 | LSLLGHDERVTPEPFDSVTAQNARGNQADVQSLPR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Has manganese peroxidase activity.
Catalytic Activity: 2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+)
Sequence Mass (Da): 3819
Sequence Length: 35
EC: 1.11.1.13
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Q9FY84 | MEATRSDDPSLNPIRNRNPNPNPNPNPLSTIISSAQVWPTIDGPLGLTEEASVDYARRFYKFGFALLPWLWFVNCFYFWPVLRHSRAFPQIRNYVVRSAIGFSVFTALLSAWALTFSIGGEQLFGPLYDKLVMYNVADRLGLSGLA | Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16489
Sequence Length: 146
Subcellular Location: Membrane
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Q9U357 | MDISKLTDVKKVDLCKKYFLIGACFLPLVWIVNTFWFFSDAFCKPINAHRRQIRKYVIASIVGSIFWIIVLSAWEIFFQHYRAQGLVWTDFLTFVFPTGRV | Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch (glp-1 or lin-12). It may represent a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11943
Sequence Length: 101
Subcellular Location: Endoplasmic reticulum membrane
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Q8JHF0 | MNLERIPNEEKLSLCRRYYLGGFAFLPFLWLVNILWFFKEAFLKPAYTEQPQIKSYVKKSALGLLLWVAVLTTWITVFQHFRAQWGEVGDYLSFTIPLGTA | Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11851
Sequence Length: 101
Subcellular Location: Endoplasmic reticulum membrane
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Q54BR1 | MLIPEDDKLDDEKMINIAKKLWFIGFFFLPWVWLINILYFIPYRNSLNDKVKWYLKFSLIGFLGYSTIFMGWMGIYLVNRNKWGAFGDDISITIPFG | Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11585
Sequence Length: 97
Subcellular Location: Endoplasmic reticulum membrane
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Q86BE9 | MDISKAPNPRKLELCRKYFFAGFAFLPFVWAINVCWFFTEAFHKPPFSEQSQIKRYVIYSAVGTLFWLIVLTAWIIIFQTNRTAWGATADYMSFIIPLGSA | Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch. It probably represents the last step of maturation of gamma-secretase, facilitating endoproteolysis of presenilin and conferring gamma-secretase activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11725
Sequence Length: 101
Subcellular Location: Membrane
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Q9NZ42 | MNLERVSNEEKLNLCRKYYLGGFAFLPFLWLVNIFWFFREAFLVPAYTEQSQIKGYVWRSAVGFLFWVIVLTSWITIFQIYRPRWGALGDYLSFTIPLGTP | Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) . The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12029
Sequence Length: 101
Subcellular Location: Endoplasmic reticulum membrane
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Q9X4A7 | MVLPNFKENLEKYAKLLVTNGINVQPGHTVALSIDVEQAELAHLLVKEAYALGAAEVIVQWSDDTINRERFLHAEMNRIEEVPAYKKAEMEYLLEKKASRLGVRSSDPDAFNGVAPERLSAHAKAIGAAFKPMQVATQSNKVSWTVAAAAGKEWAKKVFPNASSDEEAVDLLWNQIFKTCRVYEKDPVRAWKEHADRLDAKARILNEAQFSALHYTAPGTDLTLGLPKNHVWESAGAINAQGESFLPNMPTEEVFTAPDFRRAYGYVSSTKPLSYNGNIIEGIKVTFKDGEIVDITADQGEKVMKNLVFNNNGARALGECALVPDSSPISQSGITFFNTLFDENASNHLAIGAAYATSVEGGADMTEEELKAAGLNRSDVHVDFIIGSNQMNIDGIHHDGSRVPIFRNGDWVI | Cofactor: Binds 2 divalent metal cations per subunit (By similarity). Can use cobalt, zinc, and possibly also magnesium ions .
Function: Exhibits a high specificity towards peptides possessing arginine or aromatic amino acids at the N-terminus. Could be involved both in bacterial growth by supplying amino acids.
Sequence Mass (Da): 45318
Sequence Length: 413
EC: 3.4.11.-
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Q21219 | MGYSESRSESVSSKGKTSYGHELETVPLPEKKIYTTWPDMIRHWPKTTLCIVSNEFCERFSYYGMRTVLTFYLLNVLKFTDSQSTIFFNGFTVLCYTTPLLGSIVADGYIGKFWTIFSVSILYAIGQVVLALASTKNFQSSVHPWMDLSGLLIIAFGTGGIKPCVSAFGGDQFELGQERMLSLFFSMFYFSINAGSMISTFISPIFRSQPCLGQDSCYPMAFGIPAILMIVATLVFMGGSFWYKKNPPKDNVFGEVSRLMFRAVGNKMKSGSTPKEHWLLHYLTTHDCALDAKCLELQAEKRNKNLCQKKKFIDDVRSLLRVLVMFLPVPMFWALYDQQGSVWLIQAIQMDCRLSDTLLLLPDQMQTLNAVLILLFIPLFQVIIYPVAAKCVRLTPLRKMVTGGLLASLAFLITGFVQLQVNTTLPTLPEEGEASISFWNQFETDCTITVMSGIHKRVLPHDKYLHEDKKNKSGIYNLFTTKSPAKGNGDWTLTYDLSYDGACGDTSKLEKTVKVTAKSKKIIYVGVGSFGYYQNTANTDKPTDGTGEFSMGIVTVFNSSYGGNFAMCRQNTSDFDVNHPCNPRHPADFYFWETDYNSHTDDRDQNATITGSLSSQPAVTYKQKSVKPGYWQLYYLLNTPKDVDRQTYNKTATLVAPTNYGFHRVKQGGVFIYALTGTYENPKIHELQIVQSNSVSILWQIPQIVVITAAEILFSITGYEFAYSQSAPSMKALVQALWLLTTAAGDSIIVVITILNLFENMAVEFFVYAAAMFVVIAIFALLSIFYYTYNYYTTDEEDGEIGVDDEEEIEDHNPRYSIDNKGFHPDEKDTFDMHF | Function: Low-affinity peptide transporter that is necessary for proton-dependent uptake of di- or tripeptides, and to a minor extent tetrapeptides, in the intestine. Transport is independent of sodium and chloride ions. Controls the uptake of dietary fatty acids, plays a role in fatty acid synthesis and is responsible for dipeptide-induced acidification of the intestine. Regulates cellular pH differences together with the antiporter protein, nhx-2. Amino acid uptake and absorption levels influence the insulin signaling/daf-2 and let-363/TOR pathways, subsequently affecting the stress response and longevity of the organism. It is required for the uptake of the L-enantiomers of various amino acids, including L-glutamate . In response to the availability of amino acid nutrients, may play a role in promoting reproduction and fertility .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94109
Sequence Length: 835
Subcellular Location: Apical cell membrane
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P16312 | TQACRINSGNVPSELDLRSLRTVTPIRMQG | Function: Thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues.
Catalytic Activity: Broad endopeptidase specificity.
Sequence Mass (Da): 3314
Sequence Length: 30
Subcellular Location: Secreted
EC: 3.4.22.65
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P08176 | MKIVLAIASLLALSAVYARPSSIKTFEEYKKAFNKSYATFEDEEAARKNFLESVKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVIL | Function: Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues.
PTM: N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites.
Catalytic Activity: Broad endopeptidase specificity.
Sequence Mass (Da): 36104
Sequence Length: 320
Subcellular Location: Secreted
EC: 3.4.22.65
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P91679 | MASEITNGKNGQNGKNGQKEESDSQIAPPIPYPKSVAFIISNEFCERFNYYGMRTILVLYLTNKLGYNEETATVLFHTFTMLVYIFPLIGALIADGWLGKYKTILYLSLVYSLGAMVVSFGAVPLSGMPTKAVTVVGLLLIAIGTGGIKPCVSAFGGDQFSLPAQSFQLAKFFSLFYFAINAGSLISTTFTPILRADVHCFGDQDCFSLAFGVPAILMIFSVIIFMAGKRLYRCQPPAGNMIFGVSRCIADAFKGWQKRRHSEPMESFLDYAKPTVGSRMVQETKCLGRILRLFLPFPVFWALFDQQGSRWTFQATRMDGNVLGFQIKPDQMQVVNPLLILGFLPLFDYIIYPALARCGIRRPLQKLTLGLLLAALGFFLSAGLEMKMEQAAYRATPIEPDMTHLRIYNGMPCRYEISSAVVQTPRVIEPLNVWEDLSLQMTESKEYTFNAQPVSGECPSIIDKLRLQPGKSVSYFLAQDKLVEFADGLQMAATDTGRTSVRALLNTPDGEGPVLLSTESATSQEPPLTLDKGNVPQLHRITPGFARVDINGKKVASFEAKEGRLYSILVTGSARDGYQHNVIEVVALSTVSILWQLPQIVVMTAAEVMFSVTGLEFSYSQSPPSMKSVLQACWLLSVAIGNMLVVVIAEFKFTSSQSGEFTLFASLMLVDMMIFLWLARSYQYKDQREDFEDDDDATIDSVMQSKPKATTVDTTARKTNGIEAEPGYGAYRNHAYDNDFSEA | Function: Important role in absorption of dietary peptides. High-affinity transporter of alanylalanine. Dipeptide transport activity is proton dependent.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82245
Sequence Length: 743
Subcellular Location: Membrane
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Q17758 | MGASHLHDDPRPGSPVDHQPTTWGGIIKKWPKQTFLIVGNELCERFSFYGMRAVLTLYFFNILNFSQSFSTVLFHAFTVICYSSPLLGSILADGYIGKFWTIFFISIFYACGQILLAFSSIAPSGSSHHPLLDLLGLLIVGLGTGGIKPCVSAFGGDQFPAHYTRMISLFFSMFYFSINAGSLISMWLTPYFRSMSCFGHDSCYPLAFGIPAILMIVATLVFMAGSFWYKKVPPKENIIFKVIGTITTALRKKASSSSTHQRSHWLEYSLDGHDCALSTECKNLHGNCAQRRYIEDIKRLFRVIVMMIPVPMFWALYDQQGSTWVLQAVGMDAKVFGFEILPDQMGVLNAFLILFFIPIFQSIVYPTIEKLGFQMTMLRKMAGGGILTAVSFFVCGIVQLFVNPTLPYIPMANEAHLTIINTIPSCDFNVLIDSREPFDLLRKSGIAPDDSVRKPISFTGDDFFQPNITFDNLAPNCPKFTAEPMLAPATSYVLTLSPNGWAYNAVRPEKPKSGKGELSMGLNLIVPCDKIPSNVTWEQCNGTEGYSGAIALCKVESDVITDNNNVCDPTAKGKFYVLSNANPLDVHDFSKKSTVTAFGRTYSPIEMKPGTYRLFYTDDSRTHFTPLNLPPVQQDHMGGQYLITVSTRSKNDSEVLATTESLVSYNRVSILWQIPQYVILTAGEVLFSITGLEFAYTEASPQLKSVVQALWLFTTAIGDLIVVVIFMLNIFSDVAVQMFVFGGIMLFVIFVFILLAVFYYEYADYSNESEVLTEKMIVDDDHTRI | Function: Proton-dependent uptake of di- or tripeptides, and to a minor extent tetrapeptides. Transport is independent of sodium and chloride ions. Protein shows high affinity to peptide substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87567
Sequence Length: 785
Subcellular Location: Membrane
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O01840 | MEEKSLLQKLRSYPPAVFFMLGNEFCERFSFYGMKTILFIYLITEHEFSPSKATFIYHLFTCIAYLTPLIGSIMADSVFGRFKVILYGSSIYVVGHVLLSLGAVPFLSYPIRSSLDFSGLFVIAFATGCIKPCVSAFAADQFTEDQKDLRSQFFSFFYFAINGGSLFAIIITPILRGRVQCFGNAHCFPLAFGVPGVLMLLALILFLMGWSMYKKHPPSKENVGSKVVAVIYTSLRKMVGGASRDKPVTHWLDHAAPEHSQKMIDSTRGLLNVAVIFCPLIFFWALFDQQGSTWVLQARRLDGRVGHFSILPEQIHAINPVCVLILVPIFEGWVYPALRKITRVTPLRKMAVGGLLTAFSFAIAGVLQLKVNETMEFPPSLGRIYLQRVGNESLISDFRYKSDGRLIGDGMLPKGRTELDAGIYTFNTGLKNESQEIDISTPNKGYVMAVFRLKDAVEVVKFDYKVEKTDNGATRVFVVTAREDADTLVYAINKKGKILSSCELKSGSYVDVIPGIISDPNVRLYWGPKNSCSGVDCPNTVTLNAQMGAVHVLHIHPSTTEGDFNLLVRPNSVSILWSLPQYIIITLGEVLLSVTGLEFAYSQAAPNMKSVLTAMWLLTVFAGNLIDMMISGTRLIPHPALEFFFYSTLMVIVMGVFILLAMQYTYVEDNDDEITITESEKKDVIALTEIESGTATSDKKE | Function: Neuron-specific, H(+)-coupled oligopeptide transporter with broad specificity towards di- and tripeptides in a Na(+) and Cl(-)-independent manner. Shows H(+) channel activity in the absence of peptide substrates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77967
Sequence Length: 701
Subcellular Location: Membrane
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A0KIP7 | MDTLLERFLRYVTFHTRSDATNPACPSSEGQLVFARALCDEMQQMGLSRVTLDEYGYLTACLPGNQPDAPAIGLIAHMDTADYEAAHVVPQIIENYQGGDICLGKGDEVLAIRDYRFLKNYLGQDLITTDGSTLLGADDKAGIAEILTAIDHLLAHPEIPRGDVWVGFTPDEEIGRGADRFPLDRFPAKWAYTVDGGELGELEYENFNAAGATVRFIGNNVHPGTAKGSMINSQTLAARFHAAMPTEQTPEATDGYQGFFHLAQMNGTVEETCLHYIIRDFDDEGFAARKAQLKERVASLQLEAPRARIELTLTDSYRNMRSQIEPHMHIVELAKAAMQAADVTPRIKPIRGGTDGARLSFMGLPCPNLFTGGHNFHGKHEFIPLQSMEKAVTTLVELVRLTSAWRG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 44840
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 3.4.11.4
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Q7MDF5 | MKHLVQRFIRYVTFDTQSNPKKKCCPSTSGQMKFAEHLKQELLDLGLSQVELDEHGYLMAKLPSNVAYPVPAIGFIAHMDTAPDASGKNVKPQIIEDYHGGDIALGIGDEVLSPVQYPELHALHGHNLITTDGTTLLGADNKAGIAEILSAIEMLIENPSIPHGDICIGFTPDEEIGRGADLFNVERFGAEWAYTIDGGPQGELEYENFNASSADVIFHGVSVHPGTAKDKMVNAMTLASQFHCRMPADETPETTEGYQGFYHLKSAEMGVARSELGYILRDFERDGIARRKAFMQSLADDMNTQLKHGSVEIRFTDSYYNMKEKVEPFPHVIELAKQAMEVCDVEPIIKPIRGGTDGARLSFMGLPCPNIFTGGYNFHGIHEFASIEQMEKSVQVIVKIAELTAKKYA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45152
Sequence Length: 409
Subcellular Location: Cytoplasm
EC: 3.4.11.4
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A0A2R9TD79 | MQTSTNTPGGRTFFGHPYPLSGLFLSEMWERFSFYGIRPLLILFMAATVFDGGMGLPREQASAIVGIFAGSMYLAALPGGLLADNWLGQQRAVWYGSILIALGHLSIALSAFFGNDLFFIGLVFIVLGTGLFKTCISVMVGTLYKPGDARRDGGFSLFYMGINMGSFIAPLLSGWLLRTHGWHWGFGIGGIGMLVALLIFRGFAIPAMKRYDAEVGLDSSWNKPTNQRQGVGRWVTAIMAVVVVIIALISQGVIPINPVMIASLLVYVIAASVTLYFIYLFAFAKMSRKDRARLLVCFILLVSAAFFWSAFEQKPTSFNLFANDYTDRMVMGFEIPTVWFQSINALFIILLAPVFSWAWPALAKKKIQPSSITKFVIGILCAAAGFAVMMYAAQHVLSSGGAGVSPLWLVMSILLLTLGELCLSPIGLATMTLLAPDRMRGQVMGLWFCASSLGNLAAGLIGGHVKADQLDMLPTLFARCSIALVICAAVLILLIVPIRRLMNNTQGQQTA | Function: Mediates the proton-dependent uptake of dipeptides. Shows higher affinity for dipeptides with a negatively charged amino acid residue at the N-terminal position, such as Asp-Ala and Glu-Ala. Also displays specificity for Ala-Ala, Ala-Tyr and Tyr-Ala.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55499
Sequence Length: 511
Subcellular Location: Cell inner membrane
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Q43731 | MVVVNKTNLLLLLLSLCLTLDLSSAQLRRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLAGDGFDTVIKAKEALDAVPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQQGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAFN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 36076
Sequence Length: 329
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9FLC0 | MASNKLISILVLVVTLLLQGDNNYVVEAQLTTNFYSTSCPNLLSTVQTAVKSAVNSEARMGASILRLFFHDCFVNGCDGSILLDDTSSFTGEQNAAPNRNSARGFNVIDNIKSAVEKACPGVVSCADILAIAARDSVVALGGPNWNVKVGRRDARTASQAAANSNIPAPTSSLSQLISSFSAVGLSTRDMVALSGAHTIGQSRCTNFRARIYNETNINAAFATTRQRTCPRASGSGDGNLAPLDVTTAASFDNNYFKNLMTQRGLLHSDQVLFNGGSTDSIVRGYSNNPSSFNSDFTAAMIKMGDISPLTGSSGEIRKVCGRTN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34215
Sequence Length: 324
Subcellular Location: Secreted
EC: 1.11.1.7
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Q42578 | MAVTNLPTCDGLFIISLIVIVSSIFGTSSAQLNATFYSGTCPNASAIVRSTIQQALQSDTRIGASLIRLHFHDCFVNGCDASILLDDTGSIQSEKNAGPNVNSARGFNVVDNIKTALENACPGVVSCSDVLALASEASVSLAGGPSWTVLLGRRDSLTANLAGANSSIPSPIESLSNITFKFSAVGLNTNDLVALSGAHTFGRARCGVFNNRLFNFSGTGNPDPTLNSTLLSTLQQLCPQNGSASTITNLDLSTPDAFDNNYFANLQSNDGLLQSDQELFSTTGSSTIAIVTSFASNQTLFFQAFAQSMINMGNISPLTGSNGEIRLDCKKVNGS | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34989
Sequence Length: 335
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9FG34 | MAVTSSSSTCDGFFIISLIVIVSSLFGTSSAQLNATFYSGTCPNASAIVRSTIQQALQSDARIGGSLIRLHFHDCFVNGCDGSLLLDDTSSIQSEKNAPANANSTRGFNVVDSIKTALENACPGIVSCSDILALASEASVSLAGGPSWTVLLGRRDGLTANLSGANSSLPSPFEGLNNITSKFVAVGLKTTDVVSLSGAHTFGRGQCVTFNNRLFNFNGTGNPDPTLNSTLLSSLQQLCPQNGSNTGITNLDLSTPDAFDNNYFTNLQSNNGLLQSDQELFSNTGSATVPIVNSFASNQTLFFEAFVQSMIKMGNISPLTGSSGEIRQDCKVVNGQSSATEAGDIQLQSDGPVSVADM | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 37290
Sequence Length: 358
Subcellular Location: Secreted
EC: 1.11.1.7
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Q96509 | MDIRSDDAKKPMMMWFLGMLLFSMVAESNAQLSENYYASTCPSVELIVKQAVTTKFKQTVTTAPATLRMFFHDCFVEGCDASVFIASENEDAEKDADDNKSLAGDGFDTVIKAKTAVESQCPGVVSCADILALAARDVVVLVGGPEFKVELGRRDGLVSKASRVTGKLPEPGLDVRGLVQIFASNGLSLTDMIALSGAHTIGSSHCNRFANRLHNFSTFMPVDPTMDPVYAQQLIQACSDPNPDAVVDIDLTSRDTFDNSYYQNLVARKGLFTSDQALFNDLSSQATVVRFANNAEEFYSAFSSAMRNLGRVGVKVGNQGEIRRDCSAFN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 35859
Sequence Length: 330
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9LXG3 | MAALKMTISCFLFLQVIYCLLSSFAPTNVQGLKVGFYDKACPKAELIVKKSVFEAVKNDRTIAAPLLRMFFHDCFVRGCEGSVLLELKNKKDEKNSIPNLTLRGFEIIDNVKAALEKECPGIVSCSDVLALVARDAMVALNGPSWEVETGRRDGLVTNITEALLNLPSPFNNISSLITQFQSKGLDKKDLVVLSGGHTIGNGHCPQITNRLYNFTGKGDSDPNLDTEYAVKLRGKCKPTDTTTALEMDPGSFKTFDESYFKLVSQRRGLFQSDAALLDNQETKSYVLKSLNSDGSTFFKDFGVSMVKMGRIGVLTGQVGEVRKKCRMVN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 36225
Sequence Length: 329
Subcellular Location: Secreted
EC: 1.11.1.7
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Q43729 | MMKGAKFSSLLVLFFIFPIAFAQLRVGFYSQSCPQAETIVRNLVRQRFGVTPTVTAALLRMHFHDCFVKGCDASLLIDSTNSEKTAGPNGSVREFDLIDRIKAQLEAACPSTVSCADIVTLATRDSVALAGGPSYSIPTGRRDGRVSNNLDVTLPGPTISVSGAVSLFTNKGMNTFDAVALLGAHTVGQGNCGLFSDRITSFQGTGRPDPSMDPALVTSLRNTCRNSATAALDQSSPLRFDNQFFKQIRKRRGVLQVDQRLASDPQTRGIVARYANNNAFFKRQFVRAMVKMGAVDVLTGRNGEIRRNCRRFN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34098
Sequence Length: 313
Subcellular Location: Secreted
EC: 1.11.1.7
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Q39034 | MKTQTKVMGGHVLLTVFTLCMLCSGVRAQLSPDIYAKSCPNLVQIVRKQVAIALKAEIRMAASLIRLHFHDCFVNGCDASLLLDGADSEKLAIPNINSARGFEVIDTIKAAVENACPGVVSCADILTLAARDSVVLSGGPGWRVALGRKDGLVANQNSANNLPSPFEPLDAIIAKFVAVNLNITDVVALSGAHTFGQAKCAVFSNRLFNFTGLGNPDATLETSLLSNLQTVCPLGGNSNITAPLDRSTTDTFDNNYFKNLLEGKGLLSSDQILFSSDLAVNTTKKLVEAYSRSQSLFFRDFTCAMIRMGNISNGASGEVRTNCRVINN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 35023
Sequence Length: 328
Subcellular Location: Secreted
EC: 1.11.1.7
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P85351 | VALGGCLPTVQLGR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 1384
Sequence Length: 14
Subcellular Location: Secreted
EC: 1.11.1.7
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P86003 | MGDISPLTGTNGQIR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 1560
Sequence Length: 15
Subcellular Location: Secreted
EC: 1.11.1.7
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P86058 | YLGPTADSTMDQTFANN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 1846
Sequence Length: 17
EC: 1.11.1.7
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A7QEU4 | MSSKRVTWLSLTWVLVFLCLSVELEAQLQVGFYRTSCGLAEFIVKDEVRKGFIRDSGVAPGLVRMHFHDCFVRGCDGSVLIDSTPSNTAEKDSPANNPSLRGFEVIDSAKARLEAVCKGVVSCADIVAFAARDSVEITGGLGYDVPAGRRDGRISLASEASTNLPPPTFTVDQLTQFFSNKGLTQDEMVTLSGAHTIGRSHCSSFSNRLYNFNGTSGQDPTLDPQYAASLKTQCPQGSTNTNLVVPMNPSSPSITDVGYYVDVLRNRGLFTSDQTLLTDTTTATQVRQNAGNPFLWKNKFASAMVKMGQLGVLIGEAGQIRANCRVINS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 35525
Sequence Length: 329
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9FMR0 | MAVKISTIEVLILSLALLSFGHGCYGQLRLGFYSQNCQNVENIVSKVVGEAFIKDSSIAPAMIRLYFHDCFSNGCDASLLLDGSNSEKKASPNLSVRGYEVIDDIKSAVEKECDRVVSCADIIALATRDLVTLASGGKTRYEIPTGRLDGKISSALLVDLPSPKMTVAETAAKFDQRKLSLNDMVLLLGGHTIGVTHCSFIMDRLYNFQNTQKPDPSMDPKLVEELSAKCPKSSSTDGIISLDQNATSSNTMDVSFYKEIKVSRGVLHIDQKLAIDDLTSKMVTDIANGNDFLVRFGQAMVNLGSVRVISKPKDGEIRRSCRSTCNNPLCV | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 36016
Sequence Length: 331
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9FLV5 | MQFVNFFPLLALVVISLAGKATVEAATGLNPPVKLVWHYYKLTNTCDDAETYIRYQVEKFYKNDSSIAPKLLRLLYSDCMVNGCDGSILLQGPNSERTAPQNRGLGGFVIIDKIKQVLESRCPGVVSCADILNLATRDAVHMAGAPSYPVFTGRRDGGTLNADAVDLPSPSISVDESLAYFKSKGLDVLDMTTLLGAHSMGKTHCSYVVDRLYNFKNTGKPDPTMNTTLVSQLRYLCPPRTQKGQTDPLVYLNPDSGSSNRFTSSYYSRVLSHNAVLRVDQELLNNDDSKEITQEFASGFEDFRKSFALAMSRMGSINVLTGTAGEIRRDCRVTNANDGA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress (Probable). The enzyme activity has to be proved.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 37312
Sequence Length: 340
Subcellular Location: Secreted
EC: 1.11.1.7
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Q9FKA4 | MGLVRSFALVIVFLSCLIAVYGQGTRIGFYSTTCPNAETIVRTTVASHFGSDPKVAPGLLRMHNHDCFVQGCDGSVLLSGPNSERTAGANVNLHGFEVIDDAKRQLEAACPGVVSCADILALAARDSVSLTNGQSWQVPTGRRDGRVSLASNVNNLPSPSDSLAIQQRKFSAFRLNTRDLVTLVGGGHTIGTAACGFITNRIFNSSGNTADPTMDQTFVPQLQRLCPQNGDGSARVDLDTGSGNTFDTSYFINLSRNRGILQSDHVLWTSPATRSIVQEFMAPRGNFNVQFARSMVKMSNIGVKTGTNGEIRRVCSAVN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 34134
Sequence Length: 319
Subcellular Location: Secreted
EC: 1.11.1.7
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B7Z031 | MTSRTRHCARLGIVLLGICCIASGIYLFRNWIDMFTRMRGQEMALSPNSRSFEGWKVSPLPLDFDIYLFNWTNPDDFYVGSNKKPHFEQLGPYRFREKPDKVDIEWHNHNASVSFHKKSWFYFDAAGSNGSLWDKVTTVNSVAHSAARRAAVDWFARTGVNIANKLYRQGVTITKTVDEMLFKGYEHPFISVGKLLRPQDVPYKRIGYHYPRNGSSEFDGDINMFTGADDIAKMGQIHTWNNLTHTGAFEGTCGQVHGSMGEFFPPNLGTKDTVYMYMPKMCRAIPLDYVETVTVHGVTAYKFSGTRHAVDNGTLYPDTRCYCVGGKCMPSGVINIGPCSFNASVYMSFPHFYMADPSYLEAIEGLRPEREKHEFFMALEPNAGVPMDVGGGFQANYYMEPIPGITLYENVPTVMIPMMWCEERVRVSEEIAADIALVPLIVLLGQIVTGILLAGGLICTCWYPTRQVTHFCHSDPKAKASVLRPLNAFGVNSSAATAPVAQLFRNNISSSGNERVGVRLLDYNRDSGIRLESGTMESSHRERLISEDSPDVVVR | Function: (Microbial infection) Plays a role in mycobacterial infection. Mediates infection by M.fortuitum and uptake of M.smegmatis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62252
Sequence Length: 555
Subcellular Location: Cell membrane
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P10834 | MKASSKAIKLVLDHLKSTGRVLGSVESGNSATISEKTASVNKQQQLQEKKPSVLQYRSYNPYLVKEDFLSILPENLYKKRGQFTNELDFQLMKVRDPKYFQFKDQYYLFFNDYNSLTEYIKLTKHSRINKIRVKMTPLAQPLPTLLTKLQRYSKNLYNAFRSSEQYFEGLNEKVDVSGEFTTNQLRSILDSVEEIENKSVLVWNIPTKLRSHDILNYFWFYNIRSSFKIYWDDEMKRNLRFISFENSHDAYRFKRNYHGLLAKELLTLSEKGDAADYSLEMDDSKILIEHLSE | Function: Activator of specific mitochondrial mRNAs. PET54 is involved in the excision of intron aI5-beta from pre-mRNA for cytochrome c oxidase I (COX1) and plays a role in promoting the translation of COX3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34637
Sequence Length: 293
Subcellular Location: Mitochondrion inner membrane
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Q82W83 | MRMIKFLLLAILLAPFVAHSSGQEVKLDKAPIDRADKESLQRGAKGFVEYCLTCHGANFMRFNRHHDIGMSEDDIRADLIHTGQKTGDLMEAAMRKKEAEGWFGVVPPDLSVIARARGADWLYTYLRTFYQDTSTYSGWNNLIFDKVAMPHVLHHLQGWQVLEPGTGNLVQTKPGTMTKEEYDRFVADLVNYMVYLGEPHAPYRRELGITVLLFLFGMLGLTYLLKKEYWRDIH | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Part of the ammonia monooxygenase complex, which catalyzes the oxidation of ammonia to hydroxylamine, the first reaction in the process of ammonia oxidation to nitrite.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26870
Sequence Length: 234
Subcellular Location: Cell membrane
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B0C0E7 | MAKILKQPDLSDPQLKEKLKKGMGHNYYGEPAWPNDLLYIFPVVIMGTISLVIGLAVLDPAMIGEPSNPFATPLEILPEWYLYPVFQILRTVPSKLLGVLIQTTIPLGLMLIPFIENVNKFQNPFRRPIATSVFLFSVVFTLWLGIGATLPIDKSLTLGLF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17981
Sequence Length: 161
Subcellular Location: Cellular thylakoid membrane
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Q06SK2 | MAVIKKPDLSDPVLKMKLAKGMGHNYYGEPAWPNDLLYIFPVCIFGTFAIVIGLSVMEPAAMGEPANPFATPLEILPEWYFYPVFQLLRVIPNKLLGVLLMAAVPAGLLTVPFIENINKFQNPFRRPIATTVFLLGTVVAVYLGIGSTFPIDQSLTLGLF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17599
Sequence Length: 160
Subcellular Location: Plastid
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Q2JTN9 | MPVSKQVIATEAITRKVDLDNPKVLAKLKKNMGHMTYGEPAWPNDLLFMFPVVILGTIGVIVGLAVMDPAGVGEPADPFATPLEILPEWYLYPAFHILRIAPNKLLGIALMSAIPVGLLFVPFIENVNKFQNPLRRPVATTVFLIGTLVTLYLGIGATLPLDKWVTLGLF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18573
Sequence Length: 170
Subcellular Location: Cellular thylakoid membrane
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P28057 | MSIMKKPDLSDPKLRAKLAQNMGHNYYGEPAWPNDILFTFPICIAGTIGLITGLAILDPAMIGEPGNPFATPLEILPEWYLYPVFQILRVLPNKLLGIACQGAIPLGLMMVPFIESVNKFQNPFRRPVAMAVFLFGTAVTLWLGAGACFPIDESLTLGLF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17537
Sequence Length: 160
Subcellular Location: Cellular thylakoid membrane
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A0T0T7 | MSIIKKPDLTDPKLRAKLAKGMGHNYYGEPAWPNDLLYLFPVCILGTFACCIGLAVMAPTQMGEPADPFNTPLEILPEWYFFPTFNLLRVLPNKLLGVLAMAAVPAGLITVPFIENVNKFQNPFRRPIASLVFITGFIFAVWFGIGACLPIDKAVSLGYW | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17721
Sequence Length: 160
Subcellular Location: Plastid
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P0DX29 | MSALTSQPTSSGSSEKIPRLRGWRAKAAGVVLAALALTTGVAAPAPAAANPYERGPDPTTASIEATSGSFATSTVTVSRLAVSGFGGGTIYYPTTTTAGTFGALSIAPGFTATQSSIAWLGPRLASQGFVVFTIDTLTTSDQPDSRGRQLLASLDYLTQQSSVRSRIDSTRLGVVGHSMGGGGTLEAARSRPTLQAAVPLTAWDLTKNWSTLQVPTLVVGAQSDTVAPVASHSIPFYTSLPSTLDRAYLELRGASHFAPNSPNTTIAKYTLSWLKRFIDNDTRYEQFLCPIPSTSLSISDYRGNCPHNG | Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (By similarity). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) . Has a preference for medium chain length (C-4 to C-12) fatty acid esters . Active with p-nitrophenyl palmitate (p-NPP) as substrate . Hydrolyzes triacylglycerol substrates non-specifically with a preference for long, unsaturated fatty acyl chains with the highest activity for triolein . Substrates with cis-9 unsaturation are preferred over the saturated triacylglycerols . Hydrolyzes a wide range of natural oils, especially olive oil, with relatively high activity . Capable of catalyzing synthesis of the flavor ester isoamyl acetate by esterification of isoamyl alcohol using acetic acid as an acyl donor . Degrades synthetic aliphatic polyesters, namely poly(1,4-butylene succinate) extended with 1,6-diisocyanatohexane (PBSc-D) and poly(epsilon-caprolactone) (PCL) plastics . Does not degrade poly(lactic acid) (PLA) nor aromatic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world .
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 32377
Sequence Length: 309
Subcellular Location: Secreted
EC: 3.1.1.74
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