ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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-pho... |
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
S... |
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.
Catalyti... |
P0DUK2 | MVLNHSPPPGLYITGLGSQYPPYLLGPEKLEEFAARFYDVESPGLKKLLQINRSSGIETRSAIRSYESGFATRPEAPTISELAEFYHQAGVDLTTQACKKALRESQISPQHVTHTIGVTCTNQGNPGFDLLVNRKLGLSANVDRMLLHGVGCAGGLAIMRAAAQIACGASMRRKPVRILAFACELCTPNVRHDLAFAEKAPNAENISIAGALFSDAAAAFVLCNEYAMAETEITPLFQLLEWGNSLIPDTVEHMAFFADVDGYRTVLTRDVPQYTKHAIGPMFEKLLPSYQSQIQSSSGEGVGEVAKSLGVSDFDWALHP... | 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,... |
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
S... |
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
Subcell... |
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
Subcell... |
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
Subcell... |
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
Subcell... |
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
Subcell... |
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
Subcell... |
Q0RBB8 | MAGRSNIVVSATVRDALAAGAPVVALESTLIAHGLPRPRNRDVAVELEELARARGVTPATIAVIDGVPRVGLDEPDLRRIADDANVIKLSVRDLPVACATGWTGATTVASTALLAARVGIRLFATGGLGGVHRGAGDSFDESADLVTLAAMPITVVSAGVKSILDIGATLERLETLGITVVGYRTSTFPGFYLPHTTYDLDWRVGDAGQVAATMAAADLLGLTSAIVVANPLPTDQALDPALHDRVLADALAWATERGIRGKAVTPFLLETFHRETGGASLEVNINAVRNNVAVASDIALAWAAKDRSPTDPAAPDPTAP... | 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-UM... |
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-UM... |
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-UM... |
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-UM... |
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-UM... |
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-UM... |
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-UM... |
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-UM... |
Q9YPD6 | MSKYLATSVRLCLMVCIVGWLLMPSYKELDGWCSSLSSLERDKSNWLLTGLSTWFCIVPSGTDQSSLVSYFSPLEKLSKFVQDLDLDFVKLWWLETITLINTLNTTEKLLSGVTFSVVLWYPRILVTVLMLVWKLWFPVRFLVVASSLLCLRILVWPFEVIADVILETCAWFTRKYHKLMDVIEDLMMIPQRVMEWCSGNTAKMVVPTVASCVSESIESKLDRILMALGRKGTVLEAAQPGSDFVECEQWPNGLVAIRRHDGRIVGMGFLVVLNGKWRLVTAAHVARECKRGIMLSAGIDSKTVTFQDLDVVLQTQVDAC... | 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 | MSFLEQIIERAKSDVKTIVLPESTDLRVIKAASMIMKKGIAKVVLIGNEKEIKSLAGDIDLEGVMIEDSLNSEKLEDYANTLYELRKSKGMTIEAARETIKDPLYYGVMMVKKGEADGMVAGAVNSTANTLRPALQILKTAPGTKLVSSFFVMVVPNCEYGHNGTFVYADCGLVENPDADQLSEIAISASKSFEMLVGAKPQVAMLSYSSYGSAKSELTEKVIKATQLAKEKAPHLAIDGELQVDAAIVPEVAKSKAKGSSVAGKANVLIFPDLDAGNIAYKLTQRLAKAEAYGPITQGLARPVNDLSRGCSAEDIVGVA... | 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
|
P39646 | MADLFSTVQEKVAGKDVKIVFPEGLDERILEAVSKLAGNKVLNPIVIGNENEIQAKAKELNLTLGGVKIYDPHTYEGMEDLVQAFVERRKGKATEEQARKALLDENYFGTMLVYKGLADGLVSGAAHSTADTVRPALQIIKTKEGVKKTSGVFIMARGEEQYVFADCAINIAPDSQDLAEIAIESANTAKMFDIEPRVAMLSFSTKGSAKSDETEKVADAVKIAKEKAPELTLDGEFQFDAAFVPSVAEKKAPDSEIKGDANVFVFPSLEAGNIGYKIAQRLGNFEAVGPILQGLNMPVNDLSRGCNAEDVYNLALITAA... | 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
|
O51535 | MLYSFYKVFCLKDYVFKKARIFVKENKLKANIVFPESSDSRVLKAAIVILQKNLADSIILIGKKDTVINSLKEFSNCNDILGRIEVVDPNSFPDIEMYLDEYWSLQKLKGVTKQSLKTQVLDEITFAMLMVRFGYAKSCVCGAVSTSAKVLSNALRIIPKLEGVKIISSFMIMDTLCTARNVDFCFGHNGILFFADCSVVVNPNSLELAEIALQSAKSFKDILNAKPKVALLSFSTKGSSSAKETEKVKNALNIVRNKESDLLIDGELQLDSAIIKDVAEKKCRESLVAGSANVLIFPNLDAGNIGYKLVERFAFAKAYG... | 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
|
P71103 | MDLIESIWECAKQDKKRIILAEGEEKRNLIAADKIIKEGLAELVLVGDENKIKEKASELNLDISKAEIMDPETSLKTETYARDFYELRKHKGMTIEKSEKMVRDPLYFATMALKDGYVDGMVSGAVHTTGDLLRPGLQIIKTAPGVKIVSGFFVMIIPDCDYGEEGLLLFADCAVNPNPTSDELADIAITTAETARKLCNVEPKVAMLSFSTMGSAKGEMVDKVKNAVEITKKFRPDLAIDGELQLDAAIDSEVAALKAPSSNVAGNANVLVFPDLQTGNIGYKLVQRFAKAKAIGPICQGFAKPINDLSRGCSSEDIVN... | 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
|
P77844 | MSAELFENWLLKRARAEHSHIVLPEGDDDRILMAAHQLLDQDICDITILGDPVKIKERATELGLHLNTAYLVNPLTDPRLEEFAEQFAELRKSKSVTIDEAREIMKDISYFGTMMVHNGDADGMVSGAANTTAHTIKPSFQIIKTVPEASVVSSIFLMVLRGRLWAFGDCAVNPNPTAEQLGEIAVVSAKTAAQFGIDPRVAILSYSTGNSGGGSDVDRAIDALAEARRLNPELCVDGPLQFDAAVDPGVARKKMPDSDVAGQANVFIFPDLEAGNIGYKTAQRTGHALAVGPILQGLNKPVNDLSRGATVPDIVNTVAI... | 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
|
Q9ZKU4 | MQSLWIYPEDTEVLGAACKSLLKALKPRYQKIALFSPISGGCEGFGECESLSSLEVHSAIDKQKALELVSTAQEELLFETILKRYDELQSTHDFVINLGYAPKFFLNALLDLNTILAKHLNAPVVAVAQTSLDHLKAMHSHILKKEAPFAIGLFVGETLEKPHFLSASLCKQQCELEASAIENLLQTKSEIITPLAFQRSLEKKAKKQIKKVVLPESEDERILKAAHRLNLMGAVGLILLGDKEAINSQAKNLNLNLENVEIINPNTSHYREEFAKSLYELRKSKGLSEQEAERLALDKTYFATMLVHLGYAHAMVSGVN... | 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
|
P38503 | MVTFLEKISERAKKLNKTIALPETEDIRTLQAAAKILERGIADIVLVGNEADIKALAGDLDLSKAKIVDPKTYEKKDEYINAFYELRKHKGITLENAAEIMSDYVYFAVMMAKLGEVDGVVSGAAHSSSDTLRPAVQIVKTAKGAALASAFFIISVPDCEYGSDGTFLFADSGMVEMPSVEDVANIAVISAKTFELLVQDVPKVAMLSYSTKGSAKSKLTEATIASTKLAQELAPDIAIDGELQVDAAIVPKVAASKAPGSPVAGKANVFIFPDLNCGNIAYKIAQRLAKAEAYGPITQGLAKPINDLSRGCSDEDIVGA... | 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
|
Q49112 | MYTLEEIKNQLGLKSEKKSIVFPEAESEIIQSVAKTLVDEKLGLPILLFKSSKEVPSEIKNNSSIKTICLDEFDTKEFEEEFVKLRKGKATIEVAHQVMQLPNYIGAMLVKLNQADCMLSGLNNTTADTIRPALQIIGTKPGYNIASSIFVMSKGNENYIFTDCALNIKPTSEQLVEITQMAVDFAKALNVKNVEAALLSYSTNGSGKGEDVDRVHQAVEILKSKEKDYVCEGEIQFDAAFDKKTRDKKFKNCSLLKQTPDIFVFPDINAGNIGYKIAQRMGGFEAIGPFVLGLNQPVNDLSRGATFVDVLNTAIMTLYL... | 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
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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
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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
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Q9ZE39 | MKKQHIINETFLDEILAQKLGTTYIPPTEIKDSDFDKAAKHFINLLLRADGLKPIKTAVVHPIDKESLLGAVRAAQFNVIKPILIGPQHKIESVAKVNDVDLENYQVINAEHSHEAAKKAVELAKKREVAAIMKGALHTDELMSAVVYKENGLRTERRISHAFLMAVATFPKPFIITDAAINIRPTLEDKRDIVQNAIDLMHIIKEDKQVRVAVLSAVETVTSAIPTTLDAAALSKMADRGQITNAVVDGPLAFDNAISLFAAEAKGISSPVSGNADILVVPDLESGNMLAKQLKYLGQAVMAGIVLGARVPIILTSRAD... | 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
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P17127 | MFQLSVQDIHPGEQAGNKEEAIRQIAAALAQAGNVAGGYVDGMLAREQQTSTFLGNGIAIPHGTTDTRDQVLKTGVQVFQFPQGVTWGEGQVAYVAIGIAASSDEHLGLLRQLTHVLSDDSVAEQLKSATTAEELRALLMGEKQSEQLKLDNETMTLDVIASSLVTLQALNAARLKEAGAVDAAFVAKTINDSPMNLGQGIWLNDSAEGNLRSAVAVSRATQAFDVEGEKAALLVTVAMNDEQPIAVLKRLGDLLLNNKADRLLSADAATLLALLTSDDALTDDVLSAEFVVRNEHGLHARPGTMLVNTIKQFNSEITVT... | 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 transp... |
Q9KM70 | MLELTTQDIQLQQHFANKQAAIQGLAHALTAKGLVAEGYAQGMLNREAQHSTYLGNGIAIPHGTTDTRELVKQTGVTAMHFPQGLDWGDGNLVYVAIGIAAKSDEHLGILKQLTRVLSADGVEQALQQAKTAQQIIAIIKGEAQLTADFDASLIQLQFPASDMVQMSAVAGGLLKNTGCAENEFVADLVTKAPTHLGRGLWLVASDRAVKRTGMSIVTTANHCEYEQQAVKALIAFSVCNDVHQPLLNTITQCVFEQKQDQLLQADVQQLLNLFSGNAEQTIAQRTIAVGTITEETIAAETVAEPDSARAHTATFRIKNS... | 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 transp... |
P23388 | MIPLTSELVAIGKTATDKADAIAQAVDLLTAAGKIDPRYGQSMMGREAVANTFLGNGIAIPHGLPQDRDLIHDTAIAVVQLPAGVEWAPGDTARLVVAIAAKSDEHLQVLSNLTDVLGDEAEAERLATTLDAAVIVARLTGAAAPVAAPAETPADFAQGIDVVVTGAHGLHARPATTLVDLAKGFAAEIRIRNGAKVANGKSLISLLNLGAAQGAALRISAEGADATAALAAIAAAFEAGLEDEEDTGAAAPEAATPGLTGAGASMASYEGRTLVGISSSPGYALAPVFRFARDEVVFDTDAADAAFETDRLDTALQTAW... | 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 transp... |
P45597 | MSSPSIAPVTPDLVRLRATARDKDDAIAQAAQLLVAAGCVAPGYDASMRRREGLANTFLGHGLAIPHGVGEDRHLVRRDGIAVLQLPEGVEWNPGQTTRLVVGIAAQSDTHITLLRRLTRLIQDPAQLEALFTTDDPAVIVAALTGDRAPDTSAAPATDLAERFEWTIAYPSGLHARPATRWAETARGFSARAQVRAGDQAADAKSLVGLLQLGLRAGDSITVSAKGSDAPALLKRLRAVMDSLTAQEKADAERAAQRRAAPVIGWTPPQAQPAIVGIGASPGVAIGIVHRLRAAQTEVADQPIGLGDGGVLLHDALTRT... | 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 transp... |
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 transp... |
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 trans... |
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 trans... |
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 trans... |
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-histi... |
P20966 | MKTLLIIDANLGQARAYMAKTLLGAAARKAKLEIIDNPNDAEMAIVLGDSIPNDSALNGKNVWLGDISRAVAHPELFLSEAKGHAKPYTAPVAATAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVETRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYEPAGKAQTATTESKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFALMVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGI... | 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 transp... |
P44714 | MKLFLTQSANVGDVKAYLLHEVFRAAAQKANVSIVGTPAEADLVLVFGSVLPNNPDLVGKKVFIIGEAIAMISPEVTLANALANGADYVAPKSAVSFTGVSGVKNIVAVTACPTGVAHTFMSAEAIEAYAKKQGWNVKVETRGQVGAGNEITVEEVAAADLVFVAADIDVPLDKFKGKPMYRTSTGLALKKTEQEFDKAFKEAKIFDGGNNAGTKEESREKKGVYKHLMTGVSHMLPLVVAGGLLIAISFMFSFNVIENTGVFQDLPNMLINIGSGVAFKLMIAVFAGYVAFSIADRPGLAVGLIAGMLASEAGAGILGG... | 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 transp... |
P23387 | MSKIVAVTAGAKGVAHTHLAAEALSATAQALGHQIRVERHSAEGVEAPLQGAEIAAADVVLIAADLRIEDVRFVTKPVYRTSTARAVTQTAAVLAEALALTGEETPQMTTDTGQRPLRVVAITSCPTGIAHTFMAADALKKTAAARGWEIAVETQGSVGSQNALSAAQIQAADLVVIAADTHVDDSRFAGKKVYKTSVGAAVKGAAKVLDAALAEGVVLGTNLADTVDALKAQRAATRSGPYMHLLTGVSYMLPLVVAGGLLIALSFVFGIKAFEVEGTLPAALMAIGGGAAFKLMVPVLAGFIAYSIADRPGLTPGLIG... | 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 transp... |
P23355 | MSSSIVVIAAGERSTEAVLAAEALRRAATAAGRSVTIEIRSDQGVLGALPTELTNGAAHVLIVGDADADTARFGDAQLLHLSLGAVLDDPAAAVSQLAATTAPASTSATTDASGAGGKRIVAITSCPTGIAHTFMAAEGLQQAAKKLGYQMRVETQGSVGAQDALTDEEIRAADVVIIAADREVDLARFGGKRLFKSGTKPAINDGPALIQKALAEAGVHGGAAPVAGANATSDAKGNARTGAYKHLMTGVSFMLPFVTAGGLLIALAFALGGIYAGDDAHQGTLAWSLFQIGAKAGFTLMVPALAGYIAYSIADRPGIA... | 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 transp... |
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 tran... |
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 tran... |
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 tran... |
A0A140JWS9 | MSRVIRSILIILGSVALYTKYYLSFQNGFIDLLSTMGSQGSLAGLQSGLRSHYTGLDPLDRFLKACNVFFWPIFHGTSPALSLYAIAFAGSMIPMWLILLMHTCVNSSIVEIVMINALAGLLVQGIGPGVIMCVLLAMRNTSMKEFAVTGIPAVSILGPNDLPLSLVVCYILPLALSSLPAPASISVPSKQLFIAIWQGWPLYIALAVGIAHSLRNHYRRNRPQQLFRHAYAFALACSIISHVGLLSISFLSVSPQSPFLSLHSADLHPRSLLIPRLPWQEVKITSLESGVLRFLHWDYSISSTGTLLWCYDVYWKDRMR... | 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) . Con... |
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 | MGIGIIIASHGKFAEGIHQSGSMIFGEQEKVQVVTFMPNEGPDDLYGHFNNAIQQFDADDEILVLADLWSGSPFNQASRVAGENPDRKMAIITGLNLPMLIQAYTERLMDAGAGIEQVAANIIKESKDGIKALPEDLNPVEETAATEKVVNALQGAIPAGTVIGDGKLKINLARVDTRLLHGQVATAWTPASKADRIIVASDEVAQDDLRKQLIKQAAPGGVKANVVPISKLIEASKDPRFGNTHALILFQTPQDALRAVEGGVEINELNVGSMAHSTGKTMVNNVLSMDKEDVATFEKLRDLSVTFDVRKVPNDSKKNL... | 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 transp... |
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 transp... |
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 transp... |
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 gr... |
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 c... |
P54715 | MMQKIQRFGSAMFVPVLLFAFAGIIVGISTLFKNKTLMGPLADPDGFWYQCWYIIEQGGWTVFNQMPLLFAIGIPVALAKKAQARACLEALTVYLTFNYFVSAILTVWGGAFGVDMNQEVGGTSGLTMIAGIKTLDTNIIGAIFISSIVVFLHNRYFDKKLPDFLGIFQGSTYIVMISFFIMIPIALAVSYIWPMVQSGIGSLQSFLVASGAVGVWIYTFLERILIPTGLHHFIYTPFIYGPAVAEGGIVTYWAQHLGEYSQSAKPLKELFPQGGFALHGNSKIFGIPGIALAFYVTAKKEKKKLVAGLLIPVTLTAIVA... | 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 Activ... |
P19642 | MTAKTAPKVTLWEFFQQLGKTFMLPVALLSFCGIMLGIGSSLSSHDVITLIPVLGNPVLQAIFTWMSKIGSFAFSFLPVMFCIAIPLGLARENKGVAAFAGFIGYAVMNLAVNFWLTNKGILPTTDAAVLKANNIQSILGIQSIDTGILGAVIAGIIVWMLHERFHNIRLPDALAFFGGTRFVPIISSLVMGLVGLVIPLVWPIFAMGISGLGHMINSAGDFGPMLFGTGERLLLPFGLHHILVALIRFTDAGGTQEVCGQTVSGALTIFQAQLSCPTTHGFSESATRFLSQGKMPAFLGGLPGAALAMYHCARPENRHK... | 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 r... |
Q9SZY4 | MESKGSWTVADAVDYKGRPADKSKTGGWITAALILGIEVVERLSTMGIAVNLVTYLMETMHLPSSTSANIVTDFMGTSFLLCLLGGFLADSFLGRFKTIGIFSTIQALGTGALAVATKLPELRPPTCHHGEACIPATAFQMTILYVSLYLIALGTGGLKSSISGFGSDQFDDKDPKEKAHMAFFFNRFFFFISMGTLLAVTVLVYMQDEVGRSWAYGICTVSMAIAIVIFLCGTKRYRYKKSQGSPVVQIFQVIAAAFRKRKMELPQSIVYLYEDNPEGIRIEHTDQFHLLDKAAIVAEGDFEQTLDGVAIPNPWKLSSV... | 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
|
P46032 | MGSIEEEARPLIEEGLILQEVKLYAEDGSVDFNGNPPLKEKTGNWKACPFILGNECCERLAYYGIAGNLITYLTTKLHQGNVSAATNVTTWQGTCYLTPLIGAVLADAYWGRYWTIACFSGIYFIGMSALTLSASVPALKPAECIGDFCPSATPAQYAMFFGGLYLIALGTGGIKPCVSSFGADQFDDTDSRERVRKASFFNWFYFSINIGALVSSSLLVWIQENRGWGLGFGIPTVFMGLAIASFFFGTPLYRFQKPGGSPITRISQVVVASFRKSSVKVPEDATLLYETQDKNSAIAGSRKIEHTDDCQYLDKAAVIS... | 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
|
P46030 | MVSSDFENEKQPDVVQVLTDEKNISLDDKYDYEDPKNYSTNYVDDYNPKGLRRPTPQESKSLRRVIGNIRYSTFMLCICEFAERASYYSTTGILTNYIQRRIDPDSPHGWGAPPPGSPDASAGALGKGLQAASALTNLLTFLAYVFPLIGGYLGDSTIGRWKAIQWGVFFGFVAHLFFIFASIPQAIENANAGLGLCVIAIITLSAGSGLMKPNLLPLVLDQYPEERDMVKVLPTGESIILDREKSLSRITNVFYLAINIGAFLQIATSYCERRVGFWLAFFVPMILYIIVPIFLFIVKPKLKIKPPQGQVMTNVVKILA... | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69942
Sequence Length: 623
Subcellular Location: Membrane
|
Q9P380 | MSSIEEQITKSDSDFIISEDQSYLSKEKKADGSATINTADEQSSTDELQKSMSTGVLVNGDLYPSPTEEELATLPRVCGTIPWKAFIIIIVELCERFAYYGLTVPFQNYMQFGPKDATPGALNLGESGADGLSNFFTFWCYVTPVGAALIADQFLGRYNTIVCSAVIYFIGILILTCTAIPSVIDAGKSMGGFVVSLIIIGLGTGGIKSNVSPLMAEQLPKIPPYVKTKKNGSKVIVDPVVTTSRAYMIFYWSINVGSLSVLATTSLESTKGFVYAYLLPLCVFVIPLIILAVSKRFYKHTPPSGSIFVRVGQVFFLAAQ... | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68499
Sequence Length: 618
Subcellular Location: Membrane
|
P32901 | MLNHPSQGSDDAQDEKQGDFPVIEEEKTQAVTLKDSYVSDDVANSTERYNLSPSPEDEDFEGPTEEEMQTLRHVGGKIPMRCWLIAIVELSERFSYYGLSAPFQNYMEYGPNDSPKGVLSLNSQGATGLSYFFQFWCYVTPVFGGYVADTFWGKYNTICCGTAIYIAGIFILFITSIPSVGNRDSAIGGFIAAIILIGIATGMIKANLSVLIADQLPKRKPSIKVLKSGERVIVDSNITLQNVFMFFYFMINVGSLSLMATTELEYHKGFWAAYLLPFCFFWIAVVTLIFGKKQYIQRPIGDKVIAKSFKVCWILTKNKF... | Function: Uptake of small peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68044
Sequence Length: 601
Subcellular Location: Membrane
|
Q8LPL2 | MENPPDQTESKETLQQPITRRRTKGGLLTMPFIIANEGFEKVASYGLLQNMILYLMSDYRLGLVKGQTVLFMWVAATNFMPLVGAFLSDSYLGRFLTIVIASLSSLLGMVVLWLTAMLPQVKPSPCVATAGTNCSSATSSQLALLYTAFALISIGSGGIRPCSLAFGADQLDNKENPKNERVLESFFGWYYASSSVAVLIAFTVIVYIQDHLGWKIGFGIPAILMLLAGFLFVFASPLYVKRDVSKSLFTGLAQVVAAAYVKRNLTLPDHHDSRDCYYRLKDSELKAPSDKLRFLNKACAISNRDEDLGSDGLALNQWRL... | 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
|
Q9LVE0 | MVHVSSSHGAKDGSEEAYDYRGNPPDKSKTGGWLGAGLILGSELSERICVMGISMNLVTYLVGDLHISSAKSATIVTNFMGTLNLLGLLGGFLADAKLGRYKMVAISASVTALGVLLLTVATTISSMRPPICDDFRRLHHQCIEANGHQLALLYVALYTIALGGGGIKSNVSGFGSDQFDTSDPKEEKQMIFFFNRFYFSISVGSLFAVIALVYVQDNVGRGWGYGISAATMVVAAIVLLCGTKRYRFKKPKGSPFTTIWRVGFLAWKKRKESYPAHPSLLNGYDNTTVPHTEMLKCLDKAAISKNESSPSSKDFEEKDP... | Function: Low-affinity nitrate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65246
Sequence Length: 590
Subcellular Location: Membrane
|
P40739 | MDYDKLSKDILQLVGGEENVQRVIHCMTRLRFNLHDNAKADRSQLEQLPGVMGTNISGEQFQIIIGNDVPKVYQAIVRHSNLSDEKSAGSSSQKKNVLSAVFDVISGVFTPILPAIAGAGMIKGLVALAVTFGWMAEKSQVHVILTAVGDGAFYFLPLLLAMSAARKFGSNPYVAAAIAAAILHPDLTALLGAGKPISFIGLPVTAATYSSTVIPILLSIWIASYVEKWIDRFTHASLKLIVVPTFTLLIVVPLTLITVGPLGAILGEYLSSGVNYLFDHAGLVAMILLAGTFSLIIMTGMHYAFVPIMINNIAQNGHDY... | 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 simi... |
P23462 | MGYRAFALKNLARHAPKYLPFADVASEEVPLSRLLRLSLFQITVGMTLTLLAGTLNRVMIVELAVPASLVSVMLAMPMLFAPFRTLIGFKSDTHKSALGLRRAPWIWKGTIYQFGGFAIMPFALLVLSGFGESVDAPRWIGMSAAALAFLLVGAGVHIVQTAGLALATDLVAEEDQPKVVGLMYVMLLFGMVISALVYGALLADYTPGRLIQVIQGTALASVVLNMAAMWKQEAVSRDRARQMETAEHPTFKEAFGLLMGRPGMLALLTVIALGTFGFGMADVLLEPYGGQALHLTVGETTKLTALFALGTLAGFGTASR... | 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
|
O32148 | MSGRRELCTPLRTIMTPGPVEVDPRVLRVMSTPVVGQFDPAFTGIMNETMEMLRELFQTKNRWAYPIDGTSRAGIEAVLASVIEPEDDVLIPIYGRFGYLLTEIAERYGANVHMLECEWGTVFDPEDIIREIKKVKPKIVAMVHGETSTGRIHPLKAIGEACRTEDALFIVDAVATIGGCEVKVDEWKIDAAIGGTQKCLSVPSGMAPITYNERVADVIAARKKVERGIATQADRAALSGNRPITSNYFDLSQLEDYWSERRLNHHTEATTMLYALREGVRLVLEEGLETRFERHRHHEAALAAGIKAMGLRLFGDDSCK... | 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 = gly... |
O32140 | MKEQHNALQLMMLGLQHMLAMYAGAILVPLIVGAAIGLNAGQLTYLIAIDLFMCGAATLLQLWRNRYFGIGLPVVLGCTFTAVGPMISIGSTYGVPAIYGAIIAAGLIVVLAAGFFGKLVRFFPPVVTGSVVMIIGISLIPTAMNNLAGGEGSKEFGSLDNVLLGFGVTAFILLLFYFFKGFIRSIAILLGLIAGTAAAYFMGKVDFSEVLEASWLHVPSLFYFGPPTFELPAVVTMLLVAIVSLVESTGVYFALADITNRRLSEKDLEKGYRAEGLAILLGGLFNAFPYTAFSQNVGIVQLSKMKSVNVIAITGIILVA... | Function: Uptake of uric acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44862
Sequence Length: 430
Subcellular Location: Cell membrane
|
O32141 | MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKA... | 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 ... |
O94462 | MFTAVNSNPNASESISGNSAFNFPSAPVSSLDTNNYGQRRPSLLSGTSPTSSFFNSSMISSNYTFPHGSNKQASLESPVSYSNPIPSLTWLSLDGDSPDSLVSTPTAPSANHHGNPFPNGKQSIKAMPSLVNLQEDSVISKFPNSLEVPFRKRSESTSSSLSGLHSDLRPLKTELYGQLNSECGARFPQTLKSPLTPIGGDSARTVSASTARTSDKFFPRHTRAHSDFWIPATSKPSRHASHSSIGDLTTITQSSISSGSGSFKPSWDGSFDSSLMAHQSYGTSPAFANGNSPTLKNDSSFFGSASVRPTVSPIGTSFRQ... | 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 ... |
Q07807 | MEMNMDMDMDMELASIVSSLSALSHSNNNGGQAAAAGIVNGGAAGSQQIGGFRRSSFTTANEVDSEILLLHGSSESSPIFKKTALSVGTAPPFSTNSKKFFGNGGNYYQYRSTDTASLSSASYNNYHTHHTAANLGKNNKVNHLLGQYSASIAGPVYYNGNDNNNSGGEGFFEKFGKSLIDGTRELESQDRPDAVNTQSQFISKSVSNASLDTQNTFEQNVESDKNFNKLNRNTTNSGSLYHSSSNSGSSASLESENAHYPKRNIWNVANTPVFRPSNNPAAVGATNVALPNQQDGPANNNFPPYMNGFPPNQFHQGPHY... | 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 locali... |
Q9N3S4 | MEENSADIENRPVAAFRPAVSVPMPVLPQDGEVFVGPGGKKDAQKIGLGLSKLSSKRKDDIQMAKKYAMDISIKQILLRQQKQQQENQQRQQMYSQALSIMSRIYVGSISFEIREDMLRRAFDPFGPIKSINMSWDPATGHHKTFAFVEYEVPEAALLAQESMNGQMLGGRNLKVNSMMFQEMRLPQNMPQAQPIIDMVQKDAKKYFRVYVSSVHPDLSETDLKSVFEAFGEIVKCQLARAPTGRGHRGFGYLEFNNLTSQSEAIAGMNMFDLGGQYLRVGKCVTPPDALTYLQPASVSAIPASVSVACAAITAKVMAAE... | 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... |
Q9UHX1 | MATATIALQVNGQQGGGSEPAAAAAVVAAGDKWKPPQGTDSIKMENGQSTAAKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPP... | 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 cor... |
Q3UEB3 | MATATIALQVNGQQGGGSEPAAAAAAAAAAVVAAGDKWKPPQGTESIKMENGQSTGTKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATP... | 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 cor... |
Q51342 | MCGIVGIVGKSNVNQALYDALTVLQHRGQDAAGIVTCHDDKLYLRKDNGLVRDVFQQRHMQRLIGSVGIGHVRYPTAGSSSSAEAQPFYVNSPYGITLAHNGNLTNVEQLAKEIYESDLRHVNTNSDSEVLLNVFAHELAVRNKLQPTEEDIFAAVSCVHDRCVGGYAVVAMITGHGIVGFRDPNAIRPIVFGQRHTENGVEYMIASESVALDVLGFTLIRDLAPGEAVYITEEGKLYTRQCAKAPKYAPCIFEHVYLARPDSIMDGISVYKARLRMGEKLADKILRERPDHDIDVVIPIPDTSRTAALELANRLGVKFR... | 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
S... |
P35433 | MELEESGIREECGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPKFRVHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLMPVSDINDKEKKSSETEGWVVSSESCSFLSIGARYCHEVKPGEIVEISRHGVRTLDIIPRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADL... | 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
S... |
P77935 | MNQSHSFPTDDPLDGDTLHEECGVFGILGHPDAAALTALGLHALQHRGQEAAGIVSFDGKRFYQERHMGLVGDHYTNPMTLARLPGSISIGHTRYSTTGEVAMRNVQPLFAELEEGGIAIAHNGNFTNGLTLRRQIIATGAICQSTSDTEVVLHLIARSRHASTSDRFIDAIRQMEGGYSMLAMTRTKLIAARDPTGIRPLVMGELDGKPIFCSETCALDIIGAKFIRDVENGEVIICEIQPDGSISIDARKPSKPQPERLCLFEYVYFARPDSVVGGRNVYTTRKNMGMNLAKESPVDADVVVPVPDGGTPAALGYAQE... | 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 metabo... |
P41390 | MCGILALMLADPHQQACPEIYEGLYSLQHRGQDAAGIVTAGNKGRLYQCKGSGMVADVFSQHQLRQLVGSMGIGHLRYPTAGSCAHSEAQPFYVNSPYGLVLGHNGNLINGPELRRFLDTEAHRHVNTGSDSELLLNIFAYELQRLDKFRINENDIFEALRNVYDRVNGGYACVAMIAGLGVLGFRDPNGIRPLVIGERDTPEGKDYMLASESVVLTQFGYRTFRDIRPGECVFIRRSNREDILAGFRGPRLFSRQILPCLRFTPDIFEYVYFARPDSVIDGLSVYQSRLNMGEKLAHTIMKRFGPDYMEKIDAVIPVPD... | 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)... |
Q5HQA0 | MSNYSGLNEECGVFGIWNHPEAAQLTYMGLHSLQHRGQEGAGIVVSNHETLKGERGLGLLTEAIKDEHMSNIKGYPHAIGHVRYATSGNKGIENIQPFLYHFYDMSVGICHNGNLINAKSLRQNLEEQGAIFHSSSDTEVIMHLIRRSKAPTFEEALKESLRLIKGGFTFAILTKDALYGVVDPNAIRPLVVGKMENGAYILASETCAIDVLGAEFIQDIHAGEYVVITDEGIEVKTYTRQTTTAISAMEYIYFARPDSTIAGKNVHAVRKASGKRLAQENPAKADMVIGVPNSSLSAASGYAEEIGLPYEMGLVKNQYV... | 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
S... |
Q55621 | MFPPSSDLTELNDGQPLSGHHADKPEEACGVFGIYAPEEAVAKLTYFGLYALQHRGQESAGIATFAGTTVHCHKDMGLVSQVFQESKLNEMVGTLAVGHTRYSTTGSSHRVNAQPAVLPTRLGPLALAHNGNLVNTNQLREALAERGCEDFVTTTDSEMIAVAIANEVDKGKDWVEGTIAALTLCAGAYSLVIGTPEGIIGVRDPHGIRPLVIGVLEEETPRYVLASETCALDIIGATYVRTVEAGELVHITESGLVSHRLAESADRKLCVFEMIYFSRPDSVVNDESLYTYRMRIGKHLAKESPVDADLVMGVPDSGIP... | 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
S... |
Q6F973 | MSNSTSTPNTGLSYKDAGVDIEAGDALVDRIKSVAKRTTRPEVMGGLGGFGALCKIPKGYEEPVLVSGTDGVGTKLRLALNLNRHDTIGQDLVAMCVNDLLVCGAEPLFFLDYYATGHLNVDVAANVVTGIGKGCELAGCALVGGETAEMPGMYEGEDYDLAGFAVGVVEQSKIIDGSKVKAGDVLIGVASSGAHSNGYSLLRKILDVKNVDLTQEIDGRSLADAAMEPTRIYVKPVLELCKQVDVHAMAHITGGGLPGNLPRVLPNGAQAVIDEASWEWPELFKLLQREGGVEQFEMYRTFNCGVGMVIAVDAADADKT... | 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)-... |
Q8UG98 | MSQSGKNGLTYSDAGVDIDAGNLMVEKIKPAVRSTRRPGADGEIGGFGGLFDLKAAGFTDPVLVAANDGVGTKLKIAIDADYHDTVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLDPDQGAAIVSGIAAGCRESGCALIGGETAEMPGMYSDGDYDLAGFAVGAAERGQLLPAGDIAEGDVILGLSSSGVHSNGFSLVRKIVSLSGLEWSAPAPFADGKKLGEALLTPTRIYVKPLLKAIRETGALKALAHITGGGFPENIPRVLPKHLAAEIDLAAIKVPAVFSWLAKTGGVEAHEMLRTFNCGVGMIVVVSAENAT... | 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)-... |
Q7UZR7 | MDYKTSGVDIKAGREFVSEIKQSVESTYSSNVLEGIGGFGGLFKIPLEGLKKPVLVSGTDGVGTKLELAQIKNFHFEVGIDLVAMCMNDIITTGAKPLFFLDYIATGKLEKNQLLEVINGIAHSCRENKCSILGGETAEMPGFYSKNKYDLAGFCVGIADEEKLINGKKICENDLIIALQSNGMHSNGFSLVRKIIENNNQIDKQFEKKYNLDFYDELLKPTKIYFKIVNQILSQNIQIKGMSHITGGGIPENLPRCMSSDFIPYIDKKSWKIPVLFEFLKDVGQIPEKDFWNTFNLGVGFCLIIDKKYKDKILNICNAF... | 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)-... |
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