ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
|
|---|---|---|
A0A6C1PFU3 | MASRPIAYLDSGLGGFPYFDASRRALPHLAHVYYADTASFPYGERAPAELSAIVTSAVDRLIADFDPMMVVVACNTASVVALDALRATFALPFVGVVPAIKPAAERYGTGPIGLIATTRTVEDPYVSALIRRYAPESRVVMVAAGGLVDRIERNGADISASELNDVLRGPIATLATERVRCVVLGCTHFIHVRNHVQSMLGDGVALVDSVEGVTRQIVRVAGADNSQPSPSPSPPQSVLVLSSRAEIPAAYERIARSRGLLVHRAEEGAP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 270
Sequence Mass (Da): 28641
|
A0A6I7QSQ4 | MDSWNGAFAIGIIRRPHGLKGALKVFSFSGETKHFAGLREVELRRDSARLRYAVTSVEIHNDTPVLFLDGVSDPDIAQTLRGYELWVPRELAAPLKEGEYYVRDLVGLNVVVGRDPIGTVVAVVDGSQAPLLEISREGRKGTLLVPFMDPFVGVPQEQSRTVEILEPWILDTE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19196
|
G9WXU3 | MQYQDFNFHTHTYRCGHAVKTEDDYIQSAIQSGFKVLGFSEHCGYEGFDSPRERIPFKEMDNYFSDIKNAEEKYKSDIKIYVGLEFEYFDDLNSYYTELKEKYDYLIIGQHLKDRKGYDYTYRCTDKDVRYMAYQVCTALENGFTKYVAHPDYFMLARDNYSKDCETAVREIVQCAKKNNAIVEINLKGMRYGIQQYDGYKSYKYPHSKTIEIYKEENAKVVIGYDAHNPQVLLQREYEEIARRIGEGLEILQDYREILFDKKR | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 264
Sequence Mass (Da): 31530
|
A0A1Y3BBR0 | MPSSAISSITIPNGVYDQQPSTDLNNNPINELNSSNVKNVKIAIDPIVTNGYHYDDEDVEQIDKNIQQYCSIPGEPKETAELDCNNQQQPQDRNGNAEKLMKEHPPCPGKLDYVADPKIITKNRWQKIWHTACRLKWNNIFYLSALHITCVFACYHAAVYPVKFWTAASAITIGYLSGMGMSVGAHRYWAHRSFKAKPILRLALMLLQTMTMNGTIFSYARDHRNHHKYSDTEADPKNPAKGLFHAHVGWWLWKKSPVVIAMGKKFDVSDLLNDPLISFQRRFYVPLFLVINVILPTVVPWLLWNENLLTAFYVIVIIRTTVVLHLLFCVNSVAHHYGFRPYDFRIRPADNRIINYLSMGEGNHNYHHVFPYDYRSNEKEYWEYFDPISHFIHITQIIGLTYDCKKASPRVVMGIVRRKGIPAHFDHHRSLTFRILNAAFDWVAGSVVTLWFLYPFLIYKYMTDREIFIYRWQT | Subcellular Location: Membrane
Sequence Length: 474
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 55176
Location Topology: Multi-pass membrane protein
|
A0A0B4XIX5 | MLYVFDIESGVLRERGDQPNEVKQLESARWIDLVAPEDDEVALLNAMRRGSLPDIDDVEEIESSARFFTDEQGIHVHSLFLYQSEGRHRTTTVAFVLSNDQLLTLRDSEVADFRLMRMRARRGWVKVDDPFDILLSVLEQKVENMADNLEDMHRQLENVSQIVLEDENSVMEDAIDRLAKLEDSNGKTRLCLMDTQRSISFLQRHLRNDVERRATCLEIQHDLDTLMTHTNFLFEKINFLMDTAQGFINIEQSQIIKTFSIAAVVFLPPTMVASVYGMNFRIMPELDWTLGYPFALLLMFLSGLAPYLYFKYKGWF | Function: Mediates influx of magnesium ions.
Catalytic Activity: Mg(2+)(in) = Mg(2+)(out)
Subcellular Location: Membrane
Sequence Length: 316
Sequence Mass (Da): 36703
Location Topology: Multi-pass membrane protein
|
A0A812NDG1 | MESTLASEGGSAVELGQPTRTASASGSEEEATDWEALLISQHRAGKKYKYRERYETERIGAFTDAAVAIIITIGVIPLALVEESEADIPPSRLIASKKDTIGTFAVVYWWLASFVEGHFQILSQVDAITAKIVGLNNLWLLCLALVPFTFIVASEYIDQLSALTFMNIAAAMTAAGQLFLGRAVRSLRPENTASAPSHRVNFARHFSVFLGFCVNLGIVFALVAAEVDVPSWGTTMIFIFTALLPSTTARWTMWCSKCRLPSYFTKENARLRAREIRPDPSRVGGRIAALTDGVLAVVGTLTLLEIRAPPVGEQEDVSLISIFVDNRFNIISFALTFSLMLMYWTVHHDITGHVRAWPLGMRWLNMFFLYSVCFLPFAFSLMAHHPVNKVSLAFVTSLVFVSSTVLLFVQMLATRSSNSAVERASKRKVWVWTEAEPKLLRSSLAWILWMRAAIVPCAALLQFIFLAVWPEASLAPMLVAIAIAIPLQFSLQKRWASAAVEAYIADDLYSPGTIPRVAALQRGRPPSVHINAPDL | Catalytic Activity: H(+)(in) = H(+)(out)
Subcellular Location: Membrane
Sequence Length: 535
Sequence Mass (Da): 59072
Location Topology: Multi-pass membrane protein
|
A0A974A158 | MAYVEIENVSKAYGPYKIIEGLDLNVADKEFVVLVGPSGCGKTTTLRMIAGLETVTSGTIRIGNRDVTQLRPGLRNCAMVFQNYALYPHMSVGENIAYGMKVRGEPRASIEKAVKDVARVLDLEQYLDRRPKQLSGGQRQRVAIGRAIVRSPDVFLFDEPLSNLDAKLRIEMRTEIKALHRRLAKTIVYVTHDQVEAMTMADRVVVMNRGRIEQAADPITLYEKPSNLFVAGFIGAPSMNFIHGKIAARDGALLFTEPSGTALRLPKSREAAYAGSIGKPVVLGVRPDHVLPQGSPAGSTIRMIVKDVEPLGPHTLVIGAVSDFPFTAQVPVGTHRRAGSALRRRNRSRARASVR | Function: Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Membrane
Sequence Length: 355
Sequence Mass (Da): 38904
Location Topology: Peripheral membrane protein
|
A0A0G0T0Q3 | MRLYRFFVKFKINGDAVFVEDANFVNQVRNVLRMELGDSILLCDDGIDILSELESFDGNKVILKKIKESKNDSEPEKKITLYCSILKHDNFEVVAQKAVEVGATNIVPIVSARTVKTNVRLDRLEKIVKEAAEQSGRAIIPTVCGVMTFEEALTSAKSNDANIIFDVSSHDLPDKSDYGINLGIFIGPEGGWTEEEVERARINGFKVFSLGKLVLRAETAAIIATYIFAK | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25578
|
A0A1G3CDA3 | MKIDKKTIEYIANLSRIELSNQEKETFVHQLSDILAYIEKLNQLNTQDIKPMAYSINTTNVLRDDKLEPPISREDALINAPSTMGVFFKVPKVIE | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 95
Sequence Mass (Da): 10923
|
D5XB96 | MSGIVERITYTNEETGFSVIRIRSRGFNGLVTVVGNLAAVSVGAVLRLKGEWKHDSKYGKQFNAHDYRETVPATVAGIEKYLGSGLIKGIGPVYARRIVNHFREDTLRVIEEQADRLLEVEGIGQKRVEMIKKAWQEQKEIKNVMLFLQSHGVSASYAVKIYKTYGNESINIVKTNPYRLADDIWGIGFKTADKIARQLGFDKNSYERCRSGIIYVLNELANEGHCFAVREQLVSETVKILELEEPMVKSTIDRMVEEKWVIPDENNAVYLPPFYFSETGTAKRIKEILAVQAPEPAVDIERVIKEVQAECGITYDEVQLEAIKTAVTSKFMVLTGGPGTGKTTATLAIIRVFQKLGASCILAAPTGRAAKRLSETTGMEAKTIHRLLEYKPPEGYRRNGENPLECDVLVVDETSMVDIILMYNLLKAVSNETVVILAGDVDQLPSVGAGNVLKDIIDSGTVPVVRLTRIFRQAMGSAIITNAHRINRGEMPNLRGGRNSDFFFIEEEDPLKVTETVKDLCTKRLPGYYKIDPINDIQVLCPMQRGGTGAQNLNTVLQEALNPTNVTIKYGGTVFRLNDKVMQIKNNYEKNVFNGDIGTIVKIDMEDKTLVIRFDGNDVDYDATELDEVVLAYATTVHKSQGSEYKVVVAPFTMQHYMMLQRNLLYTCVTRAKQVFVLVGSKKAVAIAVSNNKIQRRNTMLAKRLAQLG | Function: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 709
Sequence Mass (Da): 79126
|
A0A813A5V9 | MAARTVGGRSNIADILTHEELVQDVLPVATGTVEVNKEHVESFLECAICRGVMQEPVMIKQCLHRFCKNCLEHSLRTLKNECPLCRTRVPSRRSLERDTRFAKLIELVYKDVGEYEAQQSSKLMAAAAASRANAAAILQAARTTRQGHHDQDSAVIREQTARLQRDAAALADVAAAAAATPTAPAVSAGKRPREAPAQAPKATAQPKRARRDEGQADVPPVIFKLGRVPEAGLLGPCFSSGIGGSQGKFHQMP | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 253
Sequence Mass (Da): 27263
|
A0A6C1PNT2 | MVRAAEHRVDARRQPRQLARRSLLRTGSDGPGTRSRDVQVLAASTGRGHPVVPRRRDQGYYSGRDRNPIVRVARWLAPFLLLAFVTHSLVTTLLAMPIVAASVASQPTVRPTDRLLVAPIVYGPRLPTLGIRLPGLRLPDRGDLVLVRPAFVSHPGFVVRAIDPVVRFVTLGRVSPAQRGRGRTGHQIKRVIGVPGDTVRVERFVAYIRPREAIAFFIEYDLARRPYSLSTDPRPAAWLGTDPFGDAAREVTLGDGEYFLLSDDRSIGIDSRHWGPIGLDDIVGKVWLRYQPFRDFGRL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 299
Sequence Mass (Da): 33352
Location Topology: Single-pass type II membrane protein
|
A0A6C1PF73 | MKTRFRVAAFVAAALLALLTVSCVPRTIPRVSQTELLLGTAVTITVQQAGASRDMLGGAFARTKDIQNRMSINDAAYDDTEVLRVNAAAGESRVRVSPDTFRVIAEGVRFGELSDGAFDLTVEPLIRLWGFGRDEPRVPDPDALAQVLRLVDFRRIELFGDTFEVFLPDQSMGIDVGGIAKGFAADEAAAVLRSDGVRHAILDFGGDIVTIGPRPDGAPWRIGIQYPTGERGRYLGILQSRDESVVTSGAYERFFVQDGVRYHHIFDTRTGMPSDSGVVSATVIGESAMKTDALSTAAFVMGVEAALAMVRDLPGYDAIIATADTIYMTPGVSKRFESRADDYRVVVVER | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Subcellular Location: Cell inner membrane
Sequence Length: 350
Sequence Mass (Da): 37915
Location Topology: Lipid-anchor
|
A0A6C1RJC3 | MNRYPDHPALPSHRVSVAPMMEYTDRHYRYFLRRITRCALLYTEMITAAAIIHGDRDWLLDFHPQEHPLALQIGGDDPAACAESVRIASLYNYDEFNLNVGCPSDRVQEGAFGACLMADPHKVARITRAMKDATDRPVTVKHRIGINGRESYDQMRSFVETVAEAGADRLIVHARIAVLGGLSPKENRSVPPLRYHDVYRLKRELPQLTIEINGQIATVEQMHGHLNHVDGVMIGRAAYDNPWLFADVDREFFGRQHEAPSRGAVIEQMIPYIEQLRSETGKHPRAVLRHMLGLFAFQPGARRWKQHLSGPIDHDVDIVALLNRATAALPDDVLDRVPAAV | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
EC: 1.3.1.91
Catalytic Activity: 5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20) in tRNA
Sequence Length: 341
Sequence Mass (Da): 38508
|
L8GGX4 | MVKSCVLLFWACLVIGLVLASHVLGAPKADLFDFYADSDELDLEDVPLTPEEEAEEALFASFSPDDDEFMEILNNEDEAVLTGRQTTVDIIQQLKDLRDRRLREAEKPKEELQRVQGQQELKEEVAAKEAEVSAADAKKAEAVVALTAKSFDEALQKYPYAFIEFYAPWCGHCKKLAPELEDAARQLAGQPGVLVAKVDCTVEEVLGRRFDVRGYPTMKFFRHGKYLQDYELGRTAAELVAFIKKKSVPITVALNTVEEVNDFMAAHPTSLIVYAEPNSDALLGVRDTANQAVVEGFAFGEVSDPELIVKLGEQVDTVKVYRSFAPDEPHVLRNPTPASILGAVLAYGFPYVNNGPEAWDRVMSRKVPIIILFVDMEGEGVQNTLDWFTEVAKENIHRFSFLYAGKDFHSRLPTLGASGDIIPTIVAVDAETTKSWPFDESKDLNRENVEALLSGIADRTLRPHYTSERPPEDNSGDVLVVVGDTFEELVLNNDKDVLIEFYAPWCGHCKQMAPTWEKVGQHFAQDPDIVVAKIDASANDNPAVVVAGYPTIFLFPAGNKSNPIEYKGLTRHFDDFVAFVEDNATILATGMLMATTMTTCNARVDVD | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 607
Sequence Mass (Da): 67326
|
A0A812N8Z8 | MPLPTPTLLTSKGKSSPVAEDKVQKDDRGADEEDSVSSAAESRARFMIEGVDVRPYLPTVGAPCFHSPGPMFKFSVSENLHLPQRYCAYADPGQMQETVDVEQGMPQRAHKSWQYPLPILRHDHYCKWINNVIGLRNHRSFVVMLFGLAALGVVGCTVDAWLFMALLIQEGIYVTPLQFFFLFFHLLYSLTLLYLDGPIIRIHWGLICRNELNQEWKEDAFWVAPGESHTPAKELGVEEYNALLDSDSLVYDASRNHFDQGVASSNIYPFDARLRSTGLSDLPPRTLRRQAKAMKRPASTAKLDPLQSYCDQVQEGLESSKVPPAVTRMLSGMVRSALLTSKDKRHKYQASVVQMVTDTIQGVGEDFEQAIADQKSKIANSETERAEREAAVKGAKEDFDAKKLLTQEKKYALAADAQAFKAAKEGVSKAQAAMREADKDLLDREKAKENLESIVTDLVTPLVQGAVTGDDARRSAENLLASLKKLALLDESLLTAIPEAITKEPAMRGAFDTSVVSGLQEELERRRAAVAQELAASTPQKEQRKGELSQAEAAFEDAKAKQHVGAEAYTEARSAQSTAEASVKQAQKALSQLDPQVKALQKDLKKLEAELADFYAGPRSALAELSERIEPTEPEVTEQADA | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 642
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 70893
Location Topology: Multi-pass membrane protein
|
A0A9E3Z5P0 | MFDIGWSEMAIVMLVALVVIGPKDLPRVAREIGRWTGKARAMARDFHRAIDDMAREADLDDLKKTVDDARSISSRRGLSKAIDPDGSLERAFDVSDAGGKKTRAKALEPAAPAASAPPDPPPPSSLSIDGAVEPPAAVQDRAEKPADTTPS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 151
Sequence Mass (Da): 16026
Location Topology: Single-pass membrane protein
|
A0A2E4HQI3 | MSKYIDSLNLSSLRPEISRRTLVVSIALVVIFSAALLLRIMPVKYGYYLNEYDPFFDYYASKFLVDNFDTQGLRGFLDYFSWHDYKTWYPEGRPVARTSQVGLHFAGAIFYLIARNIFGLSASLYDFVVMFPPMVGALTIFPIYLIARRVTSPGGSLLAALIVAFSGSIIQRGNLGWFKSEPFALFLALWGVYFFLTMFDSKRKFNSLVGRSITSGLLLGLANTAWGGSLFFAIVVSAVFIIMPFLNINQGKAIFSGAIFISMYLLISAISPRPGVAIIDGPIGIALLGSLGFAILSYVIRSYSLLKEYSTIITNVIIGSVLGGIIILSFGFLSEVSGRYLTVVLPFQRSGVPLVESVAEHFVPTGAQYFSEYLILLPFACFGIITLFNKHSIDSIFLLAFAGAGIYISSSFSRLMIYSTISIAILAAIGFAALTRSMFKPMLTGFGKRKTGGSEIRVGLKVFYSVVVIALLCFPIITPSYSFNTIYSADIPTAIANSGSTQRAFQGDFLEALAWMQTNTEEDAVIAAWWDYGYWITVMGNRTSLADNATINGTRIEVLGRMFMSPEAESLEILDTLDADYVLIFIAGRKGNDQRIGEFFLLGGGGDESKKQWFIRIGGMQDEEFVEADGFTPNENLWTNSFLGKLMPFVNSVQVDQEGQIIENQPWAQGNTQLYTYQLKYPVDSNGPLRLAFASSSIHPDAPAGAFTGVLIYEIVKDRSEVEEPVLAAPSP | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 732
Sequence Mass (Da): 80650
Location Topology: Multi-pass membrane protein
|
D2R9Z2 | MSDNFDEFFDKHAKWTEHDGEPSSESSNSSKYKSSTVSSRKRAKARLEAKKRRRRAKVVLSILLVFVLAVVGYFGYSAVRAWKLSQNSESVADWPGPGFGTVEFTIDTGEGAISVANKLVKANVVKSQSAFTSAVSANNKILYPGVYSLKKHMAAIDVVDILSDQTKAGGFLEVRAGDHAADVLQKASTLSGISLDKFKAALADGAAGILPAEANGSVEGWLEPGVYNVKAMKSADAILSAMVKKRIEKLDSLGIPKGKDREKALIMASIAEAEVNNREYYGKVIRVILNRLAKDMSLGMDSTVGYGAGVKPIKLTQAMLDDANNPYNTRIHKGLTPTPIGIAGDNALLATIKPQDGPWLYFVTTNLKTGETKFADNKDDFLKFRDEYKRNNPEGN | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 396
Sequence Mass (Da): 42975
Location Topology: Single-pass membrane protein
|
A0A0G0QRS2 | MNLKTEKEIKTMKEGGEILSAILRKLSEAAKPGIATYELEELARSLVSSYKVKSSFLGFDGYPCALCVSINEEIVHGVPSDRIIMDGDLVKIDMGVLHNGFHTDSATTVLMPGGKDRDIKERLMNVTKEALRIGISKATVGSTLGDLGHAIQKYVEDSGFNVVRDLIGHGIGRELHEDPQVPNYGKPGMGPKLVAGMVIAIEPMVVTGSWKIADGDDGFAYKTKDLSLSAHFEHTVAITEEGPLTITS | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 248
Sequence Mass (Da): 26753
|
A0A812XVU9 | MTASTTLIRIMSVLGMLLSAYALYVEHRKAEDELYVAACDINSWVACSKVFTSKYGRMMSLLGLVPSGHALDLPNAAYGLLFYVCAFFHDDLAFLPRRLRAAIMLFAASAAAASSVWLGYVLYNILHDACIVCISTYVVNTVILIAAISSMFAAAFPPVMDKKTQ | EC: 1.17.4.4
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 165
Sequence Mass (Da): 18004
Location Topology: Multi-pass membrane protein
|
G6EQD0 | MVDTEISQIIEEAAGNAYVPYSHFRVGAALLTNDGQMYKGCNIENASFGLTNCAERTAIFKAVSEGHRDFKMIVVYGDTEQPISPCGACRQVMAEFFKQDF | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 101
Sequence Mass (Da): 11166
|
A0A4P6F5K8 | MAVLITGGARSGKSAFAEQYARRIGSRGIYMATSRIWDEEMEERVALHRSGRETSGFEWHTMEEPLELADAIARVGAEHAADDPRLEPGAELDKELELEPGLRGEPAAERNAESSPAPEAKPPVVLVDCLTLWLSNWLMKLEEEQLPESVLAEQYEKLAAAAAACPYPLLFVTNEVGDGVVPAYPLGRKFRDEAGRLNQLMARQCERVFLVTAGIPVELKAIAFQWENL | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 229
Sequence Mass (Da): 25316
|
A0A2V3I233 | METWRELNNSNRFDNKFLTVIADEIRELINKGYYNVSEKIERKNTSLKDVLLSKKENYPIITEIKFSSPSLGEINSNSNSQKEILTKMEVNGSSAISVLTQPLYFDGSLDNLKIIRQNTNLPILMKDIIIDEKQIDAGYNLGADVILLIETLFVDNQNKLEQLIASAKNLGLEILLEVNSKQEFDKAVTRDVDILGINNRDLNTLELDMKTTNRILGEEFKMDKPIISESGILTSEDIKIIGKSGVDGFLVGTSIMKSDNIEKKIKELTSVRK | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 273
Sequence Mass (Da): 30831
|
A0A2E8PRF7 | MEPGKLLENSELGLRILAGENGLNRKIRNEDVNRPGLALAGFYRNFAHDRLQVFGQGEFAYLLDCGGEVEGRIKDEFFSYEYPALVFTHGNQPPSCFIKKSNETDTPLLQTTLSTHDFILNFNRIITRALAPQTSIHGVLIEVFGLGVLLLGPSGIGKSETALELIERGHRLVADDMVHIRHMGKGELIGESDPMIEHHMELRGIGIVNIKDLFGVGAIRKKVQVDLVVFLEDWKEDKEYDRLGIDEQTMEILDVSIPSITLPLRPGRNIPILVETASMNHRSRRMGFHAARSLSERIHSRISQQITEDAERENPPKKERKKASPKPLMGPV | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
EC: 2.7.11.-
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Length: 332
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
Sequence Mass (Da): 37283
|
A0A6I7PG00 | MITVVQPALVSGEPYVPGLSRSEVARRFELAPDAVAKLGSAENPFGPSPKAVLAMAAALADSSLYPNWTAEALRRKIAERFGLEPNQVVAGSGETELIGLILRTYAAPGAAVLMQRPCFPIYHLYAENEGRRPVFADMGPDFAVDTDRYVAQLQAVRPSIAFVTHPHSPTGQAASEADLRRIAEAAPDTLVVLDEAYVHYTETEGLLHLVGEYPNLMALRTFSKAYGLAGLRVGFAVGAADLIRPLWNAKPTWNIGALQSAGAIAALDDEAHVQRTVQTIVAMRAYVTERLAGLRAFRMVPNSRANFFLLEVVSPALDSTGVFEALLARGVIVKDGSVSFRGLGDRYLRIDVGLEPDMDRLVSALADIERSQA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 373
Sequence Mass (Da): 40210
|
A0A6I7QPA7 | MDLRFPRKSPGPAPVPAPPRGRSAGAASALPAGSPGGFRPQRRTPRGKRGWWSMLKCAGERRFCSSSYTVCYIVSYHTRGGAYTVEDQDRFREVLPGFIVFEGLDGAGTTTQARALADHLGRSGSAEFTFEPTSFATGRVIRTLLKGPEFARWETLALLFAADRNEHLNRPGTGIRARLDAGFTVVSDRYLFSSLAYQGAFADPRFVEQLNASFPLPRHLFFIDTPLDEAHRRIAKRLHMDPEGGDSLEVRSVQSQVAPRYREVIDSFARGPEARAGLMSVHHIDGSRSAEDVFRAILEALRHTVNPSRRSADR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 314
Sequence Mass (Da): 34770
|
A0A5B8UA80 | MSRRAPVLLRAAVTALLLAVLTVVPSAASAARAPAPPAVRAPAAILVEPATGDVVFQRGAHQRRPIASTTKLMTALVTLEHASLDDVMTTVAYRAAPAESVAGFRAGEKVTVRDLLRALLVTSANDAAATLAQRVAGSRPAFVRMMNARARQLGLTDTHYDNPIGLDGPSNYSSVTDLVKLTLILRRNAFFRETTDLARVTLRSGAHPRTFPNRNMLVRTVPAVNGVKTGHTNRAGYILVGSASRDGITVVSAVLDEPSEAARDSDSLNLLRYGLDRYHLVTAVRSGQVLGHAGLAHRSEQVDLVAGTTVRRTARRGDKLVVRLSGAPTELDGPLAKGARVGTVLVVQRGRTVARIPLVTARPVDAATFLDRLRDWLDRPVTLLLLGAFALCSLYLVLLRRRAVRRRQARRRGAPVA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Length: 417
Sequence Mass (Da): 44744
|
A0A1Y4VJC3 | MDKIKKDINQIREDIKEVDYKIAELFEKRMKYTAELAEAKKEIGAPIYDKNREDEKLADITKNRSNPFIVKGLEEIFIQMMSISRKYQYHLVHQRDRYIENYFTEVPELVMFPDTRVVYAGVPGSFTCMASEKFFGRDIDHYGVAQFKEVALALNNGDADYGVLPIENSSAGDVAGVYNILLENDVCIVGEVFVKVDHCLLGCPGSKIEEIKTVYSHPQGLMQCAPYLEKLGAEQKSVENTAIAAEMVAKRNNPQEAAIASRRAAELYGLDILAESINFDASNETRFVILSKKRQYTKDASKISISFAVLHESGTLYNILSHFIYNDLNLSHIESVPLPDRQWEYRFYVDISGNLHDPEVRNALQGVRAEAANFRILGNY | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC: 4.2.1.51
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 43149
|
F2F8D1 | MFYILLSYLLGTILFAVVLGKVTGIDLQHANSGNLGARNAGRTLGKWAFTFVAVGDGLKGLLVVVVGRMLELPELTIALAVIAVVLGHLYPFWNRGKGGKGVATVIGAMVAFSPLLIFVFLAGFLLSLLVTKSTTLSMTGGFILYGLIMSVYIEAGFIVTIALVLVIWKQRHSIVERVKPNVLE | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 184
Sequence Mass (Da): 19734
Location Topology: Multi-pass membrane protein
|
B9Y9G1 | MEELMKEKKDLSEQIESFTNKIAKPLSKFAAIPGVAAAIEGISANMNLIIIGGVFMILYVLSSAYATGTENAILPFLTPYGSNVSQVNSFTLGMIGLLASISIASKYAEKVKVDHTTSVVLSFVVFMILSNWGVVDGTLSTANFGSKGLIVAMFSSVLSIKVYKWFIDRKITIKLPASVPPAIANSFIALIPSFVIITFCWILRNLMNIDIVSVIYGLLGPVFDASETVPFAGLEGLLYSLFWSVGIHGGNMISPITQAVTNTFLSENAAALASGVSLTALPHWYNGARVGVTFINYWPLLIFMAFSKCKEFKVMAPAMIIPACFNITEPLFFGLPLILNPFLMIPYIITQVMTHLIFAVSAASGFIATKVAISVPWALPFPLQQLIGFSGDMKIFLVDILVLALCTLIWYPFWKAFEKKELEKEALLEIQ | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (Da): 47077
Location Topology: Multi-pass membrane protein
|
A0A1F3BR00 | MHIKQGNITAVILAGGNNSRYNGTPKAMLEIAGKTLYQSTKEKLEKIFCEVVLITNSPEIFPDDDCKKYADIYKNIGPLGGIHSALKNCKSQEAIFVTAVDMPFLNVRIIKSIVTQYQAQNSDILIPKINSDIEPLNAIYKTSILDELESFIRNAKRYAIRDFFEKVDTKYIDFENSDENRKAFTNINTPNEYELIIKED | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 200
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 22736
|
A7TJT4 | MYNAMVRKGKIDVNTGEEIPEDAVESMVFVHNFLNEGCWQEILEWEKPYTDVTRVAPKLLQFMGKPGELSPRARFYSTLGNWFPSYFNNEPPFDRHDWVVLRADPSSNDPETPGHRKVRYVIDFYGAPDDEEGLPSFNVDVRPALDNYSNAKDRIIRYTQQTMDKYFGDDNSKN | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 174
Sequence Mass (Da): 20238
|
A0A3B5MNP8 | MRFTDIDFFHHFKILIFIHCLRPDLQYQKEKKCLFSPGTDTASQQEFTSCLKETLRGLAKNADNLQSSGLAGDDLVKALEGLGLEEGGDGGGEDGNILPIMQSIMQNLLSKDVLYPSLKEITSKYPEWLETNKSTLSAEDHQRYQQQAKIMGDICKLFENEEEEAGDKERTFESIMDLMQKVMQFLFLFPLQPPGFTFDMDSLNLPGVGGAGAAEQCSVM | Function: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53.
Subcellular Location: Peroxisome membrane
Sequence Length: 220
Sequence Mass (Da): 24647
Location Topology: Lipid-anchor
|
A0A1R1YRD0 | MFIALFFRVYFLASTSITIICELIPVLRVNFVHYGKVKNNLNLSNEKKVENENIDSKKNTGKSTSIDNKLHSLKRNPPASKKIKEIIADKDLNSNTILEKLSRFSVPKNSFAYFYIFGSMVACHFLRELLGWDSRGEMFDSVSSRDPLFFSLLKFIECNYSPNREMYKLPSPDPLIKLCEPFVEVVPKRLIFVMGLFAINVLIRLYETASMQPLSTSRIHVAHFIAGIGFYLFAPFALIIDVIYLQSKLKKAIVFIYIIYLFCLLI | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
EC: 1.3.1.94
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 266
Sequence Mass (Da): 30622
|
A0A1Q7P2R1 | MALAGRNVVVTSHRTPVPGGIALDVTDAAAVARVLRDSRPDVVVVTVAEHTERCERDPDATRLVNVDGLQRVADGAPDALLVVFSSEYVFDGRNGPYSEEDAVIPINEYGRQKVAVESVSRQRSDHLICRSSGIYGWSAARENFVCKLVDSIRARRRFKVPMDQVITPTPAPDLARAVIELVDRSARGTFHVAGPEILPRPEFARRVAAAFGLDASLIDAVPTSELGLLAQRPLGAGLRTDKLRGFLGHGLSPSAPALAAMREAEPIS | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 268
Sequence Mass (Da): 28817
|
A0A3Q8M7G6 | MFFHPVNILFMGTLIFSLCLIFSMNTWVMVWLGLELNLLSFIPIMLKKNNKYNVEAGLKYFLIQSLGSMYLLMSFIFGFLMFSKGVSFFILVALFMKMGAAPTHSWFPSVIEGLTWPHAFVLMTLQKLGPLSLIPFVLMNSSSFYIVYFYLVSSALVGAVMGLNQSSLRKILAFSSINHTGWMLACCCLTKLYWIIYILVYSLILVPIILVLYKLQLFFINHVFKIPNFFFNIMFSVSFMSLGGLPPFTGFMLKLLVVKELINFMTNYFILFILLFSSFFSLFYYFRLMLYYFMLSFTNSINFFFFNKFSFFLVMLNVSGIFILVFFYFI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 330
Sequence Mass (Da): 38525
Location Topology: Multi-pass membrane protein
|
A0A6I7PBX1 | MNQGRIWCVVNPTVGLPLFLGAVALIAFVVHFAVLNNVDWFAAYWGG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Subcellular Location: Cell inner membrane
Sequence Length: 47
Sequence Mass (Da): 5148
Location Topology: Single-pass type II membrane protein
|
A3VA96 | MADTTDTNTQDTAEKKVNPWLRAALEYGPIIAFFVGYMLVRDMSFTVGGREYQGFLAVTAGFIPLQAICTFLLWRVTGKISAIQIATVVLVAVMGGISIWLNDERFIKMKPTILYVFFFLILMFGILRGQSYIKMIMDHTVPMSDEGWMIITKRLAMFFAVLAVLNEVVWRTMSTDMWVNFKTFGLPLAIFVFFMTQSGVFQKYGTDEDKADA | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 213
Sequence Mass (Da): 24190
Location Topology: Multi-pass membrane protein
|
A0A194SA43 | FSHHRVSCPPADWIRAAHENGTKILGTLIFEHDAGKGDIIELVTPSSSFSSATSSSASRFDRLSTRYADCLVDLTLERGFDGWLVNVEVELGGEGASDEQKRAHAAALVAWLRYLSGEMRRRVPGGEIMWYDAVTTDGKLEWQNAVTERNLPFFDASDSIFLNYWWRPEQLASTVGLLDKLGSSRHSDVHFGLDVFGRGTLAGGGFESWRAVHTTEQAVGARSTSFSTALFAPGWTVEA | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 26270
|
A0A7S4DEZ6 | SDHSREMNETWIYHEKQFSLLCGQHCLNNLLQGPYFDAPGLAQIGQELDAEERRVMLEAGADTPEALRFLAEDSGNVDETGNFSVQVLNTALEKSHGLTLLNTGRRELRDSIRDYTKEEGFVCNRSAHWFAIRRVGRYWWNLNSTLERPEHVG | Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Nucleus
Sequence Length: 153
Sequence Mass (Da): 17564
|
A0A6I7P8J5 | MDRITVVGSGAWGTALAIQAARAGRSVQVLARDGVTAEALRRTRQSPQLPGIDLARSIDVLAVAEAADLGDAVLSVVPSHATVDVARALAPRLRQGVPWTICAKGLHAAGPSLLSEAVAKVLPAAPIAILSGPSFADEVAKDLPTAVALAMAPVDRALGETLGYALHSQHFRPYLNDDPVGVQIGGAAKNVVAIACGMARGLGFGANAEAALLTRGLAEITRLSLVMGAKPTTLLGLAGVGDLALTCAGPHSRNFRFGEAVGRGIDADRAEAEGGLAEGRKAAPLLLQLARLRGVDMPIAEALDAVLAGRLDLGEAIERLLDRPLVSEFENGGR | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 334
Sequence Mass (Da): 34223
|
A0A7S4D564 | TLDLGLGLLGKPWSWRTFFSGKQRWNTVGAIGSLRSGMAYLNLIFGFLLVAGFHLECLLSLDTEGFSHSSWQVIALEGNSSKKDLEANVLVALELENAEELEEKLREISDPLSQKYAQYLSSEEIAEISCPDKTVVNEILQWLATANGQCEVSQSGDLILLTATVADLEKLFSTRLDYHGKINPKVAKEYLDHKHYLKATTNFSVPEAFRDSISFISINTPIVPSTATKKSNAATTFSAHGTDHGLLPPAGRAAALGGQEAAALYFQLGCGRNASAAPPSALCAGPPRGYTVEVAVEHYPASLYRLPTAGLACHDPRPDAAPAAPLPPGAAPSLPACDPYDPAADAPPCLCAAIVGPLPKYRSLTFSIYTDSETTDPILVSSSIAPIILSDATTPAAIRQVYGLPARPVLLATAAAAEFDQQFYANGDLRAFMARMGEAPSAILGAEVAGDGGNNPAQPGGETELDVEYLAALLPGLELGYYTTANCAPFCGAEEFLQWLFELSAPGRATEMVHSISYGGYESDGDGHPGQHEFLKRVDQEFLKLGLRGATLVFASGDDGVCSGLQLCPDRARPGWPATSPYVLAVGSTSLSDRALPACGAPWRAGAPPFECGFRGEVAAQSNKGNIITPGGGFSDVYPRPWWQHHHVPQYLERADALGRLPPAGFFSAGGRGYPDVAALGSLFYVTVGAQPALESGTSASAPVWAAVLTQLNEGRLRAGRPPLGFVNPLLYHVNVVAPEAFHDITVGNNSCAHGHMGTVQEIPCNPEYFLAEAGWDPLSGLGSPNFPLLQEAVLAVFGDKEAESLPSPPSADVQQQEQKDYITGTEFSKEEEWADHGSDGSSTDTDNHHHPPHGGGGIAPFYELSFWLPMGVALVALGVSLRNSNAYLRRGLVAPAGGYGAV | Cofactor: Binds 1 Ca(2+) ion per subunit.
EC: 3.4.21.62
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Sequence Length: 903
Sequence Mass (Da): 95665
|
A0A1Y3AMD6 | MSKYDDMANEKLYRWTVNILRTVNVDFLELHSQLFNALAYLQHKEVLFKHCMDEYTIVRRSAVTHSFIEALTRGRSSNNTHYQAMELYSNDIVRYIRDMLSYLHQTFVFERDMLRTLLKSCNQDELSRKNVIKNVISALTEGVIRILKIRVENCLVANERRDEIMTQSIQQQIRRTKNFFLIKNIINFYLHTFQEMLNEDCSFIHFIKEILLSSDKVCYNSLKFYCSQLSLKIDATINVTKSINFRDQLQHYIQMIDELLDGIPCSMSFSQEEQHLETERILSTIFEPCIQSIIIIASKFPSIDMTIYNLNCYQCLQQTIEKYNFTDSFTKNLRSKIDATSDVIADEQFRYIINSLSINSLYNAIDQNDFIKSNTPLSSLSGCDPIAIVTFLNLLDKFLQNPRQFAMKQLNDIYYPTIREKIWQFSLNAITMTYEKIHGHLIDPKNKYYDIVDRIKHCPEDVRKQLAILSE | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 471
Sequence Mass (Da): 55546
Location Topology: Peripheral membrane protein
|
A0A6P4ZYW6 | MVAYQYSWFWNERFWLPPNVTWADLRNTDEVQYPQTTQLYVSVGYAVVLLIIRLIFERFIAGPIGQSLGIPGERKYAEPNAILEKVFTSITKNPDEKRLQGLAKQLDWSERQVQRWFRRRRNQDRPTLLQKFKEGSWRFTFYTLSFSYAATILKDKPWLKDIKHCWYDFPDHPLTDDITYLYIVELGFYWSLIFSLFRDVKRKDFWQMVVHHVATIMLVSFSWVANFVRIGSLILVTHDMADIFLEAAKLLNYAKCQALCDACFVVFAIVFFVSRLFIYPYWLVYSAATDSIADKGVFPAYYVFNGLLLLLQCLHIFWGITIAKMAYKFVISGTAEKDDRSDVEENSDVDENGKINGLYQNGPTSNSTNHIH | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 372
Sequence Mass (Da): 43583
Location Topology: Multi-pass membrane protein
|
A0A3B5LDU1 | MATEKCFAKGSPAPGPVPKGQLHLYSMRFCPFAQRTRLALNSKGIKYDTININLKEKPEWFLEKNPLGLVPALETSAGEVIYESSITCEYLDEAPTKNAAGAFFQGNTLLLQDPFSKKDWRGCLYTGS | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid
Sequence Length: 128
Sequence Mass (Da): 14179
|
A0A067N0M4 | MASSSSSFWQQAWEDSQPRLHAIRSSLDHAPPVQSRVLRVGQLDAEQLDQELVTLLTEPLSKALGLIQYHYRTQFEPEMTLIVRLVLYKLSIWDQGASYGAKLQDLRYRSSRVRRIGTAMAPSGIPRVTLYMHAFLTVLIPYIHTKIRNLALTRAWPDAPSSDRRRKAWEFLTRLESAHSVLGLFGFISFLYNGRYRTIADRLLGLRLVPARILTSRSVSYEFMNRQMVWHAFTEFLLFLLPLVNARVLRRRLVRLFTLSQLSSYIPSSIRSIFGSPSPQDPDTKGKAVEKHGKYWSLPEESCAICAENATLQFNSAARSGALVSLAHNDPDMPAHPIYTPYITSCGHTYCYMCLSERMLRAQDEGEPGWECLRCAKIVASCTRYEDPLENGSFTTTDDEDDDSDLGTMGTSLTSDDFPSSTSSRSIS | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 428
Sequence Mass (Da): 48438
Location Topology: Multi-pass membrane protein
|
A0A2S6UPD1 | MKILIVESRFYSEISDQLLLGVKRELDSKKILFEVVSVPGALEIAQAMNIIISKDIQLGKEVGFDGFIALGCVIRGETSHYD | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Length: 82
Sequence Mass (Da): 9100
|
A0A194S845 | MGSWRRGAESSGDIDLLVTRDPSRDGKTHEGLVKKLWKKMKEAGIAQYELSLPKDDTSLDAKINGLCKLPGKNDAKMRRIDVLGVPWEEMPAALIYFSSGSIFNRSLRLKARRMGYRLNQRGLYKDVMRDRQGVKLTEGVLVKGVKSERDIFRILQVRYRPPEERSV | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 167
Sequence Mass (Da): 19107
|
A0A137PBT8 | MELNQSHHLFIQKLLNGRVVDGLDIKSLMEGIIECYPSEFDLTEEDTQYSQIELIFPQFLNKINSHLFSLDLEIRKGLNQTNGEIFYHLINLNPDEFSQLATNYSALELGYLKNLIESIITSSHLEFSIKMSSALRDVPLHTTSALSQQDNQVPQSQSAGSNLTKLERQQLIDRFIQDDWLYTLEGTGLLTVSDRCLNELRDKLINEFEEDIWQCKLCMNLVTQGYLCKSPNCNTYYHHPCLDKLLKDIEDNRTSLSDRGFQVKCLSCHNELKTKLVGHRDLCQFNQIYLDFNTSSQTLN | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 300
Sequence Mass (Da): 34639
|
A0A6I7PDM9 | MPQLDGSTFPSQVLWLVVAFGVLTWLMATRGVPRVADILETRQDRIAADLDRAQALRTEAEKAMQEQQAMIADAQARARTALLVAQEKSAAEAARRERELEESLQHQLKEAEARIQAARTQALSELEAVATEVSRAASGHLLGLDISAEEAAQAVASARQGAQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 17641
Location Topology: Single-pass membrane protein
|
A0A2S1K9X6 | AGMVGTSLSMXIRAELGHPGALXGDDQIYXVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVETGAGTGWTVYPPLSSSIAHGGASVDLAIFSLHLAGVSSILGAVNFITTVINMRSTGITFDRMPLFVWAVVITAILLLLSLPVLAGAITMLLTDRNLNT | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 192
Sequence Mass (Da): 20388
Location Topology: Multi-pass membrane protein
|
B9YCT0 | MSDYIASSPEELQAMLDSLGLKDLDALTGHLPEAVLLKEDGWDLPEGMSEFEALAKLKKMASHNRIYEDLYRGAGAYRHYIPSLVNALSSRGEFLTAYTPYQAEMSQGLLQSIFEYQTMICELTGMDVSNASVYDGATAAAEALLMCRDPKHRRVLVPASVHPQILQVIRTYGEAYGMEITVLECPHGVLEESVLREALSEDTACLLLQQPNYFGLIEDAETLFAAAAEKKVKGILHINPIAAALLPSAKEAGAVIAVGEGQPLGMPLNFGGPYLGFMASVSAMMRKLPGRIVGQSTDHEGRRAYVLTLQAREQHIRREKASSSICSNQALCALRAAIYCSAMGTEGIEQVASHCVSNAHYLAQELCEKTKLKLKYTGEFFHEFVTVSEVPSGVLLKHLEDHGILGGLPLSDHEILWCATEVNNKENMDHLVELIGEVAA | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 440
Sequence Mass (Da): 48039
|
A0A151QXL1 | MTSAESSAAAWDRLNKQYANRSRTRIMSLKERLASISKGTSGVADYLRSIRVIADELALIGHPVDDLDLVITALNGLGPSFREFTASIRARDSPLLFDELFDKLIDFEIFLQREERQQQSLPATAHYTQRYNASSSRGKRSQNYRNSSSVRNSTTLPSAASSNLSNNSSQRGSSSSRSVPTCQYCDRRGHTAKTCYQLHGYPSNHPRHQANLAQQEPQSDPSWLLDSGASHHVTKDIANLSLADTYQGHDQLFVANGKDADELYNLCDPDKDDELCLYGYPNGKWELKLPAPNVPAELPEPVLGINFARTMERQDWFSNVSVHCTSWLLYVAYYSAYSLDQIQRQRLFSLINNLPTISEVVANWKPTTEQPSEGSASKHQENTMNEDMIIIQCGSCAGYYNPQEFWIGCDICEWWYHGKCVMMNPAKAETLKQYKCPSCNLRRGRS | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 446
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 50295
|
A0A1Y3AZ61 | MNSSSNSQHRISFIPGEPVHDPERTLIFLITPTYTRPTQAADMTRLSQTLQLVPDIFWIVVEDAHNSSRSVEDLLRRTNVPYAHLLGPRPPTHLDKRSGRGVSNRLRAFEWLRENYSNTTQKGVIYFADDDNAYDVRIFEEMRSTRIVSMFPVGLISTLGLSTPIVSRKSGKIIGFHDPFIGRRKFAVDMAGFAVNLQFFLSQKKATMPYKVGYEEDYFLKSLGVQIWQLEPKAENCTQVLVWHTKTKPADQPKLSLMKKVTNYTETNLPDLYNNQLEQS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 280
Sequence Mass (Da): 32100
Location Topology: Single-pass type II membrane protein
|
A0A7S0F1G8 | VKIAMEPSSTRHRARHSIPSEGDPESSAQGGGAVAALDPDESPSYDSPEGGSLREGVKHFFPWAGQAEVIRAMQKDEYYVALLKKALADTTQAVLGARALTRHQNAVENLSNLVYFGLTTGSANPTLGEEYCEVREVSAHSETSASKGRRAVFIVWKLIVPYVSKIAQMRIIRQT | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 19041
Location Topology: Multi-pass membrane protein
|
A0A6P4XWW4 | MADTRAGGERVMRKVDLEQDVLTNEERTMMDRMNALQAARAMERSRARWFRRNIILGLALGGVVLGTYGFTMYRVRQETFDDVVPISKEGQSSGGS | Function: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly.
Subcellular Location: Membrane
Sequence Length: 96
Sequence Mass (Da): 10829
Location Topology: Single-pass membrane protein
|
A0A8E4HJB2 | IWAGMVGTSLSLLIRTELGTPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNNLSFDQMPLFVWAVGITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILY | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 208
Sequence Mass (Da): 22233
Location Topology: Multi-pass membrane protein
|
A0A2T2T104 | MALRVAFQGEPGAFSEEAVQRVFDGADVHPCATFKDAFEAVEDRTADRAVVPIENAVYGSVRVNYDHLRTHAVTIVGELQLRIHHCLMAPDGASIDDVEVVRSHQQALGQC | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 111
Sequence Mass (Da): 12144
|
A0A2N3G601 | MANFVFEKIAILGTGLMGGSLAMALKACEVVGEVVAYDISNDARNAARELGVADRVEDRSEDAVRGSGAIFLATPIGAMAGALKAAAPALMKGAVISDLASVKIGVISAIEAVLPAGAHYVGGHPMTGSERSGVSNARADLFRDRCYVLTPTDTTDLDSYQKLHTVLTEIGARVISMDPESHDRAMATISHVPHLLSLLMMNMAAREKEQMNNIYTLAAGGFRDMTRVAASNPRMWLDIVSVNRDFIIEELKRFASSVDVLVDILQKNDRDAVLALFVDACAAREELSMKPGVEKAELFTISLPVPDELGVISKIATAVGALGINIEDIGIAHPLEGAMGILTLKVLGAERAREVTLKLESMGYNVSSEQ | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 370
Sequence Mass (Da): 39365
|
B9Y9R8 | MLKEISLTLFHNQELISLLLIEGVILIVSFMIYKSLKEKNEIIKPQSKETSAGKAVWNAFDILICGTITLMFLVVAFWQLGDTELPQTRWQPTQSNESFILQIADGSSAFDRIYLLSGEGDNNALESGYQIGLRNVLIEGSNDLVDWDNISQIDNSSYLQWKIIEGQWNYRYLRITAGEKNNVINEIGLKRAGFNDFLPLTVYSSDTEGTYDPQLVIDEQSKLKIDPLYLNETYFDEIYHVRNAQEIAEGQVMYAFVHPLLGTQVIAFFIKLLGNNPFAWRFGGVLFSAAMIPLLYDLCRRLFNKTFYAALGAVFLACDFMHLTTARIATLEPFSVFFILLMTYFMIRYCLMNFYVDDFKKSLGLLAAAGISMGIGVSVKWTGVYAGMGLAVLFFSSLISRYVEYRLAKRAKEPTALEKHKIEVFPKYCWITLLWCCLWFVLIPLIIYALSYLPCIINRGEGWSLSGVFKQTMGMYNYHANLDATHPFQSVWWQWILDARPIWYYHHISENLVYTISAFGNPLIWWSGFIAILFCVYDFIRNKTKTAGMILVCYFAQLIPWMLVTRCVFIYHYYPSVPFLIVALVYGLKCLIDKDARYEKRIKIFTLACILLFVLFLPATAGFGTTQAYIDGFMRWFPSWYFG | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Cell membrane
Sequence Length: 643
Sequence Mass (Da): 74078
Location Topology: Multi-pass membrane protein
|
A0A6P4Z6J6 | MEDAQMRLKTYNKLIVVRDPLERLASAWLDKFFISPGRFSFIRRLRQAVGNSKFGNTTTKRALPTNRSRRGSMHGARRAPPISIRDFVWSIINNKYRNEHWEPFFSQCAPCQVQYDFIAHTDTLVEDLRLFFHMSGIVGKDGILPRQHPSRAKAGFGRTFRVVPPEDIRHLGEIYKPDFDMFGYSIEEDLEAIENALKQNV | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 201
Sequence Mass (Da): 23360
Location Topology: Single-pass type II membrane protein
|
D5XFG3 | MAEEDLKEEQEPQGKNSSAGTIKLIIAGIVIIILAAGISFAVARFAAVSAPQHGSTYNANAKIKTDNIGTTFDAGEYLTNLAGGSRYIKVKIVFSFANKELETEITNKLPAIQNTINKVLREQSADALNEPKSMDKLADRLKKSINELLVTGNIDEIYFTYFVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 165
Sequence Mass (Da): 17998
Location Topology: Single-pass membrane protein
|
A0A137NVX4 | MVLRYIRAIFRRLNGAYPMQHSQLYITLILLILFAIALSSILLIQTVSMGQVTTKTTIKNSIKVDVEVPDLSQIVKDQIQRMSGPQFNLVPKPTARLAFLALVHDEATVEGLYEFLDVAYLPHHYYFIHLDLKAPDSLMKNLMQSFRYHPNVVVATNRTKGEWGGLSLVNSELHLLNLASALNQQTEEDKRWQHAILICGNTYPSHSMKTIEERMSKFDRQANIVFSRKGLWRSCDYDPLDRYNTPIMTCGKTSGRCMDEECTKMTGTPGNAVVYKGPQWFILSKDFTSWMFQKDTYTDKITAWLDFHKKTFAPDEFFFPTLLMDSPFAHTWNLTGWPQPNPEQYTEEEVQPIFHRTEWFNCTTYKNSHIGKGPCSLGVDDWDKFTNEDEPALFIRKLIPGDPLKRKLYEDVFMKEDPSLLPWKDHKLPKK | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (Da): 49977
Location Topology: Single-pass type II membrane protein
|
A0A194S2P4 | MASPWPLAIPTDSHFSLNNVPFGVVSRRQDGAPRVCATRIGDHVVDLSLLEAEGLLDDALGGGDSSSQRRVFDQPTLNAFAALPVETRNAVRLAVQTLLSPASSTLRDNAQLRERAILPLDAVTPHSRSRSPTLSTTRSSPPTPSAPAEPFSGQVRAFSPGREVSIGASKALDWEFEIGAFVANSTPSGSTLSPSSAQSHIFGYVLLNDWSARDIQSLEMVPLGPFNGKSFATTVSPWVVLPAALEPFEVDKEVAPELEGNEAPEYLREKAGVKSAYDLECTTRLRTSSDPSTAAHLISTANFRAAHWSFAQLVAYQTFSGARLQTGDLLGSGTVSNHGERRQGCLLELAKGGKEPLELELGGGGGGGAGGERRAWLEDGDEVVFCARAGPQGSGVGFGELRGKVLPVSALRAA | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.
EC: 3.7.1.2
Catalytic Activity: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
Sequence Length: 414
Sequence Mass (Da): 43696
|
A0A6P4Y0U7 | MVRLLPLLCLVTFALCGHVVAMPKAVTQLGVMISKVTGRPPWKYWNYGCWCGKGGQGPAVDATDSCCQTHDFCYEALEQPPCRWTVKQYLTAYKYSIDGKTVTCGDQDGTCKRTLCECDKTVVNCFARSQYVEAHDHMDQTICKKGNSTEVMHDGLSGTFP | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 161
Sequence Mass (Da): 17861
|
A0A067MSU4 | MVLAEANGAPLLFSLVVQAKKALQHAESLCSLARGIEHTSARSAVDVLSLEAKVKWVTEGVLDQLKLATTMSKHITQERSKLMDDVKEWDSQRTIRNNKLDSILETLGAHLVPPSLHQLSSGSSLFGSQIMDRSDSRAEEELPKKEDKSKWKSLRDFVDERGIEEAVEKMEEDRSVLEDLMATTSTHPLTLNKHITLVRSTLPPPLVLNPSVEAELSEQDSVSSDMALHLESIANHYGQLTNALRDEEAGEVLHEDDMQVFIRDSGELAAVIPELEDAVALIEIINDRLVTARQTAQDNLDKLYDVMSLLEELGDMAVMMVEDQRQVESDAISILTTLREHLVRLEELEGTYTGYQRAYNKLILEMDRRRAYRDTVDALVQSMAMQLQNLRDDEIAQRERFLAEEEHYLPPDLCPFVGDAPVVWTLHSDGEDELPDLTASIVLDAQRDVERTQITNGLR | Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize preautophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy.
Subcellular Location: Cytoplasm
Sequence Length: 459
Sequence Mass (Da): 51639
Location Topology: Peripheral membrane protein
|
M0EPE3 | MNPEYIDALEADGLVFSGRADNRMEILERPDHPFFFGTQAHPEFRSRPDRASPPFVALVEAALGSTDTTERNADVRL | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 77
Sequence Mass (Da): 8633
|
A0A067N138 | MPSAPSPRRSRRIAGSTAPYATRSASSKAVPPKRTTYRPSMGTSNNPIVLDLSPPKAKPAASSSSRAPKPRISTATAARNKTRTPARADAKAGSKAIAPSTQVQLVLERPEHTEDTPSPDLKTEDATDPISLPSSKPGQIARATRQFSREVDDLQARQIKISEEEARLKGLDETIRNRKKALKKREEQIERLEQGAYKKSAQQMWDAMEQDITCGICMELMVAPQTFHQTRCGHVFCGPCILKIIFGSTCNGCNDWHGEPQVSCPMCNASTTLNPNAARRGNPLVPNRALASLISAFLEQMEGKGRDSQQEELGKWKTRDLVAKELMTGFNEAWDMQNKVAMGLVKKMLAQV | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 352
Sequence Mass (Da): 38636
|
A0A7S0E5C5 | MKRMADEEETTISDQPGSTHTNNPDDNRSGSWKDILLIAVFSSLVALITFENTIGGEFVFDDNGAIVENQDVTSRERFGEKIVRLFEHDFWGRPMRVSAHKSFRPLTVLTFHVNWLQAGGRLDGRVFHGTNIVLHAVNTFLVVIISALWVFPRSGGVFSLLVVGMLFATHPVHCEAVAGLVGRADLLCTLFFLLSLLFYFPVAVSADVGLGCRCVCLVLTLLMAALSLLCKETGITALAVLFALDAIKNQIRLLPYPVMRVNRPDKRQGNATVVAKWFSLRSSILALFGITLLLVRLRIMHGTPTFTAENNPAAFVEEKVYRWLSYWHYYVVNVRLLLLPNLLCCDWSMGCIKTIRALWDFRNIPSFVLMIILVASLAFSAHSCMSFFTTAPQRIITSSIVLLIVPFLPASNLFFTVGFAVAERVLYLPSIGYCCFPALVLSSDLPASSRRQIGKFSLGLISSVFAYMARARNLDWRSSERIFGSGIRVCPDNAKLHYNLAHVSCKGVAESKTDQDVEYQRCKGLYEKAVSLAPNFGEALGALAAFYEETDVHKSAELLARAVKINPYSKRAHKNLGDLLARKDLSISRAIMHYDNAIRIDPEYADAYNNLGNTLLASGDMNKVEQYYRTALRLDPSHPNANKNMKTFFSQKKSPDRAQTEQRKEKKRHIDDLPTDSRDWNRRGWQLPSKPRKDGSCSDNDRSLKHKSKSKSKDRGKSKDKGRSKDKGKGEIERQGEHNSEIEGTSKRQNNDETEEKAGKGKTSLESGGKQG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum
Sequence Length: 772
Sequence Mass (Da): 86365
Location Topology: Multi-pass membrane protein
|
A0A6P5AVV1 | MASNAISDIADEFLVCQVCLEDFRQPKMLPCLHTFCQPCLEKLLAAEPVGKLDCPTCRQDVPLPQNGVQGLKFNFLVGKLRDILQQQPAGKTPEAREDGVPCTVCEVGNSAQFYCVECTEYLCQTCNNTHRRFKATKSHKVVTVQDLQIGQVTADGDQVRAPLSPTETTLMRPDVAIGNGGVSPKHVKTVGRRGSGDGQFDLPTSLAVTAEGDIVVTDRDNSRLQFLDKDGSFKKKVDLRFKPRCTCVAALTNGELLVTGDGHKIHVLDKQGRKSRVIQVTEAAETGQTTAGVAVDCSGRIIVTIGHQVFVLSPSGDVMLKFGDKGQGQQQLGSLLHVTVNSSNQIIVSDFYNNNMKIFDSTGRHLFTCGSHGSGPGQLYRPYCAITDSEDIILADCGNHRVSLFSRDGAFIRHVLTEEELKCPTGLTLTHDGHLVVSQALSFLTALRFFHVRMVFPDGPEVDDFRKKVVKRMAAPPWNFTDSLQRGLKGSAYSPFLHDAVMLYAIVMNQTLQTGEDPRDGEAFMRHARKKAFEGMSGTVILDGRADREPEFFIWDMDPSGTFDVVAQYDARPTGTEVSDDLLQELVFVKHIVWADGTTNAPTGFRECGYMNEQCASQQDIREEEDKKKMTQLVYVQFSN | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 640
Sequence Mass (Da): 70599
|
A0A157SLJ5 | MLGQRILTAIVLLAILAGALASDQPMWFLSLLALATACAAWEWLRLTLPQELPRATAPATGILLFVVMLGTAGLWVQGGDLALPLQRFVSAVLAPASALVWLVFAAGAVVKGRADAPPGNMGWSLFAPLALLTGWAVLALMYLAYGGMFVVSLLALVWVADIAAYFAGRALGRHKLAPRVSPGKTIEGAVAGVAGAVVWILLSALWQGTFGALLVERWTVWGAIPLAALLGMIAIMGDLFESLLKRRAGRKDSSSLLPGHGGVYDRIDAIIPVMPVALLLSGVMS | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 285
Sequence Mass (Da): 29854
Location Topology: Multi-pass membrane protein
|
A0A2N1TMX7 | MHILSQYINIIISFIDWRTFFDVPIMALMVLILYRTLKSSGSWRIGMGIGVILFIYSMARLFSFSGLSWLFNNVSNIALIALIIIFQPEIRKIFERTASTLKIRKTLSEGNHLSLLICESVFQMAAGKLGAIIILPGRDSINSKVSGGIHMNGRPSVPLILSIFDNHSPGHDGAMVIENGEITTFGLRLPLSTSTRYNNEFGTRHHASLGLSEATDALIITVSEERGVISLFHEGQVELVENEKELQDRIEEHWKTAGGFTPLQQTQGKKMSLVLEGALSLLLAFILWLSIMATVSQTKELVTTIPIEYRLADKMIISGDKPIIARIKISGPASEINLVRPEELKATVDLKQSKPGKVTISVARNIINLHHNINLIDAQPSNFDVDLYSFVQQDVIIKPQLVGALPAGLDILSVEVTPEKLQVMLATEKNSNEEIYLTTTPIFLQNISQNTTIRCKVIAPPEIISLEAKPLPDVSVTIIIKKRGVK | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 486
Sequence Mass (Da): 53833
|
A0A1C9P569 | IFFMVMPIMIGGXGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLLLLLSSSLIDNGAGTGWTVYPPLSSTIAHNGASVDLAIFSLHLAGISSILGAVNFISTIINMRAPGISFDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 153
Sequence Mass (Da): 16382
Location Topology: Multi-pass membrane protein
|
A0A0F7ZJ34 | MMISDLRRIVFFGLIGLVALSASLPILERRQLPGGQIVCGTITFTDVDVNNAIAETQRINAIKPTLSKTQQKKFMYPHEYKNFEGLYSAAPPGTKYLEFPLQSGSVYSRGTNPGPHRVIMIDDDKKATEDPDSGRNHAPDNDSSGTNTPGTENRPAENPNEEPSAWGIKNPINELTGKSAQAAAFLVGCLASAENATAAENENTHSFKLLDIYDTVIQFARNNVAKISEDVAQLLDPIIYSPLHEAVDHQRQAFQKFENATDFKESLGAIMDSIKHTNIDGVVIGSTFIPEESLASVVKNVAEGVALSEQNVRGGSLKLAQFRPLVDAVIANSPDNNIWAAVFNLIADVNPSTPPPSSIAPTFKGTPIKSSSSRLADSETRDIVERELFGEIKNCTFRNVGGFWDKFFDPKSWRKEQNAMLKGILTAHDGKRWTDFPNIPDEKPVWDWLRSLEEQFLGDAPYKFHTTRTANQFKERKGQMDLFLQKPATETGSTFWYKHVLIVGEQKKSYDASRFKADFLQLTRYVRSIFADQPTRRFVHAFSLCASKMELWVFDRSGAYSSGTFDIHDEQDKFARALVGYTTMDNDVMGLDMFVERQDGRRYVTLDASGNETRVRLDKAMVRQKAIVCRGTTCYETQNGHVAKFSWASDKRKLEVEQLKLAEERCVKGVARVVAHRRITTIAAMREGLEFPKAHRFRDEAVHFEDPPSAIASANTSGHKRKSSSDNTSDNASGPKRRRSNSQKSKLVQEFNDQLSIGKAKPSLYTLGEDPWENRIYSCLVVSPAGRVISDFKTIKELLESMRDAIKAHQSLYMTGNILHRDISSNNIIITDPETADGFKGMLIDLDLAKVRDSGPSGARHQTGTMQFMAVEVLRKADHTYRHDLESFFYVLLWMCARYSWSNGFGGEEKLPKESDLRNWEIGSFRDIAKAKEGDMTVNGLERIMSEFPEALDVVKPLCLRIRKLLFPLDKDERMSFGTPAGDPGQLYKPIIAAYDEIINII | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 1002
Sequence Mass (Da): 112315
|
A0A1Y2DBI1 | MANGSATVRIDTQRVLGQIDERIYSGFTEHMGRCIYGGILDPGNKNSDPVTGYRLDVLEALKELKPPLVRYPGGNFVSSYRWQDGIGPKEDRPKRLELAWRGEESNQFGTDEFMQWCKQLGAEPFICLNMGTGTLESALDWLEYMNGSSNTHFAALRRKNGHEEPYKVKYIALGNEMWGDWQVGQMRAEDYAKAARQWGKALKLVDPTIKLISCGKEGYDDWDRIVLAEVVDIVDFHSLHLYTKGATHEINVMGPAAAEKAIQMTMEVVDLARIAKKTTNRPTICFDEWNVWDPVIADGEKGAEQVYTMSDAVAVASWLNVFVRTCKSTSIACLAQSVNVISPLMTSPEGILKQTTFYPLQLFANYMRGKALDLHVDSPRYEGPTDLPWVTSICAEQLTWLDASASLDVDASVLNLVLVNRHGSLDFDVQLRLASTEQVSGEVELFEVHHEDVGAVNSWEKQPVGIVKSTERLAADSKEISSPLLRSPHTRPMFRRFSTSNQPSSSSSPAPNVSRAATVSSRPPGSVGTNNPYRQQPPELSGLSLDDAPPPPDYNTALRHSISGPPQGHQQQQQQQPLPPPVHNAARPPPQQQQYQPPQQQARPSSQTNAPPPPQQRPNSVSSSAPTAGGGASVRRRGSVEDPLAPLGKYDVVLLVDDSPSMSDGNLWQQTRDALMGVAEKCVKYDKDGIEIRFMNNDGNQLRNVTDVSTVREAFDEIVPFGSTPTGMALDEILRDYVDAYEDSKAAKGARMKPMIVLVLTDGRADDPDGVKDCIIEMAGRLDDAKAPPFQLGVQFIQLGNDADAAAFLAELDDDLKADSGVRDMVDTTPYEGQISPDFILKAALGSVVKRLDNP | Pathway: Glycan metabolism; L-arabinan degradation.
EC: 3.2.1.55
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Length: 855
Sequence Mass (Da): 94017
|
A0A137NR77 | VSSNNEVVALHDWIHDASYNVWPIGVNDPEDGKRKVVTNQGTPETSPSGWHDQGNGQKFTTTTGNNVIAYDNSGKNPKWELAPRAEGGKDLKFDFPIDFTKEPSTYKNAAVSQLFYTANSLHDIYYAHGFNEVSGNFQQNNFGKGGKQGDAVLAAAQDGGGVNNAHFGTPPDGQQPRMQMYVWTTTTPNRDGDFDNSIITHEYTHGLSTRLTGGPANSNCLNGKESVGMGEGWGDAMANILRTRKEHTRNTDFNIGSYIYKGKTIRSYPYST | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 272
Sequence Mass (Da): 29836
|
A0A151S2H6 | MSTESKFADSLGFASPIHNTILDTHNCFNDCSSFLLEKIANGPGSDILATHNIESGFQVSKYMPFGPVEMVMPYLLRRAEENRGLLAASGFDRQLMRKELGRRLKAAVF | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 109
Sequence Mass (Da): 12127
|
A0A6P4YMF8 | MKTFDLLGSSPAQYSAMGKFRIQGSPVINLSDTVSVNNNIDDTAVSKKPSETVEVTAEQKLAWLGAAEEAARLAGKEVRSAFYREKTVTMKSSPADLVTETDQNVEKMVFSFFRRKFPTHRFIGEETTAAGVPIELTDAPTWIIDPIDGTNNFVHSFPFVAVAIALAVNKEIEVAVTYNAILDVMYTAARGVGAFRDGKRISVSGATDMHESLVVTTAKSLLTPTKMADTFHNLRSLLERSRGIRNLGTAALNMCQIAEGAAEVYFEFGIHCWDMASGALIIREAGGVVLDTTGGPFNLMGRCMLAASSAELAQTVASGLRHDHKKPDTKEPVFLRSTRD | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 340
Sequence Mass (Da): 36886
|
A0A7D6ETN8 | MGPYTITPLIRARIGTIPCEPCVHKTHIYQLVDPLPWLPICNVYQTCIKNEMHSLIGRHLICNGIPNRSVAADMLRLLLTTFNPEYIEPLSRAEVIARKTDGPQRRRYARAKESLDRYGPSTSWARVSAFIKVEKWEQPLIDKKKPPRLIQFRTYPYCMEVSRYLIPIEEHLWKWQLNGLRVFAKGMNSFALGNLFWRAFNLFDNPFIIMMDHSKFDASLTEELIELVEHGLYRQFSNDPDFVKALKYQLANRCQTKNGIKYSCIGRKMSGEYNTSCGDSVVNLAIIMHTMEGTGIRYHPLVNGDDSVVICERDPRITPADFTKYGMKTEVETCREFTQISFCQSQPIMVRPEVWRFVRNPIRVMTRGVVSVKRYNGIGWAKLVNSIGHCELACNDGVPILQEFAQYLLRAGAKHSKEILVHEITYRAKLERRNPVPVPINDCARATFAEAFGISPTEQIGIEDSLRNHTSLVHPMSKLRD | Function: RNA-dependent RNA polymerase that plays an essential role in the virus replication.
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 481
Sequence Mass (Da): 55296
|
A0A151QQ52 | LLRPYSFLRTPTLTLKPPTKKILFLLLKPQNGVVGARMSNSSTSLPPTERLISVVAYGLPFLNSVQHGQYLMAQFPKLALLFEPILPFLAFYRSIPYSSFIAFFREEKGTNPSLSDFYFHTHRKKDHSWVGPHAKYAYKKFEKRKFELSSQSSTFTPGKDGTDSQLSTRAF | Function: Involved in protein precursor import into chloroplasts.
Subcellular Location: Membrane
Sequence Length: 171
Sequence Mass (Da): 19544
Location Topology: Multi-pass membrane protein
|
A3VCU1 | MARSIGNLSDGATSGVERGSPDSGAAYQVRAKASEFCEIAKFRAVVWVSFHRHNSISAQGPNHLKRKGTNMLNNIGLPGLAIIAMVVIVLFGRGKLSSIMGEVGQGITSFRKGVEAKDEDETASV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 13231
Location Topology: Single-pass membrane protein
|
A0A1R1XD13 | VQMIVDRLHLAYGFFRTEQSIDVINYLHGRNMTELVVNLPGWHNSVCDLLSDLVLIPLRKLCTDFKVLPNVSNPKSITPYQVMSNTQRWVSYQSGRSRNNGVESVIWNLSMLSAKLLQALQLLQTQSFLSAYRNLNDLISEVSASKTNPNILINKTKLECIESPEFNKLDRVCKILFKRINSPDPLVDNQMPIQLCGVSIPSGRIYSHPKLEHLAKAVTDHLNENESNTRIMIFTQFRESVEEIVAAFRPYEPLIRPVAFVGQSNVSFGASNNEENLDINTQSSFNQPPSFGGPGFTGVSSSSARGNFRGRFRGQSRGRGRGGSSSRSAPRNGMEDVDLSFDSTDGPKKNTSSGSKGLSQKEQKKVVEDFSKGIFNVLIATCVAEEGLDIGEVDLVIHYDAPRSPIQLLQRTGRTGRTRKGGAIVLLTNKTNEYQKYKEAIRKYHNVQKQISKPGTITWHKDLSPTLLPNYFEHTRFKRQTNQYPIKVEIIIKPDDYKLGAKLGDLDLMTRAEFKKAASKERENLKKIEKDNKKMLKSNSIKKKQIKKSNKKSSLLNFDNLSGYNSNGSSIGSDRESAYSFINDLSDAELRESAKKLIRSSDRNKKDKRKKTLNDFSSDLDKSPSKSTSRNLSPVTAAIKNPNLSENDSEEKEDKVSKRIKTVTQKSKMRSSAMEKLLVSRAKNQIAIQNVLK | Function: ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 693
Sequence Mass (Da): 77936
|
A0A067LX50 | MLTSTLLSVLLAAASSVQAHSTFQELWVAGSDKAGSCMRTVASNSPVTSPTSADIACNVNGNKAAASKCTVAAGQTVTVEMHAQPGDRSCSNEAIGGNHDGPVIVYLAKVPDSSTAQGSSVGWFKIGQAGLISKDYWGTDLLNANCGKYDVKIPSDIVAGDYLLRAEVIALHVAGSVGGAQFYPGCFQLTVTGGGNASPPTVRFPGAYSANDPGILFNLYGSYTTYTVPGPAVYTGGGPAAPTTSPGSPSPTTTTTTSRPTTTAPTGPAAPHYGQCGGIGWTGPTFCEGNYTCTKSNDYYSQCL | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 304
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 30961
|
A0A6P4XE59 | MTDLGLEVHRIAADSEATLEGGDVIFTGTEFFVGESTQSNKAGHKILAETFPEYPVHSIYVHPPEVHLKGFAAMAAPGIIALVDGENGRNGWKEMCEKSSYRYKAIWLPEDCAENCIYVNGTIIHGPERQFPKSYKILTEALADYPRIEVSTEEVYKICAALTCQCLLF | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 169
Sequence Mass (Da): 18746
|
L8HAM2 | MKRTCSARRAAVVCRSTAAVAQGSSTRSLHSAQPTQSGHRAIPPHHVHGPTCPCSAAHNPQYFYRGLLGAEGAEARASLTRPGVRFARRTQSTPTTHARLSSSAATGGLSRSGPKESEADYAFEMAGSNIRFGVGATREVGLDLVDMGARHVCVFTDSTLKDLAPVITVLQSLQDAKVNFVLYDKVKVEPTDASFKHAIEFVTQTARKVTPTGHFDAFVAVGGGSVIDTCKAANLYATYPPEDFFDYVNPPVGKGKPPPGALKPLIAIPTTAGTGSEATGVAIFDHVERNSKTGIAHRRLKPTLGIVDPENTKSMPPQVAAASGFDVLCHALESYTAIPYDQRTPRPATPLLRPAYQGSNPIADVWSLKSLEMLAKYFVRSVENRDDTEARAQMALAATYAGIGFGSAGVHLCHGMSYPVSSLAHHMTYKPKDYNVDSPMIPHGMSVVLHAPAVFRFTASANPDRHKQVAALLGAKDIENVRDSDAGPVLADRIIELMKRLDIPNGLQALGFSSNDIDALVEGALPQHRHDSHTHHRTRTHARLHTFTYAHIDGDRVLKLAPVPTGQEELAKLFQQSMQIW | Catalytic Activity: (S)-3-hydroxybutanoate + 2-oxoglutarate = (R)-2-hydroxyglutarate + acetoacetate
EC: 1.1.99.24
Subcellular Location: Mitochondrion
Sequence Length: 581
Sequence Mass (Da): 62614
|
A0A0B5I287 | MRLLTTNLTFKEVQPKLKELVDTLFKIVPAGVGAKGFVKVSKQEFKGVVEQGSKWCIENGYGWNEDLKRTEGYGRIDWADASKISDKAISRGINQIGTLGSGNHYLEIQRVDEKNIVDKELAKKFGIFPEQIVIMVHCGSRGFGHQIATDYLQTFDKVMQKYNIKIRDRELSCAPFNTNEGQDYYKGMACAANMAFVNRQVILHRIREGFEKVFKKSPEELEMNLVYDVAHNIAKLEEHKVDGKKKKLIVHRKGSTRAFPPEHPELDKLYQEIGQPVIIGGSMETGSFLLVGTQKAEDTFFTTCHGSGRTMSRTQARHEVRGEKLLQDMNKKGIYVRSVSMSGLAEEAGVAYKDINEVVKTVELAGISKPVVGLRPIGNVKG | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 382
Sequence Mass (Da): 42842
|
U7MPV8 | MSLKKQLANVSKRGPHRVLVGDLDYAGLPGKVYAPAEGNSLPAVAFGHDWRISLKHYRHTLRHLASWGIVVVAPETEMGMWPDHRDFASDLETSLQIAAGVKLGQGNITVSPNKLGVIGHGMGGGAAVLAALENEKVQCVAALYPAQTSPSSQDAAKYIDKPGLIIGPEDTDIFSAGNPPQMAQNWNGPVCYRAVDNGKQATFSEDTLRKFFLGIGIGKASAVETARGLVTGFLLHQLNGDKQYSDFSDPEADGKGFSSATGDELEEEKKPSGLLGKLF | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 279
Sequence Mass (Da): 29713
|
A0A1Y2G431 | MAGTKNPSKAPTPRARFVGVPATASSTLPSLPSAVTSWLPALSAAAPFSLSNFYHAVEIQTLNPEYNSSTILRADILVNEDLEDQEQAKQSVIEMESYDCVRRIRRKLQPKQTRDGSMEQECLFYRTAGSEEDAEDAEGLVLLLPDFELLQRDNGGVVPYYHPQLAALAFRYLPPPPSTSTDSEPPSASIQLDVLALPSSPLPTPLPLDHRIYRTALALLKSLHSVACGLDEGYQKRVHHDLLAGKEEVQDLYHVLKEKYRADLVPLHEPRITFPRWMLHEWKESTDPQKHLWEDVAVTAWLIVVWKHMYPETEGKPPGGFVDLGCGNGLLTYLLHSEGYPGYGLDLRARKSWASYNPSPTLLTTSLDPPTLLSSPEPPFPAGSFLIGNHADELTPWLPLFAAKTPNSAFLNIPCCPHTHVDRFTSKEYKIPPEFLDSLPSPPADPSPASPSSTHHPLLLPFYAPTSSNGGRMHAYQLYLAHLTLICGFIPEREALRMPSTKNIGQLGRKRVWDALDGKEREVAIRRVQEEVERMVKSAKEGWKARKPEGKAGEH | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 555
Sequence Mass (Da): 61794
|
L8GJV9 | MLRVSIRRVTPAKEKAAPEEKMRQQQRCWQSSLPALGKLTSLPARQSSQQCRSLFTAARLGGCPPKARSGPTGLRLAMPPRSSLGRAPLRSFANESREDIAARQQDLKNFVGGGNKAAATKPASGEAGQVMEGGLAAWFWIFPAITVYRWQEKKEMIRYRKERLLEPTVDLPPHLTDETLRDFEFRHVEVSGKFDPVREFVVRPRTRDGQNGGLLLTPFRRSDDGTIVLVNRGWIPAALMNDIVQRRAMLDRVSGDTRLFGLIRPGEKLASIHTTTSREAEGLFVQPVVEAARKDLLGRVVVEPRDRLVSVLQQPHSRC | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 319
Sequence Mass (Da): 35720
Location Topology: Multi-pass membrane protein
|
A0A6P5A2Z4 | MLLNRTKAPEHPTRQSPGATDLHGLVMICTTMYRETWDEMSQYLESIEKVATSQKLGEEYSWTGKFEAHVYFDNGVRGNKLTDFSAQLVCLVQSRYKECTVEIKKTWYGWTLQWRLPGSLQLPLYIHLKDNQEVKSKKRWSQVMYMESAVDRFDDSEVKYILATDGDVDFDADSIVAMLMQMLSDRQEEVGAVCARTHPEGSGPFVWYQMFDYAIGHWLQKVTNHVLGSVLCAPGCFSVYRVKAIASVLEEYRSDVEEASEFLTKDMGEDRWFTTLLVKTGWRVKYCAGACDSTHCPEEFDEFWKQRRRWIPSTLANQILLLKNWKTINQNNKYISMIFLLFQIVLLLSTVISPSTCILIVTGGLYYGVGVPTWLSFVLFVLLTLAFALICMYYSQETQLKVAKILCFVFLIAMAIAVVGTASQMAISNTSSAPRIANDNGKYQGCYQEYSYSGDLLLPNAVTRIKDLTNAKCMSHCHENNFYYSGTGSPGTACFCGPQQALENATRLQENMCASPCPGDSGETCGGRPNQMSVYEINRLFGVQLQVDVTTLYIAIVAGIHIVAALLHPREFTCIFHGVVYLFTLPCVYILMNVYSVCNLTDQSWGTREAKSQKEQSKESFLDDVVAKMRQCWSFCRRSYHKLDESIEEEPEREAMEDEVDGRIDVGDSVSSGSRGHMRSIPGEAQPDPGKRFKSTRQWLQSIFGALSNKVEIYEPIFTREGYTDTSFIAGMSDEDLKDIGVADLHDRNDFRRHIRKLHQDEPDIDIRVPDNVETWLTMISLDTDEYKEKFRRAFPEGTKAQIVFQELKTMTEDRIVHKLGVQAKGHLRRLKLAITRIRQPTLREERILKAKRDIDGKFQEHPPDVIAHSKKPYLDPTTEQFRLDQNKEDEFKQNLQQLRNSYLLTYLVANSVWLVLMFTLVEHAELQVINTNPLGLVFLVTFTFVLGVQFAALVIHRLATFIQYVSRIPMTRERISAMCLNINSGYEPI | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Membrane
Sequence Length: 990
Sequence Mass (Da): 113172
Location Topology: Multi-pass membrane protein
|
A7TF45 | MIDPKIHPTIPPVKEITHTLTPPLNHFKEWITRSLTLKLFDPTAPTIIFTDASLTGGASIIFQPETHNKKQILFPITFLSVRFTPTQQRYSTVERELFAVLHALEKGNLLLSSEITIYTDNKGIISIGNSDRNTHPRFTKFLDLLNGHRLKWKYLPGTKNVLADYLSRFGLKDQPELDLDLLQKDAIDLPVATLSSLNLNSTDASPNSTTIDPASSVPLSTDNTNTPEITSNTTPSEQDETEESLDPNYVVDNVNSLTMSQLIQIQTLLSTKETLIPHLFSKVIDKFLYISDLLYINLDLVLYRVVIDNDYIEVATKLHGLYHCTHRVLQLAMNDQKLWNPNSNLLLLDVVKQCPRCETYQKFRDIPIELPEIRRIPVFSRWHLDFAGPLKDKDGYKYFLLAADYTSNLILVKPLREQTFHSVYEIMRAIYAIFGSPHMLITDNGRQFANAIIPQVARSLKLKYYQSSAYHPRGNSKAERSVKMIKEVLKKLDPTFTNWVTNIFVAANIVNNTKMLYGYSPREIAFGLPSENIEVDFQQAVKSLLQKENNETGEQITNQEQAHLSLMSHVKTNDIRLKMTDERIKIRELLKNARKDTDNYVPYTRGEIVYRLRVKKNTFEPTWDGPYHIEEVVAKNTYKLRDRDGKVRKATYDGSKLKPAYSFYGSAIRTAAEYTRVYGDKERKYFLKTLGDIDKYIAKEPKRD | Function: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 704
Sequence Mass (Da): 80878
|
A0A0P9GKJ9 | MSIDLEWSALDAHLTQACTRFLSHAFNTAPTPDFLGPLEVTAFSFGDAHPELTLVDIRDIQHDRSRSRSPAAAPGRGRPPLAGGGAHPLAQHDLHSQHTHTHPHSYAAPSPSPSLSSLPPLPPPSSAPSPSFQVHLRLSYSGNLSLGIATALRINYPSSSFMSLPLSLTLTGLALEGTLVVAFEGGRRRVHLSLLEPDPFSSTTPGARVLRAAHVESEVGQADKHVLRNVGKVEKFVVDVARKTLENELVFPCVLSLSLSLVRRVLVLATTRLVGVVGTSRRPHRRDGTDTSVVAPFHSNFQTIVF | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Location: Mitochondrion outer membrane
Sequence Length: 306
Sequence Mass (Da): 32920
Location Topology: Peripheral membrane protein
|
A0A7S3XW17 | MDQELATLIEKAGSKKSSLELLAYMRAHKVRRPDLVFKYGVKLLNSSLGDEVWTIYEQVFMASLDLGEQEVANHALNALKKKFPGSSRVKRLAGLYEESEENYPQAEALYAELLAANPANTLALKRRAAVELARGRPAAAARALGDYLRDFPADVAAWEQLLAVHLGVGGLAGARFCLEELLLAEPGRPRHHRRLAELLYTQAQGEDARGAEA | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 213
Sequence Mass (Da): 23437
Location Topology: Peripheral membrane protein
|
L8HIX1 | MSINQIINGDENFAGLMPLVRQYVASINVDLETRVVIDKYLDLVSKRASGELMTMASYTRKFVTEHKAYQKDSVVNDEINWDLMQHLLAVGEGREKAPELLGDLYTPLADADLGELLDSLPPPKCCPHDPQAATVHGEVLSPTVIATVAQ | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 150
Sequence Mass (Da): 16506
|
D5X824 | MAHVVNREIENYLRQLVPERDLLLKSLEEKAEQEYVSIVLPEVAQFLHLMALQSRAQNILEIGTAIGYSTIWLARVAKQNGGRVTTIEINQRRYEKALNSIKQSGLEDVISIIKAHAADILPTLSGTYDFIFVDAAKGQYSSFFEKLYPRLQTGGLIIFDNVLADGLVICNDEDIERRQRTMVRRLREFLKMITGYPGLVASVIPMGDGLVVGYKTG | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 217
Sequence Mass (Da): 24416
|
A0A0G1QT40 | MNRGKFIVIEGIDGSGKTKQFKLLEQRLRSIRNKLITTDFPRYYESKWGELVGRFLTGEFGKLEEVNPYLAVLPYMMDQYTWSRDVATPWIKRGGWILSNRYFTSNVHQIAKLRTATQKKYRDWLWPMGYKELGLLKPDLVIFIDTPPEVARKLNLRKGKRAYIKRKKRDIAENHWQHQRAAYREYKRTVATYHWWVSVPGIKNAERDYSNKIHENIWQVIEKTLLRKN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 229
Sequence Mass (Da): 27451
|
D2QWK6 | MAEFINVEFLSRVFAPLGWSFAPGSIWGYVLAAAIHIGLLIQVVAVGALVFIWMERKIAGRIQDRLGPTRVGGKFGWLQTLADGLKLIAKEDVTPKDADRLLFKLAPYVSFAASFTAYMALPFSSGWVAQDVNIGVFFIVAVLGLEVFGVILAGYASGSKWSLFGGMREAAQVVSYEVPIGMCIVIPVVILGTMNLVTIGDMQAGWFTNWLIFNDPFTFAVFFVYFTCATASVNRAPFDLAEAESELVAGFHTEYSGLRWSFFFMAEYGSMFLVSGLAAILFFGGWNGPIPLFGPEMLGWAYTPESTSWSILGYIATLAGCVNFIGKTVLFVTVMMWVRWTLPRLRIDQVMTVCLKYCVPLAAFCFIGAVAWRLLELPTPSDIAFLKHHPQGRAAIREGWIMEQARIDATKAAAAKPEEPAEKPAEAPAAEAEKAAAATEPAAREAAVLVKEVAR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 455
Sequence Mass (Da): 49655
Location Topology: Multi-pass membrane protein
|
R6PLD5 | MNMTALNTIAKEATVTSKGLMTGMDSTARLVPSDKKGIRFHLGDKTVEAHVDNVVSTEHCTVIGNQDIKVMLIEHFMAACAICHIEAIDVYLSHFEMPILGGGSAEWVEIFKEAGNKAQESYILTEPVSYFNGKTHIVVMPSDEFKVTYSVNFNHPELNHRWVSLDKDKLNEIIEARTFGYLKELEMLQAAGYARGVSIENTVGLTEDGYTTELKSDFEPAKHKILDLIGDFYLTGFNPMDLKAEVIVKEAGHAVHVKVAKILKDKIQKEN | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
EC: 3.5.1.108
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Length: 271
Sequence Mass (Da): 30203
|
A0A0Q5MTX0 | MENGMTAHAILVIGSINYDLIVSQERLPRRGETLVSTGFRGDFGGKGANQAVQAARLGAEVLFVGAAGADRYGELCRLNLESEGVDHRLRPTEASNGLGIVHVVGEGEVHATIVEGANAVVTGQWVGENADLVASSAVVVLQNEVPASANERAVALAAAAGVPVVYNAAPARPVSLSMTRACTWFVVNEDEAAEYLGHPLGEVTDDAAMRAVVGELGSFCSNVVLTLGSRGCYVSTDHRAEFVAAVAAHAVDTTGAGDSFIGAFAAAIAEGVDPFRAARTAALVASVTVAGMGAQSSMPTREALDDEIVRQTSADPRSRRAG | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 322
Sequence Mass (Da): 33141
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.