ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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D3DFG8 | MVKLILVRHAESEWNPVGRYQGLLDPDLSERGKKQAKLLAQELSREHLDVIYSSPLKRTYLTALEIAEAKNLEVIKEDRIIEIDHGMWSGMLVEEVMEKYPEDFRRWVEEPHKVEFQGGESLASVYNRVKGFLEEVRKRHWNQTVVVVSHTVPMRAMYCALLGVDLSKFWSFGCDNASYSVIHMEERRNVILKLNITCHLGEFYVEAHKAI | Function: Catalyzes the dephosphorylation of L-phosphoserine to serine and inorganic phosphate. Is poorly or not active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-nitrophenylphosphate, and fructose-6-phosphate. Does not display phosphoglycerate mutase activity.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 24556
Sequence Length: 211
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
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P0AFN1 | MSALFLAIPLTIFVLFVLPIWLWLHYSNRSGRSELSQSEQQRLAQLADEAKRMRERIQALESILDAEHPNWRDR | Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8763
Sequence Length: 74
Subcellular Location: Cell inner membrane
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D3DFP8 | MKRLYLVRHAQSEYNEKGIFQGRLDSDLTPLGFVQARLLAREFLKKKVDIIYSSPQRRAYKTALTISDMLGTQLVVDERLREMSFGEYEGKHFWSMLEAHKDVFLNWLSNPVKHPLPTQESMEEFEKRVRSFLEDVKSSHYQNMLIVAHGGTLHAIVCLLTGIGLENLWNIHMDNAGITEIHMEGEKSTLVYLNKLCHTRQLT | Function: Part of a complex that catalyzes the dephosphorylation of L-phosphoserine to serine and inorganic phosphate. Is poorly or not active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-nitrophenylphosphate, and fructose-6-phosphate. Does not display phosphoglycerate mutase activity.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 23548
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
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P0DUK2 | MVLNHSPPPGLYITGLGSQYPPYLLGPEKLEEFAARFYDVESPGLKKLLQINRSSGIETRSAIRSYESGFATRPEAPTISELAEFYHQAGVDLTTQACKKALRESQISPQHVTHTIGVTCTNQGNPGFDLLVNRKLGLSANVDRMLLHGVGCAGGLAIMRAAAQIACGASMRRKPVRILAFACELCTPNVRHDLAFAEKAPNAENISIAGALFSDAAAAFVLCNEYAMAETEITPLFQLLEWGNSLIPDTVEHMAFFADVDGYRTVLTRDVPQYTKHAIGPMFEKLLPSYQSQIQSSSGEGVGEVAKSLGVSDFDWALHPGGEAIIEGAKQVLGLTEDQLQASREIYRTRGNSSSATVLIVLDRLRSLGKREYVVATSFGPGLAIEMAMLRRCEVDED | Function: Type III polyketide synthase; part of the gene cluster that mediates the biosynthesis of the alkylresorcinols called soppilines . The biosynthesis starts with the HR-PKS pspA-catalyzed carbon chain assembly through nine chain elongation cycles, using acetyl CoA and malonyl CoA as a starter and extender units, respectively, to produce the polyketide soppiline A . In the first round, the KR, DH, and CMeT domains work to produce 2-methyl-2-butenyl thioester . In rounds 2 to 5, the KR, DH, and ER domains fully catalyze the reduction of the elongated beta-ketothioester, resulting in the insertion of eight methylene units . The unusual Z,E,Z-triene motif is likely constructed during rounds 6 to 8 . Typically, the DH domain introduces a double bond at an alpha,beta-position of an elongated polyketide chain, with the dehydration of a beta-hydroxy group . The last extension cycle would be carried out with L-oriented beta-ketoreduction by the KR domain to produce beta-hydroxy carboxylic acid soppiline A . The type III PKS pspB intercepts the elongated polyketide chain at round 8 from the HR-PKS pspA, followed by a tri-keto extension and decarboxylative aldol cyclization to produce 1,3,5-trisubstituted alkylresorcinol soppiline B . Subsequently, the cytochrome P450 monooxygenase pspC catalyzes three-step oxidations at the C-4 methyl group to carboxylic acid to yield soppiline C .
Catalytic Activity: acetyl-CoA + 22 H(+) + 11 malonyl-CoA + 12 NADPH + S-adenosyl-L-methionine = 12 CO2 + 12 CoA + 8 H2O + 12 NADP(+) + S-adenosyl-L-homocysteine + soppiline B
Sequence Mass (Da): 43195
Sequence Length: 398
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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Q8EDU8 | MAPKVFYISDGTAITAEVFGHAVLSQFPLEFESLTIPFVETLAKAENVKRQINDCFITTGERPLVFHSIVKPEIRDIIYSSEGLDYDFLNTFVAPLEQHLGVSASPVLHRTHGKANQGYEARIDAINFAMDNDDGQTMKHMDQADLILLGVSRCGKTPSSLYLSMQFGIKAANYPFTEDDMDNLKLPEALKRNKKKLFGLTIDPVRLHEIRQSRMENSRYSSLKQCRLEVKEVEMMFKRERIPYIDTTNHSVEEIATKILDVTGLERHMF | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Mass (Da): 30763
Sequence Length: 270
EC: 2.7.11.33
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Q2JMJ0 | MRPPFPGTPDSSKKSANLTVKLETQAVSVYYGSHLAVKQVSLKIPKNHITAFIGPSGCGKSTLLRCFNRMNDLIPGARVEGSVIFHGKNIYDPDVDPAEVRRRVGLVFQKPNPFPKSIYDNIAFGPRVNGYQGDLDELVERALRQAVLWDEVKDKLKTSGLSLSGGQQQRLCIARTLAIQPEVILMDEPCASLDPISTLRIEELLKELGRRYTIIIVTHNMQQAARVSDFTAFFNTEVDEEGFRYGRLVEFNRTEKIFNSPAHRETEEYVSGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30872
Sequence Length: 275
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
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P46341 | MSEQMVKEKPERAVIVPKQNHVLEVKDLSIYYGNKQAVHHVNMDIEKNAVTALIGPSGCGKSTFLRNINRMNDLIPSARAEGEILYEGLNILGGNINVVSLRREIGMVFQKPNPFPKSIYANITHALKYAGERNKAVLDEIVEESLTKAALWDEVKDRLHSSALSLSGGQQQRLCIARTLAMKPAVLLLDEPASALDPISNAKIEELITGLKREYSIIIVTHNMQQALRVSDRTAFFLNGELVEYGQTEQIFTSPKKQKTEDYINGKFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30003
Sequence Length: 269
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q1QSE9 | MVDFSSASSCFDIENLSLAYDDKPALSDLTLKVPRHRVTAFIGPSGCGKSTLLRALNRLHDLNDQVTRTGRIRLEGQDIHAREVDVAELRRRVGMVFQAPNPFPMSIYENVAYGLRLQGIRRKRELDEIIEWALLSAALWDEVKTNLHASAWTLSGGQQQRLVIARTLAVRPDVLLLDEPASALDPISTLKIEELIRGLKSQLTLVLVTHNMQQAARVSDYTAFLHGGELVEYAPTDTLFTNPRLRRTEDYITGRVG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28802
Sequence Length: 257
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
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Q51546 | MQNETASHGINFDALGRDRQSLDLASESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYITGRYG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31045
Sequence Length: 277
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
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Q9UZU7 | MKEFAIETRNLRIYYGSNEVIKGINLKIPKNVVFALMGPSGCGKSTLLRAFNRLLDLNPEAKVEGEVRISGVNIYSPDVDPIRVRREVGMVFQYPNPFPHLTIYENVAIGVKLNGLAKGKELDEIVKWALKKATLWDEVKNRLKDYPANLSGGQKQRLVIARVLAMKPKIILMDEPTANIDPVGTRKIEELLFELKKDYTIVLVTHSPAQAARVSDYVAFIYMGKIVEVGPTRKVFENPEHELTEKYVTGALG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28437
Sequence Length: 253
Subcellular Location: Cell membrane
EC: 7.3.2.1
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Q7UP21 | MKALNANISTMSEVSRSATPQSDSPAQAEVTPEVCIRIANFNAWYGSFQAIHNLSLDVPRNQVTAFIGPSGCGKSTLLRWINRMNDIVPSANSRGTLMIDELDVLAQTTDVVNLRRRVGMVFQKPNPFPKSIYDNVAFGPKLHLYLSRAELDELVEWSLRKAAVWDEVKDRLHAPALGLSGGQQQRLCIARAIAVGPEVLLMDEPCSALDPASTLAIEDLIYELREQYTIVMVTHNMQQASRCSDRTAFFFEGKLVESGPTQDVFTKPQEKRTDDYVRGRFG | Function: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31419
Sequence Length: 282
Subcellular Location: Cell inner membrane
EC: 7.3.2.1
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Q0RBB8 | MAGRSNIVVSATVRDALAAGAPVVALESTLIAHGLPRPRNRDVAVELEELARARGVTPATIAVIDGVPRVGLDEPDLRRIADDANVIKLSVRDLPVACATGWTGATTVASTALLAARVGIRLFATGGLGGVHRGAGDSFDESADLVTLAAMPITVVSAGVKSILDIGATLERLETLGITVVGYRTSTFPGFYLPHTTYDLDWRVGDAGQVAATMAAADLLGLTSAIVVANPLPTDQALDPALHDRVLADALAWATERGIRGKAVTPFLLETFHRETGGASLEVNINAVRNNVAVASDIALAWAAKDRSPTDPAAPDPTAPDPAAPDPTAPDPAAPDSAAPDLAGPDPSAPDPAAVARAHRP | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 36954
Sequence Length: 361
EC: 4.2.1.70
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C1AA54 | MSERLLRPRATSTVFEALERGAALVALESSVLAQGLEPPYNREAARRMTEAVTAVGAIPVITAISRGTPTLGLDDEDLERFLQRDGVRKVSARDLGIAMADGADGATTVAATLALCALGGLEVFATGGIGGVHRDAPFDESADLIELSRTPVIVVCAGAKSILDLPATLERLETLGVPVVGCGTDELPGFFSLSTGLRLTSRLDRPEQIARAWRAHRALGRESAMLVVQPPPADVAIPADIVDAATRAALQAASLAGIRGAAVTPYLLAQIQQRTEGRSVSANLALLEANARLAGQIAVALVEGTP | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 31794
Sequence Length: 306
EC: 4.2.1.70
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Q5ZU79 | MFHDLLEFNEEVLDAINDKNPIVALESTIISHGMPYPDNLTTAIEVENIIRRQGAIPATIAMHQGKIRVGLTQEVMEHLALQKEVIKASRRDISFVLSRKVTASTTVAATMFCAHMAKLPLFVTGGIGGVHQDVTMSFDISADLIELSNTPVTVVCSGAKSILDLPKTLEVLETFGVPVIGYATDEFPAFYSRSSGIPVPQRLNSAEEVANLMSIQQKLNMKNGIVVANPIPVSAELSDEEISPYIKQAHDEAKHMSGKSLTPFLLKRIAELTAGKSLEANIELIKNNAFLGAEIAIAYQKKLFSKKT | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 33570
Sequence Length: 308
EC: 4.2.1.70
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Q1D739 | MDLRFSEEVRRALEAGQPLVALETSVVAQGLPYPDNLAAARACEEAIRRAGAVPAATAIIDGQLCVGLEEPEMRRLAEGKERLLKVASRDFAVAMATRATGGTTVSATCEMAAAAGIRVFSTGGIGGVHRGASEHFDISQDIAALARFPVAVVCAGAKSVLDLPKTMELLETAGVPVIGVGTDELPSFYSRGSGIPLEHRADDVDTAARIARARFESLKQGGVLYTVPPPEETSLPRNEVELHIAATLADADRQGIRGKAVTPFLLSEMAKRTGGKTLKANLALLTNNARFAGQLAVAYARAS | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 31787
Sequence Length: 303
EC: 4.2.1.70
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A1B316 | MPPLIALSPETSQALADRQPLVALESTIITHGMPYPQNLEVAQQVEAAVREEGAVPATIAVMGGRIRVGLDAEALEALASTPAEQVMKLSRADLAACLALGRTGATTVAATMICAHLAGIEVFATGGIGGVHRGAETSFDISADLQELAQSPVTVVAAGAKAILDLPKTLEVLETLGVPVIAFGQDQLPAFWSRESGLAAPLRMDDPAQIAASARLRRELGLSGGQLVVNPIPPEAEIPRAEMIPVVEQALSEAEAQGIAAKAVTPFLLQRIFELTQGRSLDANIALVLNNARLAARIAAAMAT | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 31517
Sequence Length: 304
EC: 4.2.1.70
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A9BJN0 | MNTTPYLEIKEEVYQALKENRPIVALESTIISHGMPYPQNVEVAKNVEETIRERGAVPATIAIIDGKMKVGLSKEELEFMATSKNILKASRMDLPVILAKGFNAATTVAATMIIAELAGIKVFVTGGIGGVHRNAQETFDISADLQELAKTNVAVISAGPKAILDLQLTKEYLETFGVPVIGYQTDELPCFFSRESGINVPYRVETPKEIASIMKTKWDLGLQGGIFIANPIPKEYSLDFEEIDKTIENAIEEAKKRKIKGKELTPFLLSKINELTKGESLKANIELVYNNAQLGAEIAKEFNILS | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 33645
Sequence Length: 306
EC: 4.2.1.70
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A8F8N4 | MEKILALESTVIAHGLPFPINIDTAVELEELAAETGCSAKTIGIIAGQIKVGLSREEIVQIASRKDVLKIGTAEIPFALAKKMWAATTVSATMRIAHLNNIKVFATGGIGGVHKIDQWDVSQDLAELSRTRMIVVSAGPKSILDLRSTVEMLETFQITVVGYKTDELPAFYCKSTSIHINRVDSFEEIASIFLFKEKFNLPGAVLVFNPIPDEHAIEVEQFEEWYRLSEHDLDASSVKGKGVTPFLLSRLAHYSKGKTVRSNVELLKNNVKVACEILNQLSKMQ | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 31324
Sequence Length: 284
EC: 4.2.1.70
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B6IRJ4 | MHDFLSIHPEVAAALKAGRPVVALESTLISHGLPAPANLETAQAIEAAVRANGAVPATIAVLDGRIRVGLDAEDMQRLAAPGTAKVSRRDLPLVLAKGADGATTVAATMIAADLAGIAVFATGGIGGVHRGVETTGDISADLEELATTSVAVVCAGAKAILDLPRTLEYLETRGVPVVGFGTDAFPAFYHRDSGLPVDGRCDTPEDAARVLNAKWRLGLAGGIVVAVPIPDEAALDAAQAEAAVQQAVAEAATGGVRGKALTPFLLHRLETLTGGASLTANRALLLNNAAVGARIAVAYARLKQETTLPKKPPPSKRPTY | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic Activity: D-ribose 5-phosphate + uracil = H2O + psi-UMP
Sequence Mass (Da): 32693
Sequence Length: 320
EC: 4.2.1.70
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Q9YPD6 | MSKYLATSVRLCLMVCIVGWLLMPSYKELDGWCSSLSSLERDKSNWLLTGLSTWFCIVPSGTDQSSLVSYFSPLEKLSKFVQDLDLDFVKLWWLETITLINTLNTTEKLLSGVTFSVVLWYPRILVTVLMLVWKLWFPVRFLVVASSLLCLRILVWPFEVIADVILETCAWFTRKYHKLMDVIEDLMMIPQRVMEWCSGNTAKMVVPTVASCVSESIESKLDRILMALGRKGTVLEAAQPGSDFVECEQWPNGLVAIRRHDGRIVGMGFLVVLNGKWRLVTAAHVARECKRGIMLSAGIDSKTVTFQDLDVVLQTQVDACIMNVPAGTAASLGVRKVVINRTPSESKVVRTYGYNSGKFCMSEGLVGTTSANMGFRHGCSTLRGWSGTPIYRDNKVVGIHSRCNGIYENFGLSLDLLVGRLESEETDRYARTMEEFNTEDRPVTPPMEFSWEFEEKFERVRSTRKSFARIESEVATFTATKLSGFDWTDDAPMDFDELPVFESTMVSVFQERPLGGLPISNGNKAEEKKITSEALEPSKSSTPEAAKHTRRRRRNKKKSKNSETGHGPEEQSQQQSRPSSPIPDDSAPVSSPPVSPPSTGSVPKSWTQAYTQKLVLLLGSMDGQSKEKVDLAILEAKSFASALFPPSKPKSSEESEK | Function: Putative serine protease.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73415
Sequence Length: 657
Subcellular Location: Host membrane
EC: 3.4.21.-
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O52593 | MSFLEQIIERAKSDVKTIVLPESTDLRVIKAASMIMKKGIAKVVLIGNEKEIKSLAGDIDLEGVMIEDSLNSEKLEDYANTLYELRKSKGMTIEAARETIKDPLYYGVMMVKKGEADGMVAGAVNSTANTLRPALQILKTAPGTKLVSSFFVMVVPNCEYGHNGTFVYADCGLVENPDADQLSEIAISASKSFEMLVGAKPQVAMLSYSSYGSAKSELTEKVIKATQLAKEKAPHLAIDGELQVDAAIVPEVAKSKAKGSSVAGKANVLIFPDLDAGNIAYKLTQRLAKAEAYGPITQGLARPVNDLSRGCSAEDIVGVAAITAVQAQYVKA | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 35396
Sequence Length: 332
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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P39646 | MADLFSTVQEKVAGKDVKIVFPEGLDERILEAVSKLAGNKVLNPIVIGNENEIQAKAKELNLTLGGVKIYDPHTYEGMEDLVQAFVERRKGKATEEQARKALLDENYFGTMLVYKGLADGLVSGAAHSTADTVRPALQIIKTKEGVKKTSGVFIMARGEEQYVFADCAINIAPDSQDLAEIAIESANTAKMFDIEPRVAMLSFSTKGSAKSDETEKVADAVKIAKEKAPELTLDGEFQFDAAFVPSVAEKKAPDSEIKGDANVFVFPSLEAGNIGYKIAQRLGNFEAVGPILQGLNMPVNDLSRGCNAEDVYNLALITAAQAL | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 34791
Sequence Length: 323
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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O51535 | MLYSFYKVFCLKDYVFKKARIFVKENKLKANIVFPESSDSRVLKAAIVILQKNLADSIILIGKKDTVINSLKEFSNCNDILGRIEVVDPNSFPDIEMYLDEYWSLQKLKGVTKQSLKTQVLDEITFAMLMVRFGYAKSCVCGAVSTSAKVLSNALRIIPKLEGVKIISSFMIMDTLCTARNVDFCFGHNGILFFADCSVVVNPNSLELAEIALQSAKSFKDILNAKPKVALLSFSTKGSSSAKETEKVKNALNIVRNKESDLLIDGELQLDSAIIKDVAEKKCRESLVAGSANVLIFPNLDAGNIGYKLVERFAFAKAYGPFLQGFSKPISDLSRGCSVDEIVFASALMISI | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 38846
Sequence Length: 352
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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P71103 | MDLIESIWECAKQDKKRIILAEGEEKRNLIAADKIIKEGLAELVLVGDENKIKEKASELNLDISKAEIMDPETSLKTETYARDFYELRKHKGMTIEKSEKMVRDPLYFATMALKDGYVDGMVSGAVHTTGDLLRPGLQIIKTAPGVKIVSGFFVMIIPDCDYGEEGLLLFADCAVNPNPTSDELADIAITTAETARKLCNVEPKVAMLSFSTMGSAKGEMVDKVKNAVEITKKFRPDLAIDGELQLDAAIDSEVAALKAPSSNVAGNANVLVFPDLQTGNIGYKLVQRFAKAKAIGPICQGFAKPINDLSRGCSSEDIVNVVAITVVQAQRGI | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 36140
Sequence Length: 333
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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P77844 | MSAELFENWLLKRARAEHSHIVLPEGDDDRILMAAHQLLDQDICDITILGDPVKIKERATELGLHLNTAYLVNPLTDPRLEEFAEQFAELRKSKSVTIDEAREIMKDISYFGTMMVHNGDADGMVSGAANTTAHTIKPSFQIIKTVPEASVVSSIFLMVLRGRLWAFGDCAVNPNPTAEQLGEIAVVSAKTAAQFGIDPRVAILSYSTGNSGGGSDVDRAIDALAEARRLNPELCVDGPLQFDAAVDPGVARKKMPDSDVAGQANVFIFPDLEAGNIGYKTAQRTGHALAVGPILQGLNKPVNDLSRGATVPDIVNTVAITAIQAGGRS | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 35238
Sequence Length: 329
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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Q9ZKU4 | MQSLWIYPEDTEVLGAACKSLLKALKPRYQKIALFSPISGGCEGFGECESLSSLEVHSAIDKQKALELVSTAQEELLFETILKRYDELQSTHDFVINLGYAPKFFLNALLDLNTILAKHLNAPVVAVAQTSLDHLKAMHSHILKKEAPFAIGLFVGETLEKPHFLSASLCKQQCELEASAIENLLQTKSEIITPLAFQRSLEKKAKKQIKKVVLPESEDERILKAAHRLNLMGAVGLILLGDKEAINSQAKNLNLNLENVEIINPNTSHYREEFAKSLYELRKSKGLSEQEAERLALDKTYFATMLVHLGYAHAMVSGVNHTTAETIRPALQIIKTKPGVSLVSSVFLMCLDTQVFVFGDCAIIPNPSPKELAEIATTSAQTAKQFNIAPKVALLSYATGNSAQGEMIDKINEALTIVQKLDPQLEIDGPLQFDASIDKGVAKKKMPNSQVAGQASVFIFPDLNAGNIAYKAVQRSAKAVAIGPILQGLNKPINDLSRGALVEDIVNTVLISAIQAQDY | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 56738
Sequence Length: 519
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
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P38503 | MVTFLEKISERAKKLNKTIALPETEDIRTLQAAAKILERGIADIVLVGNEADIKALAGDLDLSKAKIVDPKTYEKKDEYINAFYELRKHKGITLENAAEIMSDYVYFAVMMAKLGEVDGVVSGAAHSSSDTLRPAVQIVKTAKGAALASAFFIISVPDCEYGSDGTFLFADSGMVEMPSVEDVANIAVISAKTFELLVQDVPKVAMLSYSTKGSAKSKLTEATIASTKLAQELAPDIAIDGELQVDAAIVPKVAASKAPGSPVAGKANVFIFPDLNCGNIAYKIAQRLAKAEAYGPITQGLAKPINDLSRGCSDEDIVGAVAITCVQAAAQDK | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35220
Sequence Length: 333
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cell membrane
EC: 2.3.1.8
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Q49112 | MYTLEEIKNQLGLKSEKKSIVFPEAESEIIQSVAKTLVDEKLGLPILLFKSSKEVPSEIKNNSSIKTICLDEFDTKEFEEEFVKLRKGKATIEVAHQVMQLPNYIGAMLVKLNQADCMLSGLNNTTADTIRPALQIIGTKPGYNIASSIFVMSKGNENYIFTDCALNIKPTSEQLVEITQMAVDFAKALNVKNVEAALLSYSTNGSGKGEDVDRVHQAVEILKSKEKDYVCEGEIQFDAAFDKKTRDKKFKNCSLLKQTPDIFVFPDINAGNIGYKIAQRMGGFEAIGPFVLGLNQPVNDLSRGATFVDVLNTAIMTLYLSY | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 35677
Sequence Length: 322
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
|
P47541 | MSVIDIFKKRLQAVSKKPVIIFPEGWSASVLKAVEMLNESKLIQPAVIFHNRQEIPANFDKKITHYVIDEMDLTSYANFVYEKRKHKGMDLKEAQKFVRDPSSLAATLVALKVVDGEVCGKEYATKDTLRPALQLLATGNFVSSVFIMEKGEERLYFTDCAFAVYPNSQELATIAENTFNFAKSLNEDEIKMAFLSYSTLGSGKGEMVDKVVLATKLFLEKHPELHQSVCGELQFDAAFVEKVRLQKAPQLTWKNSANIYVFPNLDAGNIAYKIAQRLGGYDAIGPIVLGLSSPVNDLSRGASVSDIFNVGIITAAQAIK | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 35469
Sequence Length: 320
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
|
P39197 | MKPLDRIHEAAKALDRHIILPEGEDPRVAEAARRLLAAGLARVTLMGGPEIPGAGRIDPAGGPDLAELADHWHRMRAARGMTAERALTEMRDPIRQAAMRVRLGQADGTVGGAVATTADTVRAALQIIGKAPGAGIVSSFFLMLSCGPGAPVRGGMIFADCGLVIQPDARELAAIALSAADSCRRILAEEPRVALLSFSTAGSAEHPSLGRIREALALIRAAAPGLEVDGEMQFDAALDEAIRARKAPESPLTGRPNVFVFPDLADGNIGYKIAERLAGLTAIGPILQGLAKPANDLSRACSVKDIVNATAITAMQTK | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 33185
Sequence Length: 318
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
|
Q9X448 | MRXRWPAQPSKYDRLIAAARAEAPAVTIVAHPCDETSLGGAIEAAEMGLITPILVAPEAKIRNVAAEHRLDLGRREIVDVPHSHAAAAKAVALIREGRGELLMKGSLHTDELMHEVAASATGLRTQRRISHVFVMDVPGHTDTLFITDAAINIFPDLEAKRDIVQNAIDLWVAIGLGEPRVAILSAVETVTAKIPSTIEAAALCKMAERGQITGGVLEGPLAFDNAIDQEAARIKGINSPVAGHAQILVVPDLEAGNMLAKNLTFLTHADAAGLVLGARVPIVLTSRADSVRTRLASCAVAALYAARRRAAQVAAV | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 33398
Sequence Length: 316
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
|
Q9ZE39 | MKKQHIINETFLDEILAQKLGTTYIPPTEIKDSDFDKAAKHFINLLLRADGLKPIKTAVVHPIDKESLLGAVRAAQFNVIKPILIGPQHKIESVAKVNDVDLENYQVINAEHSHEAAKKAVELAKKREVAAIMKGALHTDELMSAVVYKENGLRTERRISHAFLMAVATFPKPFIITDAAINIRPTLEDKRDIVQNAIDLMHIIKEDKQVRVAVLSAVETVTSAIPTTLDAAALSKMADRGQITNAVVDGPLAFDNAISLFAAEAKGISSPVSGNADILVVPDLESGNMLAKQLKYLGQAVMAGIVLGARVPIILTSRADPIDMRVISCVLASFIYNQTKAKLHNSSKSII | Catalytic Activity: acetyl-CoA + phosphate = acetyl phosphate + CoA
Sequence Mass (Da): 38170
Sequence Length: 351
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.8
|
P17127 | MFQLSVQDIHPGEQAGNKEEAIRQIAAALAQAGNVAGGYVDGMLAREQQTSTFLGNGIAIPHGTTDTRDQVLKTGVQVFQFPQGVTWGEGQVAYVAIGIAASSDEHLGLLRQLTHVLSDDSVAEQLKSATTAEELRALLMGEKQSEQLKLDNETMTLDVIASSLVTLQALNAARLKEAGAVDAAFVAKTINDSPMNLGQGIWLNDSAEGNLRSAVAVSRATQAFDVEGEKAALLVTVAMNDEQPIAVLKRLGDLLLNNKADRLLSADAATLLALLTSDDALTDDVLSAEFVVRNEHGLHARPGTMLVNTIKQFNSEITVTNLDGTGKPANGRSLMKVVALGVKKGHRLRFTAQGEDAEQALKAIGDAIAAGLGEGA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Sequence Mass (Da): 39594
Sequence Length: 376
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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Q9KM70 | MLELTTQDIQLQQHFANKQAAIQGLAHALTAKGLVAEGYAQGMLNREAQHSTYLGNGIAIPHGTTDTRELVKQTGVTAMHFPQGLDWGDGNLVYVAIGIAAKSDEHLGILKQLTRVLSADGVEQALQQAKTAQQIIAIIKGEAQLTADFDASLIQLQFPASDMVQMSAVAGGLLKNTGCAENEFVADLVTKAPTHLGRGLWLVASDRAVKRTGMSIVTTANHCEYEQQAVKALIAFSVCNDVHQPLLNTITQCVFEQKQDQLLQADVQQLLNLFSGNAEQTIAQRTIAVGTITEETIAAETVAEPDSARAHTATFRIKNSHGLHARPGAMLVAEAKKFESNIRVSNLDGDGQVVNAKSLMKVIALGVKHNHQLQFTAEGPDAEAALQALGVAINAGLGEG | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Sequence Mass (Da): 42614
Sequence Length: 400
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P23388 | MIPLTSELVAIGKTATDKADAIAQAVDLLTAAGKIDPRYGQSMMGREAVANTFLGNGIAIPHGLPQDRDLIHDTAIAVVQLPAGVEWAPGDTARLVVAIAAKSDEHLQVLSNLTDVLGDEAEAERLATTLDAAVIVARLTGAAAPVAAPAETPADFAQGIDVVVTGAHGLHARPATTLVDLAKGFAAEIRIRNGAKVANGKSLISLLNLGAAQGAALRISAEGADATAALAAIAAAFEAGLEDEEDTGAAAPEAATPGLTGAGASMASYEGRTLVGISSSPGYALAPVFRFARDEVVFDTDAADAAFETDRLDTALQTAWHELEELHDEVWKTSGPARAAIFRAHQEFLHDPEMVAEAKALIGQGRSAGFAWHRVFSDRADMLGAMKDAVLSGRAIDLRDAGQRVLQHLGRVRTGETHLPTAPCILLADDLTPSDTARLDPALVRGLATAQGGPTSHTSIIARALDIPAVAGVGPRLLDLATGTPVLLDGGAGVIVVAPTEADKARAETAMAALTAQRELEARERYKPALTVDGARVEVVANISDVAEAIASVEAGAEGVGLLRTEFLFVNREAPPGEDEQLAIYAAMLSALNGLPIIIRTLDVGGDKEIPYLRMPVEQNPFLGERGIRFCLSHEDLFRTQLRAIYRASAGGQVRIMFPMIAMIEELETARRIAEEVRLEVGAAPVEIGIMIEIPSAVMMAPELAKRVDFFSIGTNDLTQYALAMDRMHPVLAKQADGLHPAVLRLIDSTVRAAEAARIWVGACGGIAGDPVGAAVLSGLGVRELSVSIPAVAGIKAQLRHSAMAENRDLARRALACTTAAEVRGLK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 86394
Sequence Length: 827
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P45597 | MSSPSIAPVTPDLVRLRATARDKDDAIAQAAQLLVAAGCVAPGYDASMRRREGLANTFLGHGLAIPHGVGEDRHLVRRDGIAVLQLPEGVEWNPGQTTRLVVGIAAQSDTHITLLRRLTRLIQDPAQLEALFTTDDPAVIVAALTGDRAPDTSAAPATDLAERFEWTIAYPSGLHARPATRWAETARGFSARAQVRAGDQAADAKSLVGLLQLGLRAGDSITVSAKGSDAPALLKRLRAVMDSLTAQEKADAERAAQRRAAPVIGWTPPQAQPAIVGIGASPGVAIGIVHRLRAAQTEVADQPIGLGDGGVLLHDALTRTRQQLAAIQDDTQRRLGASDAAIFKAQAELLNDTDLITRTCQLMVEGHGVAWSWHQAVEQIASGLAALGNPVLAGRAADLRDVGRRVLAQLDPAAAGAGLTDLPEQPCILLAGDLSPSDTANLDTDCVLGLATAQGGPTSHTAILSRTLGLPALVAAGGQLLDIEDGVTAIIDGSSGRLYINPSELDLDAARTHIAEQQAIREREAAQRALPAETTDGHHIDIGANVNLPEQVAMALTQGAEGVGLMRTEFLFLERGSTPTEDEQYQTYLAMARALDGRPLIVRALDIGGDKQVAHLELPHEENPFLGVRGARLLLRRPDLLEPQLRALYRAAKDGARLSIMFPMITSVPELISLREICARIRAELDAPELPIGIMIEVPAAAAQADVLARHADFFSIGTNDLTQYVLAIDRQNPELAAEADSLHPAVLRMIRSTIDGARKHDRWVGVCGGLAGDPFGASLLAGLGVQELSMTPNDIPAVKARLRGRALSALQQLAEQALQCETAEQVRALEAQREGQA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Sequence Mass (Da): 88747
Sequence Length: 838
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P26379 | MISVIISGHGDFPIALKESSGMIFGEENNLIAVPFFKGEGIQTLQEKYHQALKDIPEEHEVLFLVDIFGGTPYNAAASFIAEDQRMDMAAGVNLPILLEVLSLREHLALKDLLNNLKAMSQQSFQVCSEHLEKVKTANQDTREDEL | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LevDE PTS system is involved in fructose transport.
Sequence Mass (Da): 16257
Sequence Length: 146
Domain: The EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB type-4 domain.
Subcellular Location: Cytoplasm
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D4GYE4 | MDVTDISTITPLELISLEEPPATKEGAIEFLLDLAVDAGRVDDRDAALDALLEREGEATTGVGFGIGIPHAKTDAVSKPTVAFARSAEGIDFDAMDDKPAKLLFMILVPAAGGEDHLQILSALSRSLMHEDVREKLLEAESKQTVQDVLAEVVE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II PtfABC PTS system is involved in fructose transport.
Sequence Mass (Da): 16453
Sequence Length: 154
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P69810 | MSKKLIALCACPMGLAHTFMAAQALEEAAVEAGYEVKIETQGADGIQNRLTAQDIAEATIIIHSVAVTPEDNERFESRDVYEITLQDAIKNAAGIIKEIEEMIASEQQ | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FryABC PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Sequence Mass (Da): 11735
Sequence Length: 108
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cytoplasm
EC: 2.7.1.202
|
P69818 | MTKIIAVTACPSGVAHTYMAAEALESAAKAKGWEVKVETQGSIGLENELTAEDVASADMVILTKDIGIKFEERFAGKTIVRVNISDAVKRADAIMSKIEAHLAQTA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FrwABC PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Sequence Mass (Da): 11248
Sequence Length: 106
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cytoplasm
EC: 2.7.1.202
|
P32676 | MAYLVAVTACVSGVAHTYMAAERLEKLCLLEKWGVSIETQGALGTENRLADEDIRRADVALLITDIELAGAERFEHCRYVQCSIYAFLREPQRVMSAVRKVLSAPQQTHLILE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Sequence Mass (Da): 12637
Sequence Length: 113
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cytoplasm
EC: 2.7.1.202
|
P20966 | MKTLLIIDANLGQARAYMAKTLLGAAARKAKLEIIDNPNDAEMAIVLGDSIPNDSALNGKNVWLGDISRAVAHPELFLSEAKGHAKPYTAPVAATAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVETRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYEPAGKAQTATTESKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFALMVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGIIAGFLAGYIAKLISTQLKLPQSMEALKPILIIPLISSLVVGLAMIYLIGKPVAGILEGLTHWLQTMGTANAVLLGAILGGMMCTDMGGPVNKAAYAFGVGLLSTQTYGPMAAIMAAGMVPPLAMGLATMVARRKFDKAQQEGGKAALVLGLCFISEGAIPFAARDPMRVLPCCIVGGALTGAISMAIGAKLMAPHGGLFVLLIPGAITPVLGYLVAIIAGTLVAGLAYAFLKRPEVDAVAKAA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57519
Sequence Length: 563
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cell inner membrane
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P44714 | MKLFLTQSANVGDVKAYLLHEVFRAAAQKANVSIVGTPAEADLVLVFGSVLPNNPDLVGKKVFIIGEAIAMISPEVTLANALANGADYVAPKSAVSFTGVSGVKNIVAVTACPTGVAHTFMSAEAIEAYAKKQGWNVKVETRGQVGAGNEITVEEVAAADLVFVAADIDVPLDKFKGKPMYRTSTGLALKKTEQEFDKAFKEAKIFDGGNNAGTKEESREKKGVYKHLMTGVSHMLPLVVAGGLLIAISFMFSFNVIENTGVFQDLPNMLINIGSGVAFKLMIAVFAGYVAFSIADRPGLAVGLIAGMLASEAGAGILGGIIAGFLAGYVVKGLNVIIRLPASLTSLKPILILPLLGSMIVGLTMIYLINPPVAEIMKELSNWLTSMGEVNAIVLGAIIGAMMCIDMGGPVNKAAYTFSVGLIASQVYTPMAAAMAAGMVPPIGMTVATWIARNKFTVSQCDAGKASFVLGLCFISEGALPFVAADPIRVIISSVIGGAVAGAISMGLNITLQAPHGGLFVIPFVSEPLKYLGAIAIGALSTGVVYAIIKSKNNAE | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57706
Sequence Length: 556
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cell inner membrane
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P23387 | MSKIVAVTAGAKGVAHTHLAAEALSATAQALGHQIRVERHSAEGVEAPLQGAEIAAADVVLIAADLRIEDVRFVTKPVYRTSTARAVTQTAAVLAEALALTGEETPQMTTDTGQRPLRVVAITSCPTGIAHTFMAADALKKTAAARGWEIAVETQGSVGSQNALSAAQIQAADLVVIAADTHVDDSRFAGKKVYKTSVGAAVKGAAKVLDAALAEGVVLGTNLADTVDALKAQRAATRSGPYMHLLTGVSYMLPLVVAGGLLIALSFVFGIKAFEVEGTLPAALMAIGGGAAFKLMVPVLAGFIAYSIADRPGLTPGLIGGMLAVNLNAGFLGGIVAGFLAGYVARWLRDAIKLPRTLEGLKPVLILPLLSTAITGLIMVYVVGTPVAAILAAMTAFLQGLGTTNAVVLGLILGGMMAVDMGGPINKAAYTFAVGLLTSSTYAPMAAVMAAGMTPPLGLALATLVAKNRFTAEEREAGGAAAVLGLSFITEGAIPFAAKDPARVIPSIIVGSAITGALSMALGCLLVAPHGGIFVLAIPHAVTNLGLYALSIVVGTLVTTGLLIALKKPIPAEERARS | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58576
Sequence Length: 578
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cell inner membrane
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P23355 | MSSSIVVIAAGERSTEAVLAAEALRRAATAAGRSVTIEIRSDQGVLGALPTELTNGAAHVLIVGDADADTARFGDAQLLHLSLGAVLDDPAAAVSQLAATTAPASTSATTDASGAGGKRIVAITSCPTGIAHTFMAAEGLQQAAKKLGYQMRVETQGSVGAQDALTDEEIRAADVVIIAADREVDLARFGGKRLFKSGTKPAINDGPALIQKALAEAGVHGGAAPVAGANATSDAKGNARTGAYKHLMTGVSFMLPFVTAGGLLIALAFALGGIYAGDDAHQGTLAWSLFQIGAKAGFTLMVPALAGYIAYSIADRPGIAPGMIGGLVAANLNAGFLGGIIAGFIAGYGVAALNRYIKLPRNLEGLKPVLILPVLGTLLVGLAMMYVFGQPVADLLAWLTAWLRGMQGSSALLLGLLLGGMMAFDMGGPVNKAAYAFSTGLIASQVYTPMAAAMVAGMTPPLGIALATWVFRNRFTVEERGSATAAGVLGLAFVTEGAIPYAARDPLRTIPALVIGSAVAGAISMTAGAELKAPHGGIFVLLIPNAVTHLLNYVLALVVGVVVTAVALRLLKKPVADVIA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Catalytic Activity: D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58647
Sequence Length: 580
Domain: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Subcellular Location: Cell inner membrane
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P37470 | MLVIAGLGNPGKNYENTRHNVGFMVIDQLAKEWNIELNQNKFNGLYGTGFVSGKKVLLVKPLTYMNLSGECLRPLMDYYDVDNEDLTVIYDDLDLPTGKIRLRTKGSAGGHNGIKSLIQHLGTSEFDRIRIGIGRPVNGMKVVDYVLGSFTKEEAPEIEEAVDKSVKACEASLSKPFLEVMNEFNAKV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20872
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q89YZ2 | MIKYLIVGLGNIGPEYHETRHNIGFMTVEALARINNAPPFIDGRYGFTTSFSIKGRQLILLKPSTFMNLSGLAVRYWMQKENIPLENVLIVVDDLALPFGTLRLKGKGSDAGHNGLKHIAAILGTQNYARLRFGIGNDFPKGGQIDYVLGHFTDEDRKTMDERLETAGEIIKSFCLAGIDITMNQFNKK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21089
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A1UTH5 | MLLIAGLGNPGSHYQNNRHNIGFMAVDAIHEAFSFSPWSKKFQAEVSNGLINGEKILLIKPQTFMNLSGQAIGEALRFYKLDLDHLIVFYDELDLPPGTVRVKIGGRSNGHNGIKSIDSHCGNNYHHVRLGIGRPISKELVDQYVLGNFTQSDQKWLSTLLGVIANNVAMLIKGDSNCFMNKISLTMKSQGLQ | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21353
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q6G2L1 | MWLIAGLGNPGLQYQNNRHNIGFMAIDAIYQSFSFSPWSKKFQAEISTGLINGKKTFLLKPQTFMNLSGQAIGEALRFYKLDLKNFIVIYDELDLPPGRVRVKIGGGNNGHNGIKSIDAHCGTDYCRIRLGIGRPNSKELVYQHVLGNFTKSDQEWLPSLLEAIAKNIALLIKGNKCLFMNEISQAMKNKNLQ | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21647
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q6MJR3 | MWLIVGLGNPGGEYKLTRHNIGFMAVDFLMEGLGNPPIKNQFKAEIAQAKIKDHPVIFCKPQTYMNLSGESVQPLMGFYKIPLERLIVIHDEIDQPFAQMKIQKNRGHGGHNGIKSISGLMGSMDYTRLRLGVGRPANPNIPVPDYVLGKFTKEEFAQMPDFLNKAGDAVESIILDGIQKASTKFNT | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20771
Sequence Length: 187
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B8DTI5 | MASEFWLIVGLGNPGAKYRNTRHNMGFMTVNELAKRWSIHFANHKGLADLGKGTMSLNGQTAKVFLCKPLTYMNDSGQAVQSIREYYHINLDHIVVIHDDMDLEFGRIKLKSGGSAGGHNGIKSIDRCLHSPDYARVRMGVGHASRSGDAHDNTINWVLGEFNAAQRKQLPEFLADGADAAETIVFEGLTKAQDKFNAR | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 22001
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q5HC85 | MLHLLVGLGNPGKEYELTRHNVGFMIIDAIMHHFLFPDFKKKHNALISSGSIRSHKVILAKPYTFMNNSGTPISSIVKLYKIPLDNIIVFHDETDIDFCTIRIKKGGGNAGHNGLKSIDTLLGRDYWRIRFGIGHPSNGYDLSYHVLSQFNNLNAVNNTISNIIEHISLLFENDKSIFKNKVKDLIKYTDISS | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21839
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A1AM05 | MSMHIIAGLGNPGSHYQWTRHNAGFLFLDRLAHLENVSITRKSFSGLAGEWSRANCRHILLKPQTFMNLSGRSVMQALQFYKLPLSQAIVVHDDLDLPFGTVRLKQGGGHGGHNGLRSIMEQLGKGDFIRLRVGIGRPLHGDTVNYVLGSMPPEQMELLPRILDGGLEMLEMLLDQGLPKAMSLFNNRNFLEK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21541
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q4FPG9 | MLLFVGLGNPTPDSENNRHNIGFKLIDALNQKFGLSKQKPKFKGLLTTGNVEDKKVYAIKPLTFMNNSGICIRELIEYFKIDAEDVIVFHDDLDLEFGKVKAKFAGSSAGHNGIESIDKFIGKDYSRVRIGIGRPKTKADVADHVLKDFDEDEMIQLEKITKNIIDSMAILIDKKLDLFSSTVNNK | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20863
Sequence Length: 186
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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C0QQW6 | MIKAVIGLGNPGKQYEDTRHNVGFMIADVVASLLKCNKKYIERCFSHIYVCEDHYLLIVKPQTFMNNSGVAVKNLLEDYDLKPDEILVVYDDLDLPLGTVRLRKKGSSGGHRGIQSIIESIKTDEFPRIKVGIGRPERKEQVVDYVLSPFKKEEKILLDKVISHTAQCILNVLKYGIDKSLNLCNKKIV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21417
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B3QZM3 | MKLIVGLGNPGQNYQFTLHNIGFMMIDYLLNTIITDKKIVKKHNSYIYKANVGSNLVLFVKPQTYMNSSGHAVKKILNEYKIILNDLLVLSDDIYLPEGNYKLKLKGGHGGHNGLRNIIDCLQTKKFKRLKIGVSQDHNISLEDYLLTPIDDKKKLMVQKSFPIISNIIKNFIQDC | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20081
Sequence Length: 176
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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A4T070 | MTKLIVGLGNPGEEHTEDRHNAGFWFLDVLAKQLNSRFESEKRFHGKVAKAKWEGEDLFLLKPSTYMNLSGQSVGALCRFHKITPAEILVVQDELDLKPGTARLKLGGGTGGHNGLKDIQAHLSTPEYWRLRLGIGHPRDLAGDGRPMDVADYVLRRPQLAEQKMIDASIENGLQILPLFLKGDTQTAMMELHSKA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21793
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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B2RHF2 | MKYLIVGLGNIGGEYNGTRHNVGFRMVNALAEDGGVQFVEARYGAIAHMRVKNAELILLKPNTYMNLSGNAVRYWMQQENIPREQVLVLVDDLALPFGTLRLKPKGSDAGHNGLKNIAEVMGSIDYARLRFGLGDEFSKGRQVDFVLGRFTPEEEEKLPELTKHAVEIIKSFCLAGIQRTMNRYN | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 20744
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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Q5XEM3 | MVKMIVGLGNPGSKYEKTKHNIGFMAIDNIVKNLDVTFTDDKNFKAQIGSTFINHEKVYFVKPTTFMNNSGIAVKALLTYYNIDITDLIVIYDDLDMEVSKLRLRSKGSAGGHNGIKSIIAHIGTQEFNRIKVGIGRPLKGMTVISHVMGQFNTEDNIAISLTLDRVVNAVKFYLQENDFEKTMQKFNG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
Sequence Mass (Da): 21169
Sequence Length: 189
Subcellular Location: Cytoplasm
EC: 3.1.1.29
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C0H3V2 | MQVLAKENIKLNQTVSSKEEAIKLAGQTLIDNGYVTEDYISKMFEREETSSTFMGNFIAIPHGTEEAKSEVLHSGISIIQIPEGVEYGEGNTAKVVFGIAGKNNEHLDILSNIAIICSEEENIERLISAKSEEDLIAIFNEVN | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Sequence Mass (Da): 15747
Sequence Length: 143
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P01252 | MSDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD | Function: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
PTM: Covalently linked to a small RNA of about 20 nucleotides.
Sequence Mass (Da): 12072
Sequence Length: 110
Subcellular Location: Nucleus
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P69825 | MRLSDYFPESSISVIHSAKDWQEAIDFSMVSLLDKNYISENYIQAIKDSTINNGPYYILAPGVAMPHARPECGALKTGMSLTLLEQGVYFPGNDEPIKLLIGLSAADADSHIGAIQALSELLCEEEILEQLLTASSEKQLADIISRG | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Sequence Mass (Da): 16046
Sequence Length: 147
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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P06454 | MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD | Function: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
PTM: Covalently linked to a small RNA of about 20 nucleotides.
Sequence Mass (Da): 12203
Sequence Length: 111
Subcellular Location: Nucleus
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P26350 | MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVDTKKQKTEEDD | Function: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
PTM: Covalently linked to a small RNA of about 20 nucleotides.
Sequence Mass (Da): 12254
Sequence Length: 111
Subcellular Location: Nucleus
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P75145 | MKLLKNNIYINVYLKNKQEIFEFVFKKFKEDGAVLDSFLPAIVERDKAASVAIGNYLFLPHPVYDEIANIQKEKMVFIGLKDVINIDGQPIKFICGLALKGEHQMDALQSLAIAFSDPEEVEKLVKDKDLTQDKVLEFLAKHN | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Sequence Mass (Da): 16313
Sequence Length: 143
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cytoplasm
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A0A140JWS9 | MSRVIRSILIILGSVALYTKYYLSFQNGFIDLLSTMGSQGSLAGLQSGLRSHYTGLDPLDRFLKACNVFFWPIFHGTSPALSLYAIAFAGSMIPMWLILLMHTCVNSSIVEIVMINALAGLLVQGIGPGVIMCVLLAMRNTSMKEFAVTGIPAVSILGPNDLPLSLVVCYILPLALSSLPAPASISVPSKQLFIAIWQGWPLYIALAVGIAHSLRNHYRRNRPQQLFRHAYAFALACSIISHVGLLSISFLSVSPQSPFLSLHSADLHPRSLLIPRLPWQEVKITSLESGVLRFLHWDYSISSTGTLLWCYDVYWKDRMRGRGWIAFFSLSSRLATMSLAFGPCSVALALYWAALSNNLMKSENARKR | Function: Part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40640
Sequence Length: 368
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 5.4.99.-
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P06302 | MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD | Function: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
PTM: Covalently linked to a small RNA of about 20 nucleotides.
Sequence Mass (Da): 12382
Sequence Length: 112
Subcellular Location: Nucleus
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Q5XAF5 | MGIGIIIASHGKFAEGIHQSGSMIFGEQEKVQVVTFMPNEGPDDLYGHFNNAIQQFDADDEILVLADLWSGSPFNQASRVAGENPDRKMAIITGLNLPMLIQAYTERLMDAGAGIEQVAANIIKESKDGIKALPEDLNPVEETAATEKVVNALQGAIPAGTVIGDGKLKINLARVDTRLLHGQVATAWTPASKADRIIVASDEVAQDDLRKQLIKQAAPGGVKANVVPISKLIEASKDPRFGNTHALILFQTPQDALRAVEGGVEINELNVGSMAHSTGKTMVNNVLSMDKEDVATFEKLRDLSVTFDVRKVPNDSKKNLFELIQKANIK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport.
Catalytic Activity: D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannose 6-phosphate(in) + L-histidyl-[protein]
Sequence Mass (Da): 35582
Sequence Length: 330
Domain: The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain.
Subcellular Location: Cytoplasm
EC: 2.7.1.191
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P69803 | MEITTLQIVLVFIVACIAGMGSILDEFQFHRPLIACTLVGIVLGDMKTGIIIGGTLEMIALGWMNIGAAVAPDAALASIISTILVIAGHQSIGAGIALAIPLAAAGQVLTIIVRTITVAFQHAADKAADNGNLTAISWIHVSSLFLQAMRVAIPAVIVALSVGTSEVQNMLNAIPEVVTNGLNIAGGMIVVVGYAMVINMMRAGYLMPFFYLGFVTAAFTNFNLVALGVIGTVMAVLYIQLSPKYNRVAGAPAQAAGNNDLDNELD | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27636
Sequence Length: 266
Domain: The PTS EIIC type-4 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
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P69807 | MSEMVDTTQTTTEKKLTQSDIRGVFLRSNLFQGSWNFERMQALGFCFSMVPAIRRLYPENNEARKQAIRRHLEFFNTQPFVAAPILGVTLALEEQRANGAEIDDGAINGIKVGLMGPLAGVGDPIFWGTVRPVFAALGAGIAMSGSLLGPLLFFILFNLVRLATRYYGVAYGYSKGIDIVKDMGGGFLQKLTEGASILGLFVMGALVNKWTHVNIPLVVSRITDQTGKEHVTTVQTILDQLMPGLVPLLLTFACMWLLRKKVNPLWIIVGFFVIGIAGYACGLLGL | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31303
Sequence Length: 286
Domain: The EIID domain, with its homologous EIIC domain, forms the PTS system translocation channel and contains part of its specific substrate-binding site.
Subcellular Location: Cell inner membrane
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P63089 | MSSQQYQQQRRKFAAAFLALIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNADCQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD | Function: Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors (By similarity). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (By similarity). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone . Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation . Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK or AFAP1L2 in order to activate the PI3K-AKT pathway . Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway . Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (By similarity). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway . Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion (By similarity). Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (By similarity). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway . Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration . In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway .
PTM: Phosphorylated by NEK6.
Sequence Mass (Da): 18869
Sequence Length: 168
Subcellular Location: Secreted
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P79281 | MQTPQFLQQRRKFAAAFLAFIFLLAVVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNADCQKTVTISKPCGKVTKPKPQAESKKKKKEGKKQEKMLD | Function: Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups. Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone (By similarity). Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation (By similarity). Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK, CTNNB1 or AFAP1L2 in order to activate the PI3K-AKT pathway. Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway. Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (By similarity). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway (By similarity). Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion. Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (By similarity). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway. Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration. In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway (By similarity).
PTM: Phosphorylated by NEK6.
Sequence Mass (Da): 18910
Sequence Length: 168
Subcellular Location: Secreted
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P54715 | MMQKIQRFGSAMFVPVLLFAFAGIIVGISTLFKNKTLMGPLADPDGFWYQCWYIIEQGGWTVFNQMPLLFAIGIPVALAKKAQARACLEALTVYLTFNYFVSAILTVWGGAFGVDMNQEVGGTSGLTMIAGIKTLDTNIIGAIFISSIVVFLHNRYFDKKLPDFLGIFQGSTYIVMISFFIMIPIALAVSYIWPMVQSGIGSLQSFLVASGAVGVWIYTFLERILIPTGLHHFIYTPFIYGPAVAEGGIVTYWAQHLGEYSQSAKPLKELFPQGGFALHGNSKIFGIPGIALAFYVTAKKEKKKLVAGLLIPVTLTAIVAGITEPIEFTFLFISPFLFAVHAVLAATMSTVMYMAGVVGNMGGGLIEAVTLNWIPLFGSHGMTYVYQILIGLSFTAIYFFVFRFLILKFNIATPGREKDEQQETKLYSKKEYRERKNKDETASAAETADDTAFLYIEALGGKDNITEVTNCATRLRVSVKDETKVEPDSVFRALGAHGVVRNGKAFQVIIGLSVPQMRERVEKILNQ | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in maltose transport.
Catalytic Activity: D-maltose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha-maltose 6'-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58055
Sequence Length: 527
Domain: The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell membrane
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P19642 | MTAKTAPKVTLWEFFQQLGKTFMLPVALLSFCGIMLGIGSSLSSHDVITLIPVLGNPVLQAIFTWMSKIGSFAFSFLPVMFCIAIPLGLARENKGVAAFAGFIGYAVMNLAVNFWLTNKGILPTTDAAVLKANNIQSILGIQSIDTGILGAVIAGIIVWMLHERFHNIRLPDALAFFGGTRFVPIISSLVMGLVGLVIPLVWPIFAMGISGLGHMINSAGDFGPMLFGTGERLLLPFGLHHILVALIRFTDAGGTQEVCGQTVSGALTIFQAQLSCPTTHGFSESATRFLSQGKMPAFLGGLPGAALAMYHCARPENRHKIKGLLISGLIACVVGGTTEPLEFLFLFVAPVLYVIHALLTGLGFTVMSVLGVTIGNTDGNIIDFVVFGILHGLSTKWYMVPVVAAIWFVVYYVIFRFAITRFNLKTPGRDSEVASSIEKAVAGAPGKSGYNVPAILEALGGADNIVSLDNCITRLRLSVKDMSLVNVQALKDNRAIGVVQLNQHNLQVVIGPQVQSVKDEMAGLMHTVQA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in maltose transport. MalX can also recognize and transport glucose even though this sugar may not represent the natural substrate of the system.
Catalytic Activity: D-maltose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha-maltose 6'-phosphate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56627
Sequence Length: 530
Domain: The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
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Q9SZY4 | MESKGSWTVADAVDYKGRPADKSKTGGWITAALILGIEVVERLSTMGIAVNLVTYLMETMHLPSSTSANIVTDFMGTSFLLCLLGGFLADSFLGRFKTIGIFSTIQALGTGALAVATKLPELRPPTCHHGEACIPATAFQMTILYVSLYLIALGTGGLKSSISGFGSDQFDDKDPKEKAHMAFFFNRFFFFISMGTLLAVTVLVYMQDEVGRSWAYGICTVSMAIAIVIFLCGTKRYRYKKSQGSPVVQIFQVIAAAFRKRKMELPQSIVYLYEDNPEGIRIEHTDQFHLLDKAAIVAEGDFEQTLDGVAIPNPWKLSSVTKVEEVKMMVRLLPIWATTIIFWTTYAQMITFSVEQASTMRRNIGSFKIPAGSLTVFFVAAILITLAVYDRAIMPFWKKWKGKPGFSSLQRIAIGLVLSTAGMAAAALVEQKRLSVAKSSSQKTLPISVFLLVPQFFLVGAGEAFIYTGQLDFFITQSPKGMKTMSTGLFLTTLSLGFFVSSFLVSIVKRVTSTSTDVGWLADNINHGRLDYFYWLLVILSGINFVVYIICALWFKPTKGKDSVEKENGKGFSVEDC | Function: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63572
Sequence Length: 577
Subcellular Location: Membrane
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P46032 | MGSIEEEARPLIEEGLILQEVKLYAEDGSVDFNGNPPLKEKTGNWKACPFILGNECCERLAYYGIAGNLITYLTTKLHQGNVSAATNVTTWQGTCYLTPLIGAVLADAYWGRYWTIACFSGIYFIGMSALTLSASVPALKPAECIGDFCPSATPAQYAMFFGGLYLIALGTGGIKPCVSSFGADQFDDTDSRERVRKASFFNWFYFSINIGALVSSSLLVWIQENRGWGLGFGIPTVFMGLAIASFFFGTPLYRFQKPGGSPITRISQVVVASFRKSSVKVPEDATLLYETQDKNSAIAGSRKIEHTDDCQYLDKAAVISEEESKSGDYSNSWRLCTVTQVEELKILIRMFPIWASGIIFSAVYAQMSTMFVQQGRAMNCKIGSFQLPPAALGTFDTASVIIWVPLYDRFIVPLARKFTGVDKGFTEIQRMGIGLFVSVLCMAAAAIVEIIRLHMANDLGLVESGAPVPISVLWQIPQYFILGAAEVFYFIGQLEFFYDQSPDAMRSLCSALALLTNALGNYLSSLILTLVTYFTTRNGQEGWISDNLNSGHLDYFFWLLAGLSLVNMAVYFFSAARYKQKKASS | Function: Peptide transporter. Mediates the transport of di- and tripeptides. High affinity, low capacity transporter. Can also transport histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64421
Sequence Length: 585
Subcellular Location: Vacuole membrane
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P46030 | MVSSDFENEKQPDVVQVLTDEKNISLDDKYDYEDPKNYSTNYVDDYNPKGLRRPTPQESKSLRRVIGNIRYSTFMLCICEFAERASYYSTTGILTNYIQRRIDPDSPHGWGAPPPGSPDASAGALGKGLQAASALTNLLTFLAYVFPLIGGYLGDSTIGRWKAIQWGVFFGFVAHLFFIFASIPQAIENANAGLGLCVIAIITLSAGSGLMKPNLLPLVLDQYPEERDMVKVLPTGESIILDREKSLSRITNVFYLAINIGAFLQIATSYCERRVGFWLAFFVPMILYIIVPIFLFIVKPKLKIKPPQGQVMTNVVKILAVLFSGNFIKRLWNGTFWDHARPSHMEARGTIYYNSKKKSAITWSDQWILDIKQTFDSCKIFLYYIIFNLADSGLGSVETSLIGAMKLDGVPNDLFNNFNPLTIIILIPILEYGLYPLLNKFKIDFKPIWRICFGFVVCSFSQIAGFVLQKQVYEQSPCGYYATNCDSPAPITAWKASSLFILAAAGECWAYTTAYELAYTRSPPALKSLVYALFLVMSAFSAALSLAITPALKDPNLHWVFLAIGLAGFLCAIVMLAQFWNLDKWMENETNERERLDREEEEEANRGIHDVDHPIEAIVSIKS | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69942
Sequence Length: 623
Subcellular Location: Membrane
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Q9P380 | MSSIEEQITKSDSDFIISEDQSYLSKEKKADGSATINTADEQSSTDELQKSMSTGVLVNGDLYPSPTEEELATLPRVCGTIPWKAFIIIIVELCERFAYYGLTVPFQNYMQFGPKDATPGALNLGESGADGLSNFFTFWCYVTPVGAALIADQFLGRYNTIVCSAVIYFIGILILTCTAIPSVIDAGKSMGGFVVSLIIIGLGTGGIKSNVSPLMAEQLPKIPPYVKTKKNGSKVIVDPVVTTSRAYMIFYWSINVGSLSVLATTSLESTKGFVYAYLLPLCVFVIPLIILAVSKRFYKHTPPSGSIFVRVGQVFFLAAQNKFNLEKTKPSCTTTVGRVTLKDQWDDLFIDELKRALRACKTFLFYPIYWVCYGQMTNNLISQAGQMQTGNVSNDLFQAFDSIALIIFIPICDNIIYPLLRKYNIPFKPILRITLGFMFATASMIYAAVLQAKIYQRGPCYANFTDTCVSNDISVWIQIPAYVLIAFSEIFASITGLEFAFTKAPPSMKSIITALFLFTNAFGAILSICISSTAVNPKLTWMYTGIAVTAFIAGIMFWVCFHHYDAMEDEQNQLEFKRNDALTKKDVEKEVHDSYSMADESQYNLEKATAEEEIMKST | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68499
Sequence Length: 618
Subcellular Location: Membrane
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P32901 | MLNHPSQGSDDAQDEKQGDFPVIEEEKTQAVTLKDSYVSDDVANSTERYNLSPSPEDEDFEGPTEEEMQTLRHVGGKIPMRCWLIAIVELSERFSYYGLSAPFQNYMEYGPNDSPKGVLSLNSQGATGLSYFFQFWCYVTPVFGGYVADTFWGKYNTICCGTAIYIAGIFILFITSIPSVGNRDSAIGGFIAAIILIGIATGMIKANLSVLIADQLPKRKPSIKVLKSGERVIVDSNITLQNVFMFFYFMINVGSLSLMATTELEYHKGFWAAYLLPFCFFWIAVVTLIFGKKQYIQRPIGDKVIAKSFKVCWILTKNKFDFNAAKPSVHPEKNYPWNDKFVDEIKRALAACKVFIFYPIYWTQYGTMISSFITQASMMELHGIPNDFLQAFDSIALIIFIPIFEKFVYPFIRRYTPLKPITKIFFGFMFGSFAMTWAAVLQSFVYKAGPWYNEPLGHNTPNHVHVCWQIPAYVLISFSEIFASITGLEYAYSKAPASMKSFIMSIFLLTNAFGSAIGCALSPVTVDPKFTWLFTGLAVACFISGCLFWLCFRKYNDTEEEMNAMDYEEEDEFDLNPISAPKANDIEILEPMESLRSTTKY | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68044
Sequence Length: 601
Subcellular Location: Membrane
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Q8LPL2 | MENPPDQTESKETLQQPITRRRTKGGLLTMPFIIANEGFEKVASYGLLQNMILYLMSDYRLGLVKGQTVLFMWVAATNFMPLVGAFLSDSYLGRFLTIVIASLSSLLGMVVLWLTAMLPQVKPSPCVATAGTNCSSATSSQLALLYTAFALISIGSGGIRPCSLAFGADQLDNKENPKNERVLESFFGWYYASSSVAVLIAFTVIVYIQDHLGWKIGFGIPAILMLLAGFLFVFASPLYVKRDVSKSLFTGLAQVVAAAYVKRNLTLPDHHDSRDCYYRLKDSELKAPSDKLRFLNKACAISNRDEDLGSDGLALNQWRLCTTDQVEKLKALVKVIPVWSTGIMMSINVSQNSFQLLQAKSMDRRLSSNSTFQIPAGSFGMFTIIALISWVVLYDRAILPLASKIRGRPVRVNVKIRMGLGLFISFLAMAVSATVEHYRRKTAISQGLANDANSTVSISAMWLVPQYVLHGLAEALTGIGQTEFFYTEFPKSMSSIAASLFGLGMAVANILASVILNAVKNSSKQGNVSWIEDNINKGHYDYYYWVLAILSFVNVIYYVVCSWSYGPTVDQVRNDKVNGMRKEEEEVIKLN | Function: Low-affinity nitrate transporter involved in xylem-to-phloem transfer for redistributing nitrate into developing leaves. Not involved in dipeptides transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65333
Sequence Length: 591
Subcellular Location: Cell membrane
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Q9LVE0 | MVHVSSSHGAKDGSEEAYDYRGNPPDKSKTGGWLGAGLILGSELSERICVMGISMNLVTYLVGDLHISSAKSATIVTNFMGTLNLLGLLGGFLADAKLGRYKMVAISASVTALGVLLLTVATTISSMRPPICDDFRRLHHQCIEANGHQLALLYVALYTIALGGGGIKSNVSGFGSDQFDTSDPKEEKQMIFFFNRFYFSISVGSLFAVIALVYVQDNVGRGWGYGISAATMVVAAIVLLCGTKRYRFKKPKGSPFTTIWRVGFLAWKKRKESYPAHPSLLNGYDNTTVPHTEMLKCLDKAAISKNESSPSSKDFEEKDPWIVSTVTQVEEVKLVMKLVPIWATNILFWTIYSQMTTFTVEQATFMDRKLGSFTVPAGSYSAFLILTILLFTSLNERVFVPLTRRLTKKPQGITSLQRIGVGLVFSMAAMAVAAVIENARREAAVNNDKKISAFWLVPQYFLVGAGEAFAYVGQLEFFIREAPERMKSMSTGLFLSTISMGFFVSSLLVSLVDRVTDKSWLRSNLNKARLNYFYWLLVVLGALNFLIFIVFAMKHQYKADVITVVVTDDDSVEKEVTKKESSEFELKDIP | Function: Low-affinity nitrate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65246
Sequence Length: 590
Subcellular Location: Membrane
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P40739 | MDYDKLSKDILQLVGGEENVQRVIHCMTRLRFNLHDNAKADRSQLEQLPGVMGTNISGEQFQIIIGNDVPKVYQAIVRHSNLSDEKSAGSSSQKKNVLSAVFDVISGVFTPILPAIAGAGMIKGLVALAVTFGWMAEKSQVHVILTAVGDGAFYFLPLLLAMSAARKFGSNPYVAAAIAAAILHPDLTALLGAGKPISFIGLPVTAATYSSTVIPILLSIWIASYVEKWIDRFTHASLKLIVVPTFTLLIVVPLTLITVGPLGAILGEYLSSGVNYLFDHAGLVAMILLAGTFSLIIMTGMHYAFVPIMINNIAQNGHDYLLPAMFLANMGQAGASFAVFLRSRNKKFKSLALTTSITALMGITEPAMYGVNMRLKKPFAAALIGGAAGGAFYGMTGVASYIVGGNAGLPSIPVFIGPTFIYAMIGLVIAFAAGTAAAYLLGFEDVPSDGSQQPAVHEGSREIIHSPIKGEVKALSEVKDGVFSAGVMGKGFAIEPEEGEVVSPVRGSVTTIFKTKHAIGITSDQGAEILIHIGLDTVKLEGQWFTAHIKEGDKVAPGDPLVSFDLEQIKAAGYDVITPVIVTNTDQYSFSPVKEIGKVQPKEALLALS | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in beta-glucoside transport (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64478
Sequence Length: 609
Domain: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Subcellular Location: Cell membrane
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P23462 | MGYRAFALKNLARHAPKYLPFADVASEEVPLSRLLRLSLFQITVGMTLTLLAGTLNRVMIVELAVPASLVSVMLAMPMLFAPFRTLIGFKSDTHKSALGLRRAPWIWKGTIYQFGGFAIMPFALLVLSGFGESVDAPRWIGMSAAALAFLLVGAGVHIVQTAGLALATDLVAEEDQPKVVGLMYVMLLFGMVISALVYGALLADYTPGRLIQVIQGTALASVVLNMAAMWKQEAVSRDRARQMETAEHPTFKEAFGLLMGRPGMLALLTVIALGTFGFGMADVLLEPYGGQALHLTVGETTKLTALFALGTLAGFGTASRVLGNGARPMRWSAGCTDRVPGFVAIIMSSLISQDGIWLFLAGTFAVGLGIGLFGHATLTATMRTAPADRIGLALGAWGAVQATAAGLGVALAGVVRDGLVALPGTFGSGVVGPYNTVFAIEALILIVAIAFAVPLLKRGGR | Function: PucC is required for high-level transcription of the puc operon.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48392
Sequence Length: 461
Subcellular Location: Cell membrane
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O32148 | MSGRRELCTPLRTIMTPGPVEVDPRVLRVMSTPVVGQFDPAFTGIMNETMEMLRELFQTKNRWAYPIDGTSRAGIEAVLASVIEPEDDVLIPIYGRFGYLLTEIAERYGANVHMLECEWGTVFDPEDIIREIKKVKPKIVAMVHGETSTGRIHPLKAIGEACRTEDALFIVDAVATIGGCEVKVDEWKIDAAIGGTQKCLSVPSGMAPITYNERVADVIAARKKVERGIATQADRAALSGNRPITSNYFDLSQLEDYWSERRLNHHTEATTMLYALREGVRLVLEEGLETRFERHRHHEAALAAGIKAMGLRLFGDDSCKMPVVTCVEIPGGIDGESVRDMLLAQFGIEIASSFGPLAGKIWRIGTMGYSCRKENVLFVLAGLEAVLLRHNAGIEAGKALQAALDVYENAGRQAAV | Function: Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used.
Catalytic Activity: (S)-2-ureidoglycine + glyoxylate = glycine + N-carbamoyl-2-oxoglycine
Sequence Mass (Da): 45743
Sequence Length: 416
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 2.6.1.112
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O32140 | MKEQHNALQLMMLGLQHMLAMYAGAILVPLIVGAAIGLNAGQLTYLIAIDLFMCGAATLLQLWRNRYFGIGLPVVLGCTFTAVGPMISIGSTYGVPAIYGAIIAAGLIVVLAAGFFGKLVRFFPPVVTGSVVMIIGISLIPTAMNNLAGGEGSKEFGSLDNVLLGFGVTAFILLLFYFFKGFIRSIAILLGLIAGTAAAYFMGKVDFSEVLEASWLHVPSLFYFGPPTFELPAVVTMLLVAIVSLVESTGVYFALADITNRRLSEKDLEKGYRAEGLAILLGGLFNAFPYTAFSQNVGIVQLSKMKSVNVIAITGIILVAIGLVPKAAALTTVIPTPVLGGAMIVMFGMVISYGIKMLSSVDLDSQGNLLIIASSVSLGLGATTVPALFSSLSGAASVLAGSGIVIGSLTAIALHAFFQTKQPNSADIKT | Function: Uptake of uric acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44862
Sequence Length: 430
Subcellular Location: Cell membrane
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O32141 | MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA | Function: Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Mass (Da): 56560
Sequence Length: 494
Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
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O94462 | MFTAVNSNPNASESISGNSAFNFPSAPVSSLDTNNYGQRRPSLLSGTSPTSSFFNSSMISSNYTFPHGSNKQASLESPVSYSNPIPSLTWLSLDGDSPDSLVSTPTAPSANHHGNPFPNGKQSIKAMPSLVNLQEDSVISKFPNSLEVPFRKRSESTSSSLSGLHSDLRPLKTELYGQLNSECGARFPQTLKSPLTPIGGDSARTVSASTARTSDKFFPRHTRAHSDFWIPATSKPSRHASHSSIGDLTTITQSSISSGSGSFKPSWDGSFDSSLMAHQSYGTSPAFANGNSPTLKNDSSFFGSASVRPTVSPIGTSFRQSLPDISAFGIPKTETNPSEVVAPGTIPISVLPTSNFSAATPANPSLINQNGQEFLQQSRVLYLFHANKQRHFELSDILGNVVLFSTDQHGSRFIQQKLATATEEEREAVFQEIASTSCLQLMMDIFGNYVVQKYFEFGNEKQKQILLSQIKGHVFSLSLQMYGCRVVQKAIEYISPEHQVQLIQELDGHVLDCVCDQNGNHVIQKAIECIDTGHLQFILRALRPQIHVLSAHPYGCRVIQRAIEHCHSERKLIIEELLPHILKLTQDQYGNYVVQHILRTGSESDKKYIFDLMIDHLLFLSCHKFASNVVERCISYISDVDRRRILNKIISEKAENCSILMLMMKDKYANYVIQKLLDASPEEERDLLISYIYPHISVLKKFTYGKHLIMSVERFRQKSISAVPKLASKECK | Function: RNA-binding protein involved in post-transcriptional regulation. Predominantly binds to mRNAs encoding mitochondrial proteins and localizes them to the vicinity of mitochondria for translation. Regulates mitochondrial biogenesis, motility and morphology (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 81069
Sequence Length: 732
Subcellular Location: Mitochondrion outer membrane
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Q07807 | MEMNMDMDMDMELASIVSSLSALSHSNNNGGQAAAAGIVNGGAAGSQQIGGFRRSSFTTANEVDSEILLLHGSSESSPIFKKTALSVGTAPPFSTNSKKFFGNGGNYYQYRSTDTASLSSASYNNYHTHHTAANLGKNNKVNHLLGQYSASIAGPVYYNGNDNNNSGGEGFFEKFGKSLIDGTRELESQDRPDAVNTQSQFISKSVSNASLDTQNTFEQNVESDKNFNKLNRNTTNSGSLYHSSSNSGSSASLESENAHYPKRNIWNVANTPVFRPSNNPAAVGATNVALPNQQDGPANNNFPPYMNGFPPNQFHQGPHYQNFPNYLIGSPSNFISQMISVQIPANEDTEDSNGKKKKKANRPSSVSSPSSPPNNSPFPFAYPNPMMFMPPPPLSAPQQQQQQQQQQQQEDQQQQQQQENPYIYYPTPNPIPVKMPKDEKTFKKRNNKNHPANNSNNANKQANPYLENSIPTKNTSKKNASSKSNESTANNHKSHSHSHPHSQSLQQQQQTYHRSPLLEQLRNSSSDKNSNSNMSLKDIFGHSLEFCKDQHGSRFIQRELATSPASEKEVIFNEIRDDAIELSNDVFGNYVIQKFFEFGSKIQKNTLVDQFKGNMKQLSLQMYACRVIQKALEYIDSNQRIELVLELSDSVLQMIKDQNGNHVIQKAIETIPIEKLPFILSSLTGHIYHLSTHSYGCRVIQRLLEFGSSEDQESILNELKDFIPYLIQDQYGNYVIQYVLQQDQFTNKEMVDIKQEIIETVANNVVEYSKHKFASNVVEKSILYGSKNQKDLIISKILPRDKNHALNLEDDSPMILMIKDQFANYVIQKLVNVSEGEGKKLIVIAIRAYLDKLNKSNSLGNRHLASVEKLAALVENAEV | Function: RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding mitochondrial proteins and localizes them to the vicinity of mitochondria for translation. Regulates mitochondrial biogenesis, motility and morphology.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 98068
Sequence Length: 879
Subcellular Location: Mitochondrion outer membrane
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Q9N3S4 | MEENSADIENRPVAAFRPAVSVPMPVLPQDGEVFVGPGGKKDAQKIGLGLSKLSSKRKDDIQMAKKYAMDISIKQILLRQQKQQQENQQRQQMYSQALSIMSRIYVGSISFEIREDMLRRAFDPFGPIKSINMSWDPATGHHKTFAFVEYEVPEAALLAQESMNGQMLGGRNLKVNSMMFQEMRLPQNMPQAQPIIDMVQKDAKKYFRVYVSSVHPDLSETDLKSVFEAFGEIVKCQLARAPTGRGHRGFGYLEFNNLTSQSEAIAGMNMFDLGGQYLRVGKCVTPPDALTYLQPASVSAIPASVSVACAAITAKVMAAEAAAGSSPKTPSESGGSRAASPAPRAQSPATPSSSLPTDIENKAVISSPKKEPEEIEVPPLPPSAPDVVKDEPMEIEEEEEYTIPEEKPKPVAIVPPPGLAIPSLVAPPGLIAPTEIGIVVPNPSFLAQQQQKIEEKIEEEEEARTERVKLSTSQRKKMKREKLNQMTFEEKMAQVLGQQKAVQNQRMADPVTFGALDDTVAWKDPSNEDQTSEDGKMLAIMGPGRGGDNVASMALALMDGGSSLMLANNAKAKEAAAALALEPKKKKKVKEGKKIQPKLNTAQALAAAAKAGEMSDALKNEVMNSEDASLASQEGLEIRGNDARHLLMTKLMRTNRSNVIVLRNMVTPQDIDEFLEGEIREECGKYGNVIDVVIANFASSGLVKIFVKYSDSMQVDRAKAALDGRFFGGNTVKAEAYDQILFDHADYTG | Function: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation (Probable). Ensures the correct splicing of genes involved in immunity to promote longevity in response to infection by pathogenic bacteria such as S.aureus .
Sequence Mass (Da): 81616
Sequence Length: 749
Domain: The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Subcellular Location: Nucleus
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Q9UHX1 | MATATIALQVNGQQGGGSEPAAAAAVVAAGDKWKPPQGTDSIKMENGQSTAAKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPPAAAVAAAAATAKITAQEAVAGAAVLGTLGTPGLVSPALTLAQPLGTLPQAVMAAQAPGVITGVTPARPPIPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARHMVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYDQERFDNSDLSA | Function: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA.
Sequence Mass (Da): 59875
Sequence Length: 559
Domain: The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Subcellular Location: Nucleus
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Q3UEB3 | MATATIALQVNGQQGGGSEPAAAAAAAAAAVVAAGDKWKPPQGTESIKMENGQSTGTKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPPAAAVAAAAATAKITAQEAVAGAAVLGTLATPGLVSPALTLAQPLGALPQAVMAAQAPGVITGVTPARPPIPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARHMVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSMASETHKAIQALNGRWFGGRKVVAEVYDQERFDNSDLSA | Function: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA (By similarity).
Sequence Mass (Da): 60249
Sequence Length: 564
Domain: The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Subcellular Location: Nucleus
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Q51342 | MCGIVGIVGKSNVNQALYDALTVLQHRGQDAAGIVTCHDDKLYLRKDNGLVRDVFQQRHMQRLIGSVGIGHVRYPTAGSSSSAEAQPFYVNSPYGITLAHNGNLTNVEQLAKEIYESDLRHVNTNSDSEVLLNVFAHELAVRNKLQPTEEDIFAAVSCVHDRCVGGYAVVAMITGHGIVGFRDPNAIRPIVFGQRHTENGVEYMIASESVALDVLGFTLIRDLAPGEAVYITEEGKLYTRQCAKAPKYAPCIFEHVYLARPDSIMDGISVYKARLRMGEKLADKILRERPDHDIDVVIPIPDTSRTAALELANRLGVKFREGFVKNRYIGRTFIMPGQAARKKSVRQKLNAIELEFRGKNVMLVDDSIVRGTTCKQIIQMAREAGAKNVYFCSAAPAVRYPNVYGIDMPSAHELIAHNRSTEDVSKLIGADWLVYQDLPDLIDAVGGGKIKIDHFDCAVFDGEYVTGDVNEAYLNRIEQARNDATKAKSQAVSAIIDLYND | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 55370
Sequence Length: 501
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
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P35433 | MELEESGIREECGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPKFRVHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLMPVSDINDKEKKSSETEGWVVSSESCSFLSIGARYCHEVKPGEIVEISRHGVRTLDIIPRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADLVSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYLAEYLGANSVVYLSVEGLVSSVQQEIKFKKQKVKKRDITIQENGNGLEYFEKTGHCTACLTGQYPVDLEW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 57437
Sequence Length: 517
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
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P77935 | MNQSHSFPTDDPLDGDTLHEECGVFGILGHPDAAALTALGLHALQHRGQEAAGIVSFDGKRFYQERHMGLVGDHYTNPMTLARLPGSISIGHTRYSTTGEVAMRNVQPLFAELEEGGIAIAHNGNFTNGLTLRRQIIATGAICQSTSDTEVVLHLIARSRHASTSDRFIDAIRQMEGGYSMLAMTRTKLIAARDPTGIRPLVMGELDGKPIFCSETCALDIIGAKFIRDVENGEVIICEIQPDGSISIDARKPSKPQPERLCLFEYVYFARPDSVVGGRNVYTTRKNMGMNLAKESPVDADVVVPVPDGGTPAALGYAQESGIPFEYGIIRNHYVGRTFIEPTQQIRAFGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSLKIVQMIREAGAREVHIRVASPMIFFPDFYGIDTPDADKLLANQYADVEAMAKYIGADSLAFLSINGLYRAVGGEDRNPARPQFTDHYFTGDYPTRLLDKNGESMGNKLSMLASNG | Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 54162
Sequence Length: 496
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
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P41390 | MCGILALMLADPHQQACPEIYEGLYSLQHRGQDAAGIVTAGNKGRLYQCKGSGMVADVFSQHQLRQLVGSMGIGHLRYPTAGSCAHSEAQPFYVNSPYGLVLGHNGNLINGPELRRFLDTEAHRHVNTGSDSELLLNIFAYELQRLDKFRINENDIFEALRNVYDRVNGGYACVAMIAGLGVLGFRDPNGIRPLVIGERDTPEGKDYMLASESVVLTQFGYRTFRDIRPGECVFIRRSNREDILAGFRGPRLFSRQILPCLRFTPDIFEYVYFARPDSVIDGLSVYQSRLNMGEKLAHTIMKRFGPDYMEKIDAVIPVPDSARTSALALAQTAQLPYVEAFIKNRYIGRTFIMPGQQIRRKSVRRKLNVQPQEFFDKNVLIVDDSIVRGTTSREIVQMARESGAKNVYLASCAPMITHPHVYGIDLADCKDLIAYGKTEDEVAEAISADGVIYQTLEDLLDSCRTAELTEFEVGLFTGEYTTGASKEYLVHLEQMRIANNRARKHSFAEDEEREAPEDISLHNTHSDVTFDFV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 59832
Sequence Length: 533
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
|
Q5HQA0 | MSNYSGLNEECGVFGIWNHPEAAQLTYMGLHSLQHRGQEGAGIVVSNHETLKGERGLGLLTEAIKDEHMSNIKGYPHAIGHVRYATSGNKGIENIQPFLYHFYDMSVGICHNGNLINAKSLRQNLEEQGAIFHSSSDTEVIMHLIRRSKAPTFEEALKESLRLIKGGFTFAILTKDALYGVVDPNAIRPLVVGKMENGAYILASETCAIDVLGAEFIQDIHAGEYVVITDEGIEVKTYTRQTTTAISAMEYIYFARPDSTIAGKNVHAVRKASGKRLAQENPAKADMVIGVPNSSLSAASGYAEEIGLPYEMGLVKNQYVARTFIQPTQELREQGVRVKLSAVKDIVDGKDIVLVDDSIVRGTTIKRIVKMLKDSGANRIHVRIASPEFMFPSFYGIDVSTTAELISASKSPEEIKNHIGADSLAYLSVDGLIESIGLDYDAPYHGLCVESFTGDYPAGLYDYEKNYKKHLSERQKSYIANNKHYFDSEGNLHV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 54431
Sequence Length: 494
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
|
Q55621 | MFPPSSDLTELNDGQPLSGHHADKPEEACGVFGIYAPEEAVAKLTYFGLYALQHRGQESAGIATFAGTTVHCHKDMGLVSQVFQESKLNEMVGTLAVGHTRYSTTGSSHRVNAQPAVLPTRLGPLALAHNGNLVNTNQLREALAERGCEDFVTTTDSEMIAVAIANEVDKGKDWVEGTIAALTLCAGAYSLVIGTPEGIIGVRDPHGIRPLVIGVLEEETPRYVLASETCALDIIGATYVRTVEAGELVHITESGLVSHRLAESADRKLCVFEMIYFSRPDSVVNDESLYTYRMRIGKHLAKESPVDADLVMGVPDSGIPAAIGFSQASGIPYAEGLIKNRYVGRTFIQPTQHMREHGIRMKLNPLKDVLAGKRIIIVDDSIVRGTTSRKIVRALREAGATEVHMRISSPPVTHPCFYGIDTDSQDQLIAARLTVAEIAEQIEVDSLAYLSQEGMLLCTGEDISHFCSACFNGRYPITVPDAVRRSKLMLENITA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Sequence Mass (Da): 53670
Sequence Length: 495
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
|
Q6F973 | MSNSTSTPNTGLSYKDAGVDIEAGDALVDRIKSVAKRTTRPEVMGGLGGFGALCKIPKGYEEPVLVSGTDGVGTKLRLALNLNRHDTIGQDLVAMCVNDLLVCGAEPLFFLDYYATGHLNVDVAANVVTGIGKGCELAGCALVGGETAEMPGMYEGEDYDLAGFAVGVVEQSKIIDGSKVKAGDVLIGVASSGAHSNGYSLLRKILDVKNVDLTQEIDGRSLADAAMEPTRIYVKPVLELCKQVDVHAMAHITGGGLPGNLPRVLPNGAQAVIDEASWEWPELFKLLQREGGVEQFEMYRTFNCGVGMVIAVDAADADKTIQVLNAQGEKSWKIGHIQDNAESIEGADEKIRVIFA | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 37697
Sequence Length: 356
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
Q8UG98 | MSQSGKNGLTYSDAGVDIDAGNLMVEKIKPAVRSTRRPGADGEIGGFGGLFDLKAAGFTDPVLVAANDGVGTKLKIAIDADYHDTVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLDPDQGAAIVSGIAAGCRESGCALIGGETAEMPGMYSDGDYDLAGFAVGAAERGQLLPAGDIAEGDVILGLSSSGVHSNGFSLVRKIVSLSGLEWSAPAPFADGKKLGEALLTPTRIYVKPLLKAIRETGALKALAHITGGGFPENIPRVLPKHLAAEIDLAAIKVPAVFSWLAKTGGVEAHEMLRTFNCGVGMIVVVSAENATKVTEALTAEGETVFPLGRMVAREDGAHGTIYKGTLGL | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36799
Sequence Length: 357
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
Q7UZR7 | MDYKTSGVDIKAGREFVSEIKQSVESTYSSNVLEGIGGFGGLFKIPLEGLKKPVLVSGTDGVGTKLELAQIKNFHFEVGIDLVAMCMNDIITTGAKPLFFLDYIATGKLEKNQLLEVINGIAHSCRENKCSILGGETAEMPGFYSKNKYDLAGFCVGIADEEKLINGKKICENDLIIALQSNGMHSNGFSLVRKIIENNNQIDKQFEKKYNLDFYDELLKPTKIYFKIVNQILSQNIQIKGMSHITGGGIPENLPRCMSSDFIPYIDKKSWKIPVLFEFLKDVGQIPEKDFWNTFNLGVGFCLIIDKKYKDKILNICNAFDISSWVLGKVLKKNNSKENNFLPEIII | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 38869
Sequence Length: 347
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
|
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