ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q01836 | MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVATEEKAEKSVSATWLNVRSGAGVDHSILTSIKGGTKVTVETTESNGWHKITYNDGKTGYVNGKYLTDKATSTPVVKQEVKKETTQQVKPATEAKTEVKQPTTQQTAPAPKAAETKEAPVVDQNATTHNVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQPTKTVAPKAETKTQAPAAEKQTAPAVKENSNANTATTEKKETATEQQTTTKAPTQAAKPAPAPSTNTNKTNTTNNN... | Function: This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria.
Sequence Mass (Da): 49044
Sequence Length: 467
Domain: LysM domains are thought to be involved in peptidoglycan binding.
EC: 3.4.-.-
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P21171 | MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNNEVAAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNT... | Function: This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria.
Sequence Mass (Da): 50587
Sequence Length: 484
Domain: LysM domains are thought to be involved in peptidoglycan binding.
Subcellular Location: Cell surface
EC: 3.4.-.-
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Q9H3D4 | MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcriptio... |
O88898 | MNFETSRCATLQYCPDPYIQRFIETPAHFSWKESYYRSAMSQSTQTSEFLSPEVFQHIWDFLEQPICSVQPIELNFVDEPSENGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. May be required in conjunction with TP... |
P0CJ81 | MDINKPGWNQSDQQATAYDPNQQQYYGDGSTYYDPDQAVDPNQAYYPDPNTYPDAAAYYGYGQDGQAYPQDYAQDPNQAYYADPNAYQDPNAYTDPNAYVDPNAYQDPNAYVDPNNYTDPNAYYGYGQDGQAYPQDYAQDPNQAYYADPNAYQDPNAYTDPYYVTSTDPNAYYGQVDNVPALEASDLAYEVTPQEQAAEQELFSEPETKVIREIHEFPFEKIRSYFQTDFDSYNSRLTQLKDKLDNAIFSMRKAIDTVKENSANLQIMKQNFERQLKEQQTQRLTSNTDAEKIGAKINQLEERMQRLSRTMESVEWTKKE... | PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47040
Sequence Length: 405
Domain: The penta/hexapeptides repeats form a proline-rich acidic domain. In addition, a part of this region contains a perfect direct repeat.
Subcellular Location: Cell membrane
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Q86YP4 | MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALKETSTEALMKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTGSVGSTVTTPPPLVRGTQNIPAGKPSLQTSSARMPGSVIPPPLVRGGQQASSKLGPQASSQVVMPPLVRGAQQIHSIRQHSSTGPPPLLLAPRASVPSVQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTPASLKGTTAT... | Function: Transcriptional repressor . Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin . Enhances MBD2-mediated repression . Efficient repression requires the presence of GATAD2B .
Sequence Mass (Da): 68063
Sequence Length: 633
Domain: Both CR1 and CR2 region... |
Q8CHY6 | MSEEACRTRSQKRTLEPDLTEDDVENKKMKMEKGSSELTVDGDSRVMPEPSAGSAQGLLRTTEAMGTGSGEGLLGDGPVDMRTSHSDMKSEKRPPSPDVIVLSDSEQPSSPRVNGLTTVALKDTSTEALLKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTASSGSTVTTPPPLVRGTQNIPAGKTSLQTSSTRIPGSIIPPPLVRGGQQVSAKLGPQASSQVVMPPLVRGAQIHNIRQHSSTGPPPLLLAPRASVPSMQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTAASMKGTAVASAQAN... | Function: Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.
Sequence Mass (Da): 67334
Sequence Length: 629
Domain: Both CR1 and CR2 regions ar... |
Q8WXI9 | MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGIEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGVEPQNLRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGLVRTTTPNMNPAINYQPQSSSSVPCQRTTSSAIYMNL... | Function: Transcriptional repressor . Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin . Enhances MBD2-mediated repression . Efficient repression requires the presence of GATAD2A . Targets MBD3 to discrete loci in the nucleus . May play a role in synapse deve... |
Q6SLM1 | LVAVCVSLLGAANIPPQPLNLKQFKNMIQCAGTRTWTSYIGYGCYCGYGGSGTPVDELDRCCYTHDHCYNKAANIPGCNPLIKTYSYTCTKPNITCNDTSDSCARFICDCDRTAAICFASAPYNINNIMISASTSCQ | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities.
PTM: Homodimerization and interaction of the catalytically important Asp-49 (here Asp-111) with mannose molecules may render this protein inactive.
Catalytic Activity: a 1,2-diacyl... |
P0CAS1 | SLVQFEKMIKEVAGKNGVPWY | Cofactor: Binds 1 Ca(2+) ion.
Function: Snake venom phospholipase A2 (PLA2) that induces a conspicuous local myotoxic effect and moderate footpad edema. In vitro, it shows anticoagulant effects and is not cytotoxic on myoblast but is able to lyse myotubes. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl g... |
P86525 | SIPLPSLNFEQFGNMIQCTI | Function: Heterotrimer: Snake venom phospholipase A2 (PLA2) that has presynaptic neurotoxicity. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl. Causes a fade in tetanic contractions. Displays a triphasic mode of action with... |
P0DKU0 | SEIPQPSLDFEQFSNMIQCTIPPGEECLAY | Function: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. Enzymatic activity is essential for the neurotoxic effects . May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1... |
P77455 | MQQLASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARQFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTLWPEDELIPLSKEGGFAARHLLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQMLRVQPNIVAKSIPFTMEADSLNCCVLGEDVTPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQ... | Function: Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reac... |
Q9DDY9 | MAAVSSVASLRGADYENGLRGVAGPSDGGQDPGEDDPMGRGTLDLEMELLEQGRRSRRVGGRTTPGRRSGGRGGSGGGGAGGLEELEDEELEEEEPGELTGDQTIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSVEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFTGHPKGFAYIEFCDKESVRTSLALDESLFRGRQIKVVPKRTNRPGISTTDRGFPRARYRARASSYSSRSRFYSGYTPRPRGRVYRGRARATSWYTPY | Function: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affin... |
P28819 | MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLPIEGVQFHPESIMTSFGKEMLRNFIETYRKEVIA | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P00903 | MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P06194 | MILLIDNYDSFTWNLYQYFCELGAEVLVRRNDELTLADIISLAPAKIVISPGPCTPDESGISLAAIRHFSGQTPILGVCLGHQAIAQVFGAAIVRAAKVMHGKTSPVSHTGQGVFLGLNNPLTVTRYHSLLIDPRTLPECFEVTARSEEGEIMGIRHRVFDLEGVQFHPESILSEQGHQLLANFLNR | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P27627 | MTSVLMIDNCDSFTYNLVDQFSPHGTIVIVKRNHPFYDGEIEAIMALTSICITPGPCYPAEAALNSCSIIGHLAGRIPILGICLGQQALGQARGGLVIFAHGKLSNIEHNGIFAPLFNPPRALPAGRYHSLVVEPARIEVTGQCNQLEVVPQEIMAIRHRDLPVEGVQFHPESILSSNGAAILANLIHRPCH | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P28820 | MAQRRPAGKKIPFQKDSFLQQFEKLAQSRKHHVLLESARGGRYSIAGLDPIATVKGKDGITTIKHGDEMLFKEGDPLRAFHSWFKTLETETNHEFPDFQGGAIGFLSYDYARYIENFKMLSLDDLETPDIYFLVFDDIAVYDHQEESLWLITHVNGSDQETADVKLSELEQMWLTELPAVTSREMKPETAGSFAAPFTEDGFSQAVEKIKQYIASGDVFQVNLSIRQSQSLSVHPYQIYKTLREVNPSPYMAYLETPDFQIICGSPELLVSKKGKLLETRPIAGTRSRGKTNEEDEALANELIHNEKERAEHVMLVDLER... | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P05041 | MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTFGKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFESLPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDRAENLMIVDLMRNDIGRVAVA... | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P27629 | MFTISGVVLITRPVYDEGSLNYCQSGAMNNGILLESVEGNKPRYSIGGAEPIGTINANAVLTAATYAEDVKFTDADPLNGTRVAICNGEDTQQEEMGFQGGALGYFAYDVGRRLEGYNDLGIEDWAIPDLAGSSYEIGVSADHQNDVIVLIAHASADGNDVFITSSRQLSMVAGPTCCASGDVEILRNKLHYYGVIPFSQDDCGFNRLKDYLGSGDMYQVNLGNRNVGAIVMTLFQGYNQLRLMNPGPYMVFLDEANIIMASPEIVLADEANDLNTRPIAGTLMRLNEQDEDGVNAACLGQHHKDRAEHMMIVDLVRNDL... | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P27630 | MASCRMGARSALEPCQVDCLDEAADERCAETPRCHAELLESVTGASRMSRYSIIVLDPIGTIRAAEALTALVDADDVIFKDEDPLKGIRSVFELGDLDPTNHEEIEFQGGALGRFAYDIARRLEAIRDLGDRELAGPDAGTALYDLILYDHQDDVIWILVPNEAGEQDPSEDFRDLVNAWSYDDEFDIGAEFGANYTDDAYADGVDRLKDYLGSGDMYQVNLAQRRVGMISAEDYQLYIRLRDANPAPYMAYLDIDEGLLVASPERIILDEASDLDTRPIAGTLRGRPRAGGDDEDDGRAIDLLRVDKDRAERIMIVDLD... | Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second st... |
P28821 | MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDIKDGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKDIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEVNYGSQSGEATSALQLLYKKEIKNMIHEKGGRAWRSTQ | Function: Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate (By similarity).
Catalytic Activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate
Sequence Mass (Da): 33515
Sequence Length: 293... |
P41586 | MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVN... | Function: This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm m... |
P06875 | MKNRNRMIVNCVTASLMYYWSLPALAEQSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRAQIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLTALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNYPLKFNQQNSQTAALLPRYDLPAPMLDRPAKGADGALLALTAGKNRETIAAQFAQGGANGLAGYPTTSNMWVIGKSKAQDAKAIMVNGPQFGWYAPAY... | Cofactor: Binds 1 Ca(2+) ion per dimer.
Catalytic Activity: a penicillin + H2O = 6-aminopenicillanate + a carboxylate
Sequence Mass (Da): 94643
Sequence Length: 846
Subcellular Location: Periplasm
EC: 3.5.1.11
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P12256 | MLGCSSLSIRTTDDKSLFARTMDFTMEPDSKVIIVPRNYGIRLLEKENVVINNSYAFVGMGSTDITSPVLYDGVNEKGLMGAMLYYATFATYADEPKKGTTGINPVYVISQVLGNCVTVDDVIEKLTSYTLLNEANIILGFAPPLHYTFTDASGESIVIEPDKTGITIHRKTIGVMTNSPGYEWHQTNLRAYIGVTPNPPQDIMMGDLDLTPFGQGAGGLGLPGDFTPSARFLRVAYWKKYTEKAKNETEGVTNLFHILSSVNIPKGVVLTNEGKTDYTIYTSAMCAQSKNYYFKLYDNSRISAVSLMAENLNSQDLITF... | Function: The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase.
Catalytic Activity: a penicillin + H2O = 6-aminopenicillanate + a car... |
Q60136 | MKTKWLISVIILFVFIFPQNLVFAGEDKNEGVKVVRDNFGVPHLYAKNKKDLYEAYGYVMAKDRLFQLEMFRRGNEGTVSEIFGEDYLSKDEQSRRDGYSNKEIKKMIDGLDRQPKELIAKFAEGISRYVNEALKDPDDKLSKEFHEYQFLPQKWTSTDVVRVYMVSMTYFMDNHQELKNAEILAKLEHEYGTEVSRKMFDDLVWKNDPSAPTSIVSEGKPKRDSSSQSLQILSSAVIKASEKVGKERENFVQTSEELGLPLKIGSNAAIVGSEKSATGNALLFSGPQVGFVAPGFLYEVGLHAPGFDMEGSGFIGYPFI... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a penicillin + H2O = 6-aminopenicillanate + a carboxylate
Sequence Mass (Da): 91988
Sequence Length: 802
Subcellular Location: Secreted
EC: 3.5.1.11
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P10601 | MAVAYCCLSLFLVSTWVALLLQPLQGTWGAPLEPMYPGDYATPEQMAQYETQLRRYINTLTRPRYGKRAEEENTGGLPGVQLSPCTSPPVGLIPCSAPWS | Function: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2.
PTM: No icosapeptide-like peptide is cleaved from the C-terminal.
Sequence Mass (Da): 11020
Sequence Length: 100
Subcellular Location:... |
P06303 | MAVAYYCLSLFLLSTWVALLLQPLQGAWGAPLEPMYPGDYATHEQRAQYETQLRRYINTLTRPRYGKRDEDTAGLPGRQLPPCTSLLVGLMPCAAARS | Function: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2.
PTM: No icosapeptide-like peptide is cleaved from the C-terminal.
Sequence Mass (Da): 10975
Sequence Length: 98
Subcellular Location: ... |
Q10E49 | MPPAGSLTDEQLRFFDANGYLVLGSFSSAEEVRAMRDRMAELVDGFDGAGDVFSTKDHRQVKNDFFFKSAENISFFFEEKAFGDDGCLKQAKELSINKVGHALHELDPVFKKFSFGANVSSLFSSLRYKRPAVIQSMYIFKQPGIGGEVVPHQDNTFLYTDPPSCTGLWLALEDATKTNGCLWAIPGSHKNGLKRRMIRDEIDTHFDHPSPTYDLKEFVPLEVKSGDLVVIHGDLIHQSFENLSPVSRHALSLHVIDTEGCEWSKQNWLQRKIPPQPLYEN | Function: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 31700
Sequence Length: 281
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 1.14.11.18
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Q9ZVF6 | MGITGSLTPDQLDFFHSQGYLVIESFASEDEIRGLRKRMDELLNQFDCSVSSIFSTKNQKHTTDNYFFESAEKISFFFEEKAFGDDGKLKQPKQLSINKVGHALHELDPLYKDFTYSSKFSSLASSLGYRRPVVMQSMYIFKQPGIGGEVVPHQDNSFVYTDPQSCTGLWIALEDSTLVNGCLWAIPGSHKNGLVRRFIRGDNGITFDQPSPSYEQKDFVSIEMKAGSLIAIHGDLIHQSFENLSSKSRHAYSLHVVESDGCKWAKDNWIQRAKMPEPLYVLP | Function: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 32028
Sequence Length: 283
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 1.14.11.18
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O18778 | MDRNRASARLTVLLRHLGCRSAGTIIAHHTSGVGSLASFHPQQFQYTRENNVLSLEQRKFYEENGFLVIKNLVSDADIQRFRNEFERICRKEVKPLGLSVMRDVTITKSEYVPSEKVVSKVQDFQEDEELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSNSIVCAWTAMEHIDRNNGCLVVLPGTHKGPLQPHDYPQWEGGVNIMFHGIQDYDKNNARVHLVMEKGDTVFFHPLLIHGSGRNKSQGFRKAISCHFADANCHYIDVEGTSQENIEKEVVDIVRKKYGFKDVTLK... | Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono- branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon a... |
O62515 | MLGKGVVDYTREGSILSAEQRRFYEKNGYLLIRNCVPQYELNRFRQRFQDICEKKVKAPENMTVMKDISIAKSEFKDGEKAITKIQDFADDPVLFEYCKYPGVVDVVKDLIGNPKSNLMAMHTMLINKPPDNGKLTSRHPMHQDLQYFPFRPADFICCAWTAMEKITRANGCLVVVPGTHKGVLLPHEYPKWEGGVNKAYHGIQDYDTSTPRIHVEMEPGDTVFFHPILIHGSGANRTEGFRKAISCHYANDDLCRYVNVEGTTQETLAEEIIEIAKKRLTRYGLDPNTVTLDFADIWRVRAREVNGRRSNL | Function: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 35720
Sequence Length: 312
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 1.14.11.18
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Q50EX7 | MEYANENCNGHASQDICVKGHDQQLDPLNWNMAADALKGSHLDEVKRMVKEFRKPVVRLGGETLTVAQVAAIASQSGTDVTVQLSEASRAGVKASSDWVLQGMINGTDSYGVTTGFGATSHRRTKEGAALQKELIRFLNAGIFGNGTESSHTLPHSATRAAMLVRINTLLQGYSGIRFEILEAITKLLNNNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKATGPNGELLDAVKAFQRAGIDTGFFELQPKEGLALVNGTAVGSGLASMVLFDANILAVLSEVLSAIFAEVMQGKPEFTDYLTHKLKHHPGQIEAA... | Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehyd... |
P07218 | YIAGLLTGRPNSKAVGPSGVVLTAKQAFELANINSEFYELQPKEGLALVNGTAVGSGMASIVLFDANILAVLSEVLSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYMKDAKKLHEIDPLQKPKQDRYALRTSPQWLGPLIEVIRFSTKSIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLALASIGKLMFAQFSELVNDFYNNGLPSNLTASRNPSLDYGFKGAEIAMASYCSELQYLANPVTSHVQSAEQHNQDVNSLDLISARKTNESIEILKLMSSTFLMGLCQAIDLRHLEE... | Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehyd... |
Q9UU83 | MMVIENPFLSTATSSQTPQEDGVYTSSLHNSNNPFLAPKTERVADPVMESMADDLFNSIQKKKEPSPASSASASPVKKSAEALAERSNSSMGTFDPPPRYSKIARARSTHVASSSRHRSPSHNDSSPSTQSSLKSRGSIRRYKSVREGSHRPGRSSKEPLDQIDRLDVTGLYGSGSFHHDGPFDACRPHRNRNSKKAPVAAFPKDSIANSIPKVGETYNDPSVPKDFSRKAIHESLRTKNILQSPYKSVGIEEEFPSSGNNDTPGLTDSTRIEGAMASKNAIARNEEMLAMEKAGLGRKNSLIRKLGLNRSASMMSRTPN... | Function: Involved in cellular morphogenesis and cell wall integrity. Important for the maintenance of a cylindrical cell shape.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46629
Sequence Length: 425
Subcellular Location: Cell membrane
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P35511 | MDLCKKSINDPLNWEMAADSLRGSHLDEVKKMVDEFRKPIVKLGGETLSVAQVASIANVDDKSNGVKVELSESARAGVKASSDWVMDSMSKGTDSYGVTAGFGATSHRRTKNGGALQKELIRFLNAGVFGNGIESFHTLPHSATRAAMLVRINTLLQGYSGIRFEILEAITKLINSNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPNGEKLNAEEAFCVAGISGGFFELQPKEGLALVNGTAVGSAMASIVLFESNIFAVMSEVLSAIFTEVMNGKPEFTDYLTHKLKHHPGQIEAAAIMEHILDGSSYVK... | Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehyd... |
Q05518 | MENRNSSTSSRPFSVNNPFRNATVDSSINQYKNDSQFQEWAKNQSRTNSFDMPQLNTRTSSQLSFPNIPEDEPQRNADQQGAFYSGLESFSSGSLSPPSRPLSSKNPFLDDVSSATDFRRSPPPVSRNKNHPTAKEEKEQLRQRYLEESDVSTVGNTRENTDLPPSYEEITSTNGSRRAYPKEKVSRPSSHREHSNSGTYISRRSSSHHHREASSSSTPSKKGKRKSKVIVPKNVDTIDKLDVTGLFGGSFHHDGPFDAVTPHRNKNNKAAPVLAFPVDGPNSTIGGASTKKSALDEVFGRDDTDDSDIYQYSSQTLRRG... | Function: Involved in the early step of endocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54996
Sequence Length: 499
Subcellular Location: Cell membrane
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Q9W1L5 | MSRLLFVALLAISLGYVASSSSNHLPAGLAMDLGPGVNLNERFFDQVRALIKRRLQEKGLAKPEQPELAMPLTDDDAVALQNQRSYDNVPLPAASVPTPVLVENWPTEQHSFGQVTAVAVDPQGSPVVFHRAERYWDVNTFNESNIYYLIEYGPIKENTIYVLDAKTGAIKSGWGSNMFYMPHGLTIDLHGNYWITDVAMHQAFKFKPFSNKPLLTIGKRFRPGSSVKHLCKPTSIAVATTGEFFIADGYCNSRILKFNAAGKLLRTIPQPPEFLSLQVPHAITLLEHLDLLCIADRENMRVVCPKAGLISSHGEGEPAA... | Function: Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides s... |
Q3M5Z3 | MKTLSQAQSKTSSQQFSFTGNSSANVIIGNQKLTINDVARVARNGTLVSLTNNTDILQGIQASCDYINNAVESGEPIYGVTSGFGGMANVAISREQASELQTNLVWFLKTGAGNKLPLADVRAAMLLRANSHMRGASGIRLELIKRMEIFLNAGVTPYVYEFGSIGASGDLVPLSYITGSLIGLDPSFKVDFNGKEMDAPTALRQLNLSPLTLLPKEGLAMMNGTSVMTGIAANCVYDTQILTAIAMGVHALDIQALNGTNQSFHPFIHNSKPHPGQLWAADQMISLLANSQLVRDELDGKHDYRDHELIQDRYSLRCLP... | Function: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: ... |
Q5AEM8 | MFSLGVQSRLFTRRALFSGFRFNSTTTTTTTASQPRLTWVDYFQLKKQNNRINTIAGVFTGLGGAFITLSYLGNIEIDVEKPIMGFDPLMVMGGAVILGGLVGFLVGPFIGSSIFRLTNRAQLKQFELKNTEFLSRLRIKRPDPSSQSFSNPIPDYYGEKIYSLKDYKQWLRDCNAFRRKSKEFL | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21051
Sequence Length: 185
Subcellular Location: Mi... |
Q6FJJ0 | MLSITQGIVRRSVARPGLIRPLVKCNARYYSDKPEDSLTWTDFFQLRKQERRINVGSSVFTALVGANVSWAYLSTMEIDPTQMIFGFDPLVVVTAGLMASGALGYLMGPAVGSQVFKLTKGNKLAQYNLKNKEFLKHVIQNRVDASSQSFSNPVPDYYGEKIGSVKEYRQWLRDCHAYAKKAKEFL | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20953
Sequence Length: 186
Subcellular Location: Mi... |
P0CP48 | MSRSVFSTLRPVIGQKTTLAPFAFSLRHASSSSSPFSTPTEPTSFHTQPSHSTPTGPLPLTWPSYLSLRRQRRLWSTLTSVPTTFLGLFLGGGYFASLEADPSQLIFGVEPMFVYGGATLGCMALGYLIGPSVGATLFSLTHPSIARGNPAPLEVMDREFYHRIRKNRADPRFQSVQNIVPDFYGEKIVSLSTYRRWLRDQAVYKRKAMHGVPGEDL | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24072
Sequence Length: 217
Subcellular Location: Mi... |
C8VTR5 | MHTTLLSNSMRGAALCTRVSSTTLNPVTLQTSAIYQTISLKNQTRPSSTSTVRFLKASPTLRTSSARPQAQIATSCINAKNTISVRSNSTTSTSAREEAAKLDWNSYFKLRASRRRYTLASSIVSSAVSTVVGVQVLSSQNLENLGAQVMGLDPFVVLGMATAACGAVGWLVGPFLGNAVWGLVNRSYKKAFLVKEKEFFDRIKRYRVDPSSNSMTNPVPDYYGEKIGSVQGYRQWLKDQRAYNRKRRSFIK | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27812
Sequence Length: 252
Subcellular Location: Mi... |
Q4ICM9 | MASPLKTFVLRMPATGLVRSSPKASFSTISAARPASCLSRSPFRKQCFKPAISINKSFSRAVSDKPQPETVQATPQPAPSNVLPPLDWNSFFKLRVKRRRYQMLFSITNGIFAGSGGAIFLSTGSAEPIISQIPLDPFMTLGLMTLAFSGLGWLSGPSVGNQVFYILNRQWKKQMTQKEAIFFERIKRNRVDPTNSSANNPVPDFYGEKISSVAGYRSWLKDQKAFNKKKTANFV | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26093
Sequence Length: 235
Subcellular Location: Mi... |
Q7SEE1 | MLSSTATTMLRAGVSRSSGALQPMLLRSAACPCSPFSMNTKLSQPTSVRPLSTSPSALVLRFRAQQQAQLAQQQLRRASSSSSSSSSSTRPRSDAELDANAAEAAAAAQSAAHAGEPVLDWNTFFKLRKTRRRVQLAFSVIMTLITSGAGGAVLSTGVADAMVAQVPLEPMFAVGLMTASFGALGWLMGPAMGGMVFNALKSKYRGQMEIKEGQFFARIKKHRVDPSASSMGNPVPDFYGEKISSVAGYRQWLKDQRAFNKKRTTFV | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28607
Sequence Length: 267
Subcellular Location: Mi... |
O94539 | MKYTFSNKQGFVMIPIIRPGLVVKRLQSPKIFLTLWKTCYNVKTYSTESIKQKKPQDLNWPTFLKLRKSRRIFETLTSIPTALTGLGLGSAYFLTRTVDPTMTIMGLDLFTLYVIGTIASGGLGWLLGPSIGRKIWTLLHKSQARQIAAREQEFYRHLVKNRVTPQMESYSNPIPDYYGEKIYSLSDYRRWLRDQKAYIQRAFWRTSNR | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24401
Sequence Length: 209
Subcellular Location: Mi... |
Q4P983 | MPVAIAAARYAALSAGASSSRSAIMLSSSHRALSTSSKVASSSSSSNRGTFSPTSPILFSASSSSSSSSSPSSSRELSHLSWDKYLQLRRSRRLAGMVTTIPTTLLAGAAAGSYFLTLELDPTNAIAGLDPVYINAGLTLACTGLGWLIGPTVGNSIWGLLHRSDAKQIAQKDHDFYEHIKRNRVDPTRQSVQNPVPDYYGEKIGSIKQYRQWLRDQAAFRRKAAHGLEQDA | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24904
Sequence Length: 232
Subcellular Location: Mi... |
Q6CFW6 | MSLQMLRSRVALARPTLVRPSVGQMTKRFAGTAPVPLTWERFLLLRTRRRQINFVASIFTGVATSVLAWGFISEAELDLEQQDVFFGLDAFTAAGLGVVAAGFMGSLLGPTIGQLIFKATNSKQWPAFLMKETDFLSHIQKNRVNPRYQSVSNPVPDYYGEKIGSLKDYRRWLRDCAKYNRAREV | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20893
Sequence Length: 185
Subcellular Location: Mi... |
B7JBM8 | MHKKIARWVQDKKSGIKRAVVTAYDYPFARLAAEAGVHGILVGDSLGMVVGGGSDTLGVTLEQMAYHTGMVVRGAGDCLVFADLPFGSYEKGPEQAWAAAVTLLRAGADVVKLEGGAEMASTVAFCTERGINICAHIGLTPQRVRQWGSFQRQGTDADSARRLQADAGALAEAGARFLVLEAVPDALAANITRDIAIPTIGIGAGPDTDAQVLVIHDLLGLGTESPPFARRYIEGGRIMRDALAEYVREVGNSEFPPRRKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q9YE97 | MPGDKVTARRILKMKGSRPIVAVTAYDYPTAWIADEAGVDVILVGDSLGMVVLGYPSTLQVTLDDMVRHTAAVARAAKRPLIVADMPFGSYEPSSSAAVESAVALARVGAEAVKLEGGSEYADRVKAIVDAGIPVMGHLGLTPQRAMRIGGYRPRARGRDEARRLLLDAESLVEAGVFSIVLEFVSEEAAEMVTRRVPVPTICIGSGRRCDGQIIVFHDIVGLSRHTPPFAKKYVDARRIMVEAVTRYAEDVRNGRFPGEEHVVHAKEPLEDIS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q18C32 | MKNTIQTFKNAKYEGKKLSMLTAYDYSIAKIMDECDINGILIGDSLGMVIKGEENTLSVTIDEIIYHTKAVKNGVKNALIVSDMPFLSYHVSIEDAVKNAGRLIKEGGAHAVKLEGGSNVIKQIESIVNAQIPVMGHLGLTPQSVNSFGGFKVQGNTSETARQLIEDAKLIEKAGAFSIVLEGVPTKIAEMVTNSISIPTIGIGAGINCDGQILVYQDMLGMFGDFVPKFVKQYANIGDIMKDSIKNYILEVNTGAFPQEKHSFSINESELEKLY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A5N5W0 | MAKNNVSTFVSAKHNNEKITMLTAYDYSMAKLMDESGINGILVGDSLGMVCLGYKDTLSVTMEDMLHHIKAVTRGAKDALVVGDMPFMSYQTSVYDAVKNAGRIIQEGLAGAVKLEGGVSVYEQVKAIVKAQIPVMGHIGLTPQSVNVFGGFKVQGKDESKAKNIIEDAKRLEEAGAFSIVLEGIPYKLAKIITETVSIPTIGIGAGKYCDGQILVYQDMLGLFSDFKPKFVKSYGNAGEVIRKAFKDYITEVKEGIFPDEEYSFKMDDSIIDKCIKEGV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q9X712 | MSGIDAKKIRTRHFREAKVNGQKVSVLTSYDALSARIFDEAGVDMLLVGDSAANVVLGRDTTLSITLDEMIVLAKAVTIATKRALVVVDLPFGTYEVSPNQAVESAIRVMRETGAAAVKIEGGVEIAQTIRRIVDAGIPVVGHIGYTPQSEHSLGGHVVQGRGASSGKLIADARALEQAGAFAVVLEMVPAEAAREVTEDLSITTIGIGAGNGTDGQVLVWQDAFGLNRGKKPRFVREYATLGDSLHDAAQAYIADIHAGTFPGEAESF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q4JWH1 | MTATSGTSSSTPTGYLVPTKKVRIADLKARKGTGEPFAMLTAYDYSTAVAFAEAGVEIMLVGDSAANVVFGYDATQRISMDEMVYLTAAVVRGAGNAAVVADLPFGTYEASDEQAVKAASEMLHRTGAHAVKIEGGVRIADRIRAITDAGISVCAHIGFTPQSVNQLGGFKVQGRGAGAEQLLADARAVQEAGADMVVLEMVPADVAASVTKELDIPTIGIGAGPDCDGQVLVWHDMAAFPAGGHRPRFAKQWASVGSDLTAAAAAYKREVAEGGFPTQEHCF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A9KEG7 | MIAMNTPDFQRMKKDNKKISMVTCYDYWSACIISQSNVDCILVGDSLAMVMYGHSTTLPATVEIMAQHIQAVSRGAPNKFIIGDMPFCSYRKDLTTSMNAVERLMQAGAQAIKLEGADAHNLKFIHHVVKSGIPVIGHLGLTPQSIYTLGGFKVQGKEPSAAKKLMADAKALAETGCFAVVLECVPSELAELITHSISIPTIGIGAGPATSGQVLVLQDLLGTNNQFQPKYLKKFLNGFELIKKALDDFDQEVKTSTYPHLETHCY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q0K762 | MSYLLDPSRKTITIPKLQAMRDAGEKIAMLTAYDSSFAALLDYCGVEMILVGDSLGNVMQGQQTTLPVTLEQMAYHTECAARGNQTSLLLTDLPFGTYPTPEAAFASAVTLMKAGAQMVKLEGGDWLAPIVKFLVERSIPVCAHIGLTPQSVHALGGFKVQGKTNAGAAQLKRDALALQAAGAQVVLMEAVPAALAGEITQSLTVPTIGIGAGADCSGQVLVLQDMLNVYPGRKAKFVRNFMDGQTSIEAAVRAYVAAVKDGSFPAAEHTFSA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q8ELF4 | MKALKDFMRMKHEGEKISMLTAYDYPSAKQAEAAEIDMILVGDSLGMTVLGYESTVDVTLDDMKHHARAVRRGAKDTYVVVDMPFGTIGIDASTDTAFAIELYRDTHANAIKIEGAHAAPVIKKCHDIGIPVVAHLGLTPQSYGITGYQLQATSKEAAKQLIEDAKLVEKSGAIMLVLEAIPSDLAHVITESLTIPVIGIGAGVGTNGQVLVYHDVLNYGVEHKPKFVKRYGDFSIGVESIKNFHDEVKRQAFPTEEYTYKKQIMNEVDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q311U7 | MSTHAETRAITAADIRAAKNTRRLAMLTAYDYPTASIADEGGMDMLLVGDSLAMVVLGHEDTLSVTLDEMIHHCRAVTRGASRALVVGDLPFMTYEQGPDQAMHSAARLFREGGVRAVKLEGGKEVAPQVEALVKAGIPVMGHIGLTPQRVAALGGFKVQGRSAAAARSLAEDARILEDAGCFALVLEAIPAPVAAHITRTSGIPTIGIGAGAQCDGQVLVVHDMLGLFDRFTPKFVKRYAELRGHAVKAVQQYGDEVRQGEFPAAQHSFGMPEDEQRRWEENVSGADD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q4FMW6 | MNKKILNFIKKKNKTKIISLTAYSKNIASIIDRHCDLVLVGDSLGSVLYSFSSTKKVTLDMMIEHSKSVRMGVKKSLMVVDMPHNTYRNSKEALSNAKKIISKTKCDAIKLEGGKKVIQIIKTLIKNKIPVMGHLGVLPQSATNFKFKGKEIAERKIILRDSKLLEDAGVFSIVLECVESSLAKEITKTVKVPTIGIGASVHCDGQVLVTDDLIGLNKIKARFVKRYSNIEKQINDAALKFKKDVIRSKFPTKKHSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A1VKS3 | MSQAPSESLSATAYGTLPPASTPSARKPLSLPRLREMHAHGEKITMLTAYDATFAAVADAAGVECILVGDSLGMVCQGLSSTVGVTLETMRYHTECVTRGLRRSQGVAWVIGDLPFGTYHESKEQALRSAVVLMQAGAHMVKLEGGGWTTETVRFLVERGIPVCAHLGLTPQTVHALGGYRVQGKTDESAALLRREASALQDAGASMLVLEMVPAALAAEVTQQLTHCATIGIGAGSGTAGQVLVLHDMLGMNLGKMARFVHNFMDGAPSVRGAMEAYVRAVKNVSFPDNSVHAW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A3DDV6 | MRVIETISDLKAIIRTQKNLGRVIGLVPTMGYLHEGHLSLVNMSRQNNDYTVMSIFVNPTQFGPNEDFDRYPRDLERDLKLAEAAGVDVVFAPSVKEMYPDGYKTYVNVEGITEVLCGKSRPGHFRGVTTIVTKLFNIVEPHRAYFGQKDAQQVAVIKKMVKDLNMNVEIITCPIVREEDGLAMSSRNVYLSPEERKSAVILSKSLMEAEELIKKGETDAKKIRKYIIDRIQTEKNAVIDYVEVVNADTLENVDEIKGRVLVALAVKFGSTRLIDNVIVEV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31664
Sequence Length: 281
Pathway: Cofactor biosynthesis; (R)-pan... |
Q6F855 | MKTETTIQGLTASLNPARTTRKIIGFVPTMGNLHQGHLNLVREAKKLCDIVVVSIFVNPIQFGEGEDFENYPRTLEQDSHLLADVGCDIIFAPSVEQMYGKHPRLTNISVADITDDLCGQSRPGHFDGVAVVVTKLFNIVQPNVAFFGQKDYQQLAVIRQLVQDLNLPIDIIGVPIARDHDGLALSSRNGYLSEAERQIAPTIYQSLKLAEQQLHQGVELVDVLDELKFRLTAAGFVVDYVEARQPNLQPIAQFDRDLVLFVAAKLGKTRLIDNLQVKLKA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31209
Sequence Length: 281
Pathway: Cofactor biosynthesis; (R)-pan... |
A0LRC5 | MIATGHGGAERRTTAGDGTARPVVARTIGELRAARAALTGPVAFVPTMGALHDGHRSLLRIARHHGDHVVVSIFVNPLQFGPAEDFDRYPRTLDADLAMCAAEGVDLVFVPPAAEMYPSEPQVRVSAGPLGERFEGSVRPGHFDGVLTVVAKLFQLVQPDVAVFGRKDAQQLALVRRMVADLNLPVQIIAAPTFREPDGLAASSRNRYLTDADRAQARALPTALTTAAAVAAAGGPPSEMIEMARKVLADAAVTLDYVAVVDEATFDEIDDAEWSQRGEGLCIAAIRVGGTRLIDNMPMRKAD | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32219
Sequence Length: 303
Pathway: Cofactor biosynthesis; (R)-pan... |
C1F8U3 | MRRAETIAEIRAAVRELRYRENPRLKGETWGTRSIGFVPTMGALHEGHLSLVRAAKAECDAVVASIFVNPTQFGPNEDFGKYPRTVEADCALLEREGVDAVFLPQVEEMYPAGATTWVEVEELSGRLDGASRPGHFRGVATVVAKLFHIVGPDRAYFGQKDAAQVANLRRMVRDLDFDLEVVVCPIVREADGLAMSSRNRYLSVEERRQGLVLSRALRAMEAGHAAGERDGRRLLAAGASVMAEEPAVRVDYLRVVDPETLVDVEAVSGPALATVAAYVGATRLIDNVLLGETPAAFKL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32598
Sequence Length: 299
Pathway: Cofactor biosynthesis; (R)-pan... |
B7JBM7 | MAIFKDIAGLRQWRQSLHGTLALVPTMGNLHEGHLALVRLAANRAEHVLVSIYVNPLQFGPGEDFANYPRTLDQDLQRLHEAGCQTVFTPDDGLMYPRGRQDISIVMPPRSLSKVLCGASRPGHFAGVCTVLSKLLHMVAPEILILGEKDYQQLRIVQQMVADLNLNVQVLPGPLQREADGLAYSSRNIYLNLAERQVAPLLAETLFDLARRSTNDAAVSDLAATGWERLERAGFLPEYLELRDAQTLQSLALPQPGARWFAAARLGQIRLIDNVIIS | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30789
Sequence Length: 278
Pathway: Cofactor biosynthesis; (R)-pan... |
Q6ALV3 | MKKISSRQEIREQVKKWQEQGLTVALVPTMGCFHQGHLSLIKKGREIADRLIVSLFVNPIQFGPGEDLDAYPRPYEKDSRLAEELGTDVLFCPETTEMYGPNFQTNISVTTLTADLCGAGRPGHFDGVATVVTKLFHLCQPDFAIFGEKDFQQLAMIKQLVIDLDFDLQIISCPIYREDDGLAMSSRNKYLNAEQRLKALCLSQALEVAKDYVLARSAAGKTIESDEVITKARGVIIDAGYEPEYISIVDQQTLEPSPTVQPGNVMALAVRIAERIRLIDNSALLT | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31808
Sequence Length: 286
Pathway: Cofactor biosynthesis; (R)-pan... |
Q729A4 | MQIITEPQTIQQACLRWRADGVHTALVPTMGYYHAGHESLMAHARAVSEKVIVSLFVNPAQFGPGEDFAAYPRDLERDAAMAEAQGVDVLFAPKAEDLYKKDHATWVEVPALSQTMCGLSRPTHFRGVCTVVTKLLMLTMPRIAVFGQKDWQQVAVIRRMVRDLNIPVDIVGRPIVREPDGLAMSSRNIYLTAEERLQAPHIHHGLALGRAITQSGERDAETIKTAIRRYWAQNLPGGEEDYLTIVDPVSLEPVDRLTGATLCATAVRVGQARLLDNMMLLGD | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31345
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
Q54I80 | MKELIICNNIKLIKEEIHKKKIEISKRNNKEYYEIKVGFVPTMGYLHSGHISLVERAKLENDIVVVSIFVNPTQFNANEDLSSYPSDIENDSKLLKNVGTDLLFLPTPDIMYPKESGYSTFVTVESMEQVMEGKSRPGHFRGVATIVTKLLLITTPTNLYIGQKDAMQCICIKRLVADLNIDTNVIICNTIREDTGLAKSSRNSYLSNEEQIQASSIYKILESFKNNINSFTDRQSFINEITKQLEQNPLFKVEYVSIASNITGLEIIDQFPPPKDSNLSLALLFFAEKRKTRLIDIIIL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 34105
Sequence Length: 300
Pathway: Cofactor biosynthesis; (R)-pan... |
Q88DW8 | MNTVKTVRELRAAVARARGEGKRIGFVPTMGNLHSGHAALVTKAAQRADFVVASIFVNPLQFGANEDLDKYPRTLAADQERLVQAGCNLLFAPTVEEMYPDGMSVQTRVSVPQLSEGLCGASRPGHFEGVATVVNKLFNMVQPDLAVFGEKDYQQLAVIRAMVRDLNMPIQIIGEPTVRAEDGLALSSRNGYLTPEQRTAAPALYRTLQHIAAGIGRGQRDFAALVAEGQAQLSAAGFRPDYLEVRHAVSLRPAVINDRDLVVIAAAYLGNTRLIDNLYLHLEEKTA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31190
Sequence Length: 287
Pathway: Cofactor biosynthesis; (R)-pan... |
Q888Q6 | MNTVKTVLELRAAVARARSEGKRIALTPTMGNLHSGHAALVSKAAQRADFVVASIFVNPLQFGPNEDLATYPRTLAADQEKLLQAGCNLLFTPGVEEMYPHGMADQTLVSVPHLSQGLCGASRPGHFEGVATVVSKLFNMVQPDLAIFGEKDFQQLAVIRAMVRDLNMPIQIIGEPTVRADDGLALSSRNGYLDEAQRAAAPALYQAIRQTAEAISAGEQDFETLLNSKKQQLQAAGFRIDYLEIRNADSLRPTTAEDPDLVILAAAFMGKTRLIDNLHLTRG | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30663
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
Q98ND0 | MSRPEVVNSVAALRAQVSDWRRDGLRVAMVPTMGALHEGHLSLIRIAREKAERCVVSIFVNPTQFAPSEDLDKYPRQLARDLDLLARVKADLAFTPTVGAMYPAGFATRISVGGPSAGLESDFRPTFFEGVATVVAKLFLQATPDCAVFGEKDYQQLCVVRQLCRDLDLPVEIIGAPTIRDAHGLAMSSRNAYLDEAELAVARRLNVILHKAAAALAAGTHQDDATGEANRALIAAGFQKIDYVEARESLTLAPWRRDRAGRVLAAAWLGKTRLIDNVDVPVA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30756
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
A5VA26 | MQIVRNIDDLRQEVAKLRISGAPVALVPTMGALHRGHVALVDAARSRGCEVVVSIFVNPTQFGPSEDLDAYPRREAADAAMLDGAGATLLWAPDVATMYPPGFATSISVGGVSERWDGAARPGHFAGVATVVTKLFQQVKPDIAFFGEKDFQQLAVIRRFVADLDIDIEIVGVPTQRDDDGLALSSRNAYLSPEERVTARTLPRALGEAAAAIGRGGDVAAALAAAIARLAEAGFDPIDYVALVDAASLEPIDRLDGPARLIAAARLGGTRLIDNLAVEPAP | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 29653
Sequence Length: 282
Pathway: Cofactor biosynthesis; (R)-pan... |
Q7UTQ8 | METFTSIDAMRAWCREKSRGGNTIGLVPTMGALHEGHLSLVHAAKKDCDHCVTSIFVNPTQFAANEDLDQYPRPIEDDLAMLRDAGVEAVFMPTADEMYPGGPQTHATSVHPSAVAFPLEGVHRPEHFVGVATVVMKLFQAAPSDRAFFGRKDLQQLCVIEHMVRDLNLPIEIVPCDIVREPDGLAMSSRNRYLSDDQRQRALCISKSLNQVEQAFLEGNHDPKQLESIMADHLSPCDSVDYAVVVDRQTLLPISEITQNAVALVAVRVGVTRLIDNRELIVA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31265
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pan... |
Q5WGA5 | MYRTMMKAKLHRARVTESNLNYVGSITIDEDLMDAVDLLENEKVQIVNNNNGERFETYVIKGPRGEGGICLNGAAARKVQPGDVVIILSYAMMENAEALAHQPKVAILDENNRIVEMLGTEPASTVR | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q0AB67 | MQLNMLKCKLHQACVTDTELDYEGSCAIDANLMDAAGIREFEQIHVYNLANGARFTTYAIRGEAGSRMISMNGAAAHLCSEGDRIIICCYANVDESELDRHEPALVYCDGDNRITHQRNGIPLQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B7GHT2 | MFRTLMNAKIHRARVTEANLNYVGSITIDEDILDAVGMVPNEKVQIVNNNNGARFETYIIPGERGSGVFCLNGAAARLVQKDDIIIVISYVLVPEEKLTSHRPKIAIMDEHNRIKELIVQEPAATVL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
O66773 | MLREMLKSKIHRLTVTDADLHYEGSLSLDEYLMELADLKPFEKIDVYNINNGARFQTYVIPAPRYSGEVKLNGAAARLGHKGDLIIIASYAQYTEEELENYAPKLIFVNEKNQPVEVKESTEVK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q8Y603 | MFRTMMNGKIHRATVTEANLNYVGSITIDSAILEAVDMLPNEKVQIVNNNNGARIETYIIPGEPGSGVICLNGAAARHVQVGDVVIIMSYGMFTDEEAKTHEPKIVVLDEKNHIEMILPEEKAHTTL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q2VZZ9 | MMKIIRAKLHGIRVTNADLNYHGSITLDPEQCEMAGIYPMEFVDIWNKNSAARISTYVIFGEPGSRCCVLNGAAARTCQKGDELIIAASADISGPEKLYDIKPRILTFLPDNHVDQVLYYDVFQSEKRPYDFRIVDADKHTIESCHTWPNVDITKLRSDLAAKGWSEAEIDSFIASHFSL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B8IQG9 | MRRIVAGKLHGIYVTDANLNYHGSITLDPDHCEEAGILPMEFVEIWNKNSGARISTYVILGERGSRCCILNGAAARTCQPGDQIIICNSIYIRESELPDIRPRVLTFDSDNRVLDRLEYIVKFDDFGRYRFAIERARSLNHASIAGEPKTVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A2SLT3 | MNRLMLRAKLHRATVTEADLHYEGSCGIDAALLEAADMREFEQIELYNVNNGERFSTYVIPAPPGSGVISLNGAAARKAHVGDLLIICTYAPMNDAEVATHKPKVVLLGPGNRIESVRKF | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B8ELJ7 | MRKLVGGKLHGIRVTESNLEYHGSITLDPAHCEAAGILPLEFVEIWNKNSGARITTYVILGQRGSRCCVLNGAAARTCQPGDELIICSSVYLDGAEITNLSPAVLTFDANNNIVERLHYSVTRDGAGHYQFGIVAEDGEILQPPLKSGMRQKRAS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B0JNW2 | MGTIRLMHAKLHRVRVSEANVDYVGSITIDRELIERVGILPLEEVDVVNLSNGKRFSTYVFPGHTGEICPNGGAALLCQPGDILIIYAYEQRPRQEVLEKGHFAKVLVADAENRCQQFFEQSLIPRGDGRGVEFSSQEC | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q8ZT70 | MLRVIGLGAVGSLFTYFLNRAGVVPEVVQRRRCGEFLFCVEGDCEKLKFREGGAADDVGYTIVAVKAYDSRSVVPHLKGVAVVAQNGIGGYEEIKEAYPNSVPAVVTYGVYREGCRAELRGVGEIYLPSAVSTLAELLERGGGRVRLVEDIEPYRWLKLAVNAAINAITALLQAPNGVIISSPYAQTLALEVAQEVLNVATALGVKMPRNPVEEVLRVASATAKNLSSTARDVAACAKTEIDYINGAVVKYGEALGVATPVNKALFNLIKARESLCNSG | Function: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Mass (Da): 29732
Sequence Length: 279
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.1.1.169
|
Q987N5 | MKITIFGAGAIGGYLAAKLAIAGRTDLSIVARGAHLEAIQANGLRLIEDGEESMAPVRAAAKAEELGAQDYVVLALKAHSLTPALDQIAPLLGDHTSVVTMQNGVPWWYFHGVGGPLEGTRLNAVDPGGAIWQRIGPQRVIGSVVYPAVEVDAPGLIRHVEGKRFSLGEPSGERSERVTLLAEEMVKAGLQAPVRDDIRSEIWVKLWGNLSFNPISALTGSTLAAIVADEGTRALARTMMLEAQAIGESLGVRFPIGVDRRIKGAGDVGEHKTSMLQDLERGRPMEIDALVSAVQELGRLVDKPTPTIDAVLALVRRLAV... | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 34712
Sequence Length: 326
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q9HDU6 | MNNTIYILGAGSIGSLLAYELASLKSINNRVILLLRDKSRVNSFKDKNSTLKIDRLFEENVPHLCCQVTASEPSQLNVQSIENMIVTTKAGQTENALSKYLPYLSKNSNILFVQNGMGAVENVCGKLWPEEQNKPSIYQGVISHGCFQTAPFHFSHAGLGDLKISKVPKNPKKILPDEAAETPCEMIKSLGKSELLRLRYMNYPELLVNQCEKLVINACINPTTATLDCVNGELYNDESAKELFRCIIKECVDIFFKCIPLFKNNEEAEKILNVNRLLDRVMFVGTKVNGANSSSTRQDCLLLRETEIDAINGYVVKLAE... | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 39114
Sequence Length: 350
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
P65666 | MLVYIAGSGAMGCRFGYQISKTNNDVILLDNWEDHINAIKENGLVVTGDVEETVKLPIMKPTEATQEADLIILFTKAMQLPQMLQDIKGIIGKETKVLCLLNGLGHEDVIRQYIPEHNILMGVTVWTAGLEGPGRAHLQGVGALNLQSMDPSNQEAGHQVADLLNEANLNATYDENVVPNIWRKACVNGTMNSTCALLDCTIGELFASEDGLKMVKEIIHEFVIVGQAEGVELNEEEITQYVMDTSVKAAHHYPSMHQDLVQNHRLTEIDFINGAVNTKGEKLGINTPYCRMITELVHAKEAVLNIQ | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 33829
Sequence Length: 307
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
Q5JGC2 | MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSYSTKTALECARQCIGRNTWVLSIQNGLGNEELALKYTPNVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPTGRDDFVDEVASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLELLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKERINRGKTRNISEGC | Function: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid. Prefers NADH rather than NADPH as the electron donor.
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Mass (Da): 34050
Sequence Length: 309
Domain: Cooperative binding of CoA and ketopantoate indu... |
Q9KPQ9 | MNIVVLGPGAVGSLWALHLHSAGHQVALWSRQAQPTITLQLDEEAPISFRNQNLDTLIHADLLLITVKAWQVEAALQPLLPHLNRETILLFMHNGMGAVEAISESLTHFPVLFATTTHGALKATLNQVSHTGFGQTQVGPFNALGARCDFIADVFNHALAPVTWNPEIQQALWRKLAVNCAINPLTAIHQCANGALVAPEFTPIITAILDEVTAVMQAEAISGEAEALRDGVYQVIQATAANLSSMHQDVFHRRPTEIDFITGYVVRKGEQHGIATPVNSALYQQIKTLEQSWSKA | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 32201
Sequence Length: 296
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
P38787 | MTAPHRSTIHILGLGAMGTVLAVDLLRFTNALVVPLFRSQERLAQFQKTNGNNISIRKLYLEGSPIFSYPVEKCECPETFSKKPIDNLVVTTKTYQTKEALAPYLPYINKNTNLILIQNGLGVLELLREEIFTDSKNRPHLFQGVISHGVYQDKAGVFNHAGWAGMKIAKLPWTEEEMIQKKSVVEDDAANNSLVKLLTEPKFAKEFGIEHSTYQEMLFGQLFKFLVNACMNPVTAILDCVNGEMKASCGPVFTSIIDECLQILRVAYRPLFQYHEKYSGNEEYPEMDVNAVLTTDNMVSEVTRIGCDINSRNSSSMRQD... | Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Mass (Da): 42821
Sequence Length: 379
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step... |
P16256 | MQLEVILPLVAYLVVVFGISVYAMRKRSTGTFLNEYFLGSRSMGGIVLAMTLTATYISASSFIGGPGAAYKYGLGWVLLAMIQLPAVWLSLGILGKKFAILARRYNAVTLNDMLFARYQSRLLVWLASLSLLVAFVGAMTVQFIGGARLLETAAGIPYETGLLIFGISIALYTAFGGFRASVLNDTMQGLVMLIGTVVLLIGVVHAAGGLSNAVQTLQTIDPQLVTPQGADDILSPAFMTSFWVLVCFGVIGLPHTAVRCISYKDSKAVHRGIIIGTIVVAILMFGMHLAGALGRAVIPDLTVPDLVIPTLMVKVLPPFA... | Function: Catalyzes the sodium-dependent uptake of extracellular pantothenate.
Catalytic Activity: (R)-pantothenate(in) + Na(+)(in) = (R)-pantothenate(out) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51717
Sequence Length: 483
Subcellular Location: Cell inner membrane
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P9WIK8 | MRIGPVELSAVKDWDPAPGVLVSWHPTPASCAKALAAPVSAVPPSYVQARQIRSFSEQAARGLDHSRLLIASVEVFGHCDLRAMTYVINAHLRRHDTYRSWFELRDTDHIVRHSIADPADIEFVPTTHGEMTSADLRQHIVATPDSLHWDCFSFGVIQRADSFTFYASIDHLHADGQFVGVGLMEFQSMYTALIMGEPPIGLSEAGSYVDFCVRQHEYTSALTVDSPEVRAWIDFAEINNGTFPEFPLPLGDPSVRCGGDLLSMMLMDEQQTQRFESACMAANARFIGGILACIAIAIHELTGADTYFGITPKDIRTPAD... | Function: Required for the biosynthesis of sulfolipid-1 (SL-1), a major mycobacterial cell wall lipid. Catalyzes the acylation of trehalose-2-sulfate-2'-palmitate (SL659) by adding the (hydroxy)phthioceranoyl group at the 3'-position to yield the diacylated intermediate 2-palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D... |
Q7TVL3 | MFSITTLRDWTPDPGSIICWHASPTAKAKARQAPISEVPPSYQQAQHLRRYRDHVARGLDMSRLMIFTWDLPGRCNIRAMNYAINAHLRRHDTYHSWFEFDNAEHIVRHTIADPADIEVVQAEHQNMTSAELRHHIATPQPLQWDCFLFGIIQSDDHFTFYASIAHLCVDPMIVGVLFIEIHMMYSALVGGDPPIELPPAGRYDDHCVRQYADTAALTLDSARVRRWVEFAANNDGTLPHFPLPLGDLSVPHTGKLLTETLMDEQQGERFEAACVAAGARFSGGVFACAALAERELTNCETFDVVTTTDTRRTPTELRTT... | Function: Required for the biosynthesis of sulfolipid-1 (SL-1), a major mycobacterial cell wall lipid. Catalyzes the acylation of trehalose-2-sulfate by adding the palmitoyl group at the 2'-position to yield the intermediate trehalose-2-sulfate-2'-palmitate (SL659).
Catalytic Activity: 2-O-sulfo-alpha,alpha-trehalose +... |
P9WIK4 | MLRVGPLTIGTLDDWAPSTGSTVSWRPSAVAHTKASQAPISDVPVSYMQAQHIRGYCEQKAKGLDYSRLMVVSCQQPGQCDIRAANYVINAHLRRHDTYRSWFQYNGNGQIIRRTIQDPADIEFVPVHHGELTLPQIREIVQNTPDPLQWGCFRFGIVQGCDHFTFFASVDHVHVDAMIVGVTLMEFHLMYAALVGGHAPLELPPAGSYDDFCRRQHTFSSTLTVESPQVRAWTKFAEGTNGSFPDFPLPLGDPSKPSDADIVTVMMLDEEQTAQFESVCTAAGARFIGGVLACCGLAEHELTGTTTYYGLTPRDTRRTP... | Function: Involved in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid that could have a role in anchoring the bacterial capsule. Catalyzes the sequential transfer of two palmitoyl groups onto a single glucose residue of trehalose generating the diacylated product 2,3-diacyltreha... |
Q02279 | MFPGSVIRKLSHSEEVFAQYEVFTSMTIQLRGVIDVDALSDAFDALLETHPVLASHLEQSSDGGWNLVADDLLHSGICVIDGTAATNGSPSGNAELRLDQSVSLLHLQLILREGGAELTLYLHHCMADGHHGAVLVDELFSRYTDAVTTGDPGPITPQPTPLSMEAVLAQRGIRKQGLSGAERFMSVMYAYEIPATETPAVLAHPGLPQAVPVTRLWLSKQQTSDLMAFGREHRLSLNAVVAAAILLTEWQLRNTPHVPIPYVYPVDLRFVLAPPVAPTEATNLLGAASYLAEIGPNTDIVDLASDIVATLRADLANGVI... | Function: Catalyzes diesterification of phthiocerol, phthiodiolone, and phenolphthiocerol with mycocerosic acids, the final step in the phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters (PDIM) synthesis. Can directly transfer the mycocerosate bound to the mycocerosic acid synthase (mas) onto the su... |
P25116 | MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFC... | Function: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.
PTM: Proteolytic cleavage by thrombin generates a new N-terminus that functions as a tethered ligand . Also proteolytically cleav... |
P30558 | MGPRRLLIVALGLSLCGPLLSSRVPMSQPESERTDATVNPRSFFLRNPSENTFELVPLGDEEEEEKNESVLLEGRAVYLNISLPPHTPPPPFISEDASGYLTSPWLTLFMPSVYTIVFIVSLPLNVLAIAVFVLRMKVKKPAVVYMLHLAMADVLFVSVLPFKISYYFSGTDWQFGSGMCRFATAAFYGNMYASIMLMTVISIDRFLAVVYPIQSLSWRTLGRANFTCVVIWVMAIMGVVPLLLKEQTTRVPGLNITTCHDVLSENLMQGFYSYYFSAFSAIFFLVPLIVSTVCYTSIIRCLSSSAVANRSKKSRALFLS... | Function: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.
PTM: Proteolytic cleavage by thrombin generates a new N-terminus that functions as a tethered ligand. Also proteolytically cleaved by cathepsin CTSG.
Location Topology: Multi-pass membrane protein
S... |
Q2HJA4 | MRSPSAAWLLGGVLLLAASGSCNRTVPGNKSKGRSLIGNVDNSPVVAGRGVTVKPGFSVDEFSTSVLTGKLTTVFLPVVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVTWFPLKIAYHIHGNNWIYGESLCKVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMVHPKKQANIAIGVSLGIWLLILLLTIPLYVVKQTSYIRALNITTCHDVLPEEVLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRTLQSSAMDESSGKKRRRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKTRGQSHV... | Function: Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. Can also be transactivated by c... |
P55085 | MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQS... | Function: Receptor for trypsin and trypsin-like enzymes coupled to G proteins . Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho . Can also be transactivated by... |
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