ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1I7XAV9 | MNQTDIYRFNRASLINVGWYESDRIDCDYMVMHDVDLLPINSDITYAWPGLGTVRHISSPQYHPKYNYSKFIGGVLMLTMQDYKLLNGMSNKYWGWGLEDDEFYLRIKDRGLNLSRITGLSTNRNNSFRHIHGRERKRDYAVITKTEKSIKRKRDKISGLGNVKYNITNRRILHYGNAIVRIVDVNLICDLKWTPYCLMPNSAVG | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 205
Sequence Mass (Da): 23992
Location Topology: Single-pass type II membrane protein
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A0A8J5FEU2 | MEIDLTRGSQLVYVIPDTMLTISDFYRNIQISILARGYEAWQHGEANLLLTRGLVGRLSNTPNVGFAYEVQNVVDYLASSGIRALPGRRYNTRDVLGQNWIIRQSTINIPMQPTEVNTRNLLDGRISLHFENYQVAAASMQARDDHYDNEDKERAHTIAVLLKDNEEDVLYVKCLTSTAVLPQRKTEGAAGYDLIFNQSYHIPPYGQAMLNTSISIKLPKGTYARIAPRSNYAMRGMTIGGGVVDPDYRGEIKILVYNYSDDEMNFAEGESIAQLILECCKTPPIIQVHDLDKIKRQDKSFGSTSQQYPCTSEKANPLSD... | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A0T5ZKG5 | MKLATRDIVREIDRISIEEYGIQGLILMENAGRAVAEVVLDEFPKVKRVAIFAGGGNNGGDGFVVGRHLMNKGLDVTTYLTVDPKKYKGDALINFQALSKIGGEIIRLNNGFAGYKGADLIVDALFGTGLDREVDGFYREVIDYINSQAVPRIAVDIPSGLDSDTGFPLGVSVKADVTVTFVLPKIGLAIYPGINYAGKVYVVDITTPKFLEEDIPFELIAYNNVREILQPRHPNTHKGTYGHLFILAGSPGKTGAATLAALGGLRVGTGLVTIGIPKSLNPIMEEKTTEAMTEPLPETENTTLGKVSIEAAKRIISARK... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A7X4RUT4 | METSFLALTLKREMPKNTVFYAHGLTFHWLNHGVMVIEPAGVDDSLPSIILSAGVHGNETAPIELLDSMVADLRSGALSLTRPLLVLLGNLDAMNQGERYLDYDMNRLFCQNHRRFPDARESKRAAELEKAVIRFANEQLGPVYHFDLHTAIRGSHHMRFGLLPFVERGEYPDVFVEQLNALALDALVINHAPANTFSFFTKDQLNVESCTLELGSAKPFGHNNAADFTHIDQALRTMLEGKAPLQSQHPALVYRVAQQITKLSDKFQFYVADDVKNFTPYEPGFVLAEDGETRYQVGKQTEYVLFPNPKVKAGLRAGLM... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
EC: 3.5.1.96
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + su... |
A0A0T5ZW55 | MKVIIAGGGTGGHIFPSISIAEEILKRHIENQVLFVGTKKGLEIKLLSKRDYTLELISSGGIKGKGIVGSLKGIALALKGVFDSLRIISRFKPDLVLGVGGYASGPLVFAAALLSIPTAICEQNSVPGITNRVLSRFVKRVFASFEESNRFFSQKKTIVVGNPVRSSILINKEYSQAHNGFTILVFGGSQGAHKLNLLVPKAFGTLRRNDVFLIHQTGKEDLEDVRKAYEWYGIRADVLPFIEDIATVYKNANLVIGRAGAGTVAEITALGKPSILVPYPFSAYNHQLENAKVLEKAGAAIVVEEKDAVPERLTDILKDL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A7V6HSE7 | MRDFQAIKEEILSHIQSENYKRKNASTLYKVLGLTDTISFSQMTRILAELEQEHLIGRTKKGTYDLFERLGFAKGTIVIKESGYGFVICPNHEEDFFVPRDKTKGAMSGDQVIVKVDNSDPKGPSGEVVEILERAYTYLFGTVVKKGKHYYVEPDDYRVTTSVFIKDVPGWNLKPGLKVKVFLTKYFPDGRLDGEIVQVLGDEDTPGLDITTVVLASGIRTEFNEEIKAELKRLPQEVEEKDLINRRDLRHKPIVTIDGADAKDFDDAVYAEKLENGNYLLGVYIADVSHYVHPGQAIDVEAEIRQFSVYLPDRVYPMLP... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 704
Sequence Mass (Da): 807... |
A0A9D7LU50 | MEKKGQYDVLHRLSNTLASRRNADPESSYTAQLFAGGPDSILKKIGEECAELIMAGKEGKRLKIVWESTDVVYHLMVLLAFYGLGAEDVLQELRRREGISGIDEKKSRGAGHHHKKAKDDHK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 122
Sequence ... |
A0A2H6GSL6 | MRELIVKSEQSKQRIDKFLVRELFSYTRAEIVRNIKNGNILVNGKKAKPSYKLKGSDIIVIPSPLSSPGGRGRLKPNPEVKFEVIYKDRDIIVVDKPAGLKTHPINYDDKNSLINGLIAKFPEIKNISDPSTRLAKTSPRRTSSEQADLRPGIVHRLDKDTSGIMIVARNQESFNELKKLFKERKITKKYLAVIHGKLKSKKGIIEKPIARAGNYKKQVIAGRKTKTKIREAVTEYKVLKEYKDYSLVELTPHTGRMHQIRIHLFSLDHPVVGDDKYKLKKTIKPKNVSRQLLHAKDLEFKLWSKKHSFQTELPEDFSDF... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 333
Sequence Mass (Da): 38184
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A0A8I6RGA4 | MQKMDCESDSEKLKMWAAISFAVMLIVIGIPLWWKTTEVERAFLPYDEIYKLKPSVVNIQMKVFIHCQYPSRTNALIGDLKNMLMTDIYDLVYTPFKINNEIETYLDIENDERLNNVTYGNILLVEVHHLPQRYKVLVSNKRIIYFTPETSNHLIVEVMRDWHLRESDLKTKIKSIIVPQSVQESENLDSLRAALNYDMVFTIINSNPENVKLVWDISTDIKRYIKPLLDQISAVSLHSLKSQWLYFIDFGVLPEKNSNGYTLPLSQLPHIITPLEKKLGSGISKNPCVHLILYTSSCDQSPLSFVSPTGRLVNSMISPQ... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 518
Sequence Mass (Da): 59010
Location Topology: Multi-pass membrane protein
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A0A4P7JBZ1 | MKPTWRWFGDTDPISINAVSQTGAKGVVSALHHLDPGVVWSGPEIAAHQEKICNTPSGEATGLSWDVVESLPVSEEIKQRKGNFEDHILAYKDSLTHLAAAGIRTVCYNFMPVIDWTRTDTEHRQPNGATCMRFDYVDFAVFDVFLLRRENAKADFPAEVIAEAQLRYGSLSQEGQTRLIHTIIAGLPGSAKGYHLDEFRKAIDAYKDITPDGLRNNLRAFLAEIVPHAEQSGIRMAIHPDDPPFPLLGLPRIVSTLGDYKAIGQMHDSPANGFTLCSGSLGARGDNDLVDMFKQLKDRIYFLHLRNVARESETVPTSFH... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 401
Sequence Mass (Da): 44475
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A0A7S3D6X9 | RFHLSRTPIPISRCTARNSFPMKFYPPAAVGAVVLTQMALFYFNAGGTSLALPSFLVWVGLVLLLLCGIAFFHATRCFAVHDTTIFPDGRPSALIRKGPFLLSRNPIYLILAVAMTGTALISQCALSFLLPPAFVVWVDRRWIVIEEENLKKEFGKEYEDYCKKVRRWI | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 169
Sequence Mass (Da): 19099
Location Topology: Multi-pass membrane protein
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A0A3C1FET4 | MNTTTSVAELLALGDEELFARAQADRADLPQFTWSPNLINPACRTDPRCEHCKWECFKTEQQMFEARRPIDQILAQAEVQVSMGVKRILMPSGWLGYHLPSYFFASVRAVKERFDVEVFGLSGAIDRESLAGLKDAGMGGYWCGLESINEEIYRRFRPGGDTLADRLETIANVQDLGLKLQSGFVLGFGLPEADVIASLELLAGMELNSLVIQPFIPFPHTGMAAEDPVNPHYWARVVAAAGIYLPKVNVIITEADGPHANFATLTGANVWPTFPKLFAGGNQQPESTGLTLPKAG | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe... |
K2GCS6 | MEKKSIQKLKEEEQTGLLTLANLHELYGDERKGVQQIVKRIRTKEEKKLKLKDKWDRMNGLEEDAKDRGHAYVAGIDEAGRGPIAGPVMAGAVCLPESFVLYGLDDSKKLSERDKDHFYNEIMARADVGVGAASAEEIDEWNIYRATKLAMKRAVLNMRETPDHLLVDAMEVPVPIKQESFVKGDERSVSIAAASVIAKVTRDRFMKEVDKKYPGYNFLKNKGYGTKEHMEAIKEKGITPYHRKSFVPDGIK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A0A1H7T6 | MSTSTGEERKSPSPSRPPLSHPAHWIATGLGSGLLRPGPGTWGTALAWALFVVIAPHGAPDLATGLLVVAVALMLGTWAAQHTGEMLGEADSGTIVVDEIVAFWLVLVLLPAGDHPWGLQAVAFVLFRIFDITKPPPIRNIDRHWKGGVGVMADDLVAALYTLLVIAIGLRLLR | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A1Y5EZ15 | MSHKMSRFFDSMWYGQRPVALLFAPLSWVFGRIVWLRSFMFKKGWLASTRLNVPVIIVGNITVGGTGKTPVVIWVAELLKSAGYTPGVISRGYGGIASSWPQQVREDSDSRVVGDEAKILARRTGCPVAVGPIRADSAQALIDHHDCDVIISDDGLQHYALQRDIEIALVDGERRSGNGYLLPAGPLR | 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 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A7X8VTW9 | MDKNDQNPQNNHIRIKKHLGQNFITDVNLLKKIVSQAKVTKNTFVIEVGPGRGSLTEVLLDKANKVLAYEIDSELIPELVRRFQNRNNLILVNQDVLNVDINADLEKYFPADAEIAIVSNLPYYITTSILMKFLEATDKLSRIIVMTQLEVAKRLTSKPGTKEYNALSIAIDYRSDAKLLFKVPREVFKPIPRVDSAVIALGMPKATPYAKPIDEQLFFTLIRAAFAQRRKTLANNLLSAGLVCDRDAIKQLFEQTRIPISARAEIINTATFIDLANRLVNTEENITKTPAEELI | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A7X6VQW0 | MSSFKSGFIAIIGRPNVGKSSLLNSLLNTKVAITSPKPETTRSRILGVLNKTDQYQLVFVDTPGINEQFNLLDQKINEVTISSLEGNDLIYYVVDQAYHKKDEAIINLFKRLDTPIYLIVNKIDLLKGKQGIDKIILSFLDKFPFEAVIPVSAKDKTYLNRLIEITVNLLEDDGVMFFPDDYLTNQSDALMISELIREKILNLTEKEVPYATTVIIETLDYNEEFKTYDVNASIIVERDSQKKILIGKNGEKIKQIGTEARKDINQVLETRVHLDLFVKTKKDWRNNPVKLKSYGIGEY | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 299
Sequence Mass (Da): 34113
Location To... |
A0A8E2JFY1 | MWITKWLWDVFESLGLWKKHAKLLMMGLDNAGKTTLLHLLMNDRIEVVQPTLYPSTEEFTFENCKFTAYDLGSSNSFRNRRLWKDYFPVISGIVFIVDAADPERFEEGKEEIQALLRADTLSSTPILVLGNKTDLPMAVSKDELRHELGLHDTTNDIAPIESVQPPVEVFMCSVVCRQGYQEGLQWLSQHV | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 191
Sequence Mass (Da): 21904
Location Topology: Peripheral membrane protein
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A0A7G6E0D6 | MRGNKILTVSEVSFHIQKLLDDDPLLSNLWIRGEISNFKHHSTGHFYFSLKDKECTLRAVMFKSKTWRLNFLPKDGMDCLVRGYVSSYPKDTVVQLYAEEIIPAGVGLQALALAELKEKLQKKGYFAPERKKPIPYLPGAIGVVTSPAGAAIRDIYRVVQKRYPGMPVILFPAGVQGEKAAQSIVEGIRALNGRKEIDVIIVARGGGSAEDLSVFNVESVADAVFASTKPIVSAIGHEIDWTITDLVADVRAATPSMAGELVVPVRWELENSLSKYKERLLRAARGRMERENMRLAYLKEAGVMKKPERWLNRYQDHLSR... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A2T2XLZ1 | MNSVTAPVFRFGNDVDTDVIVPGQYLKLGYEEAAAYVMEGIRPGFGNLLQNGGIIIAGENFGCGSSREAAPAALKFAGIRAVIAPYFARIFYRNAINVGLPAIECPEVVESPIQEGEWVTIDFVSAFIQHNRTGNRWSYTPLSLHLREILLAGGLVPFLKGQRQSDKGARL | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
EC: 4.2.1.33
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
... |
A0A1F4XL47 | MPTPLIVSALLGLAVGIVGMILYQSFIRRSKISKLEAQAQESLRQAQKEEQNIIREAKGQSQKLLDQVRKEELERKKKLQELEQKNQKHEHEIERKLSELTNQQKELDSALEKLRAEESTLSEKKKSAEELLQKISSLSPAEAKEILFKKIEEEYQEDLMKHTEKIIKESQEKAAIQIKNILAEAMQRYHGESIAESTVTTVTLPNDEMKGRVIGREGRNINAFEKLSGVDVIVDDSPGVVILSGFDLIRRYIAKLALERLVADGRIHPTRIEEMLSKAEEDVNKMIKEFGEKVVYELGITGFPAEIMKLLGRLRFRTAY... | Function: Endoribonuclease that initiates mRNA decay.
EC: 3.1.-.-
Subcellular Location: Cell membrane
Sequence Length: 508
Sequence Mass (Da): 57314
Location Topology: Single-pass membrane protein
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A0A2G9XM39 | MPVFFISIRWGKTLIQLDYSLLLQIINFVFLIFLLNFLLYKPMLSVVDKRKRRLEESEEEINRLKRTVEEKMAVYEEKMRATRSEYLGKNKEYVKEGADKAKEILDETGRGISLIVEEFSGRLEKEVHVARKFLSGQSRILSVEIAEKTLGRRIQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 18258
Location Topology: Single-pass membrane protein
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A0A1F4XIM6 | MLSSWLTIDRQAIAHNLQAFRKLLKPQTKLFGVVKSNAYGHGLGILSAVEPLVDGLAVVNVAEGLEIRKRGFKKRVLVLGPFFSHEELLEAQKNNLEIEIVKQEDLTYLRFALPSNLLPPLKVHIKVNTGLNRLGFLPQDLSTILPQLQNNPNIVTQGIFSHLSDAENPASLQTKEQLQSFTEAINSFPESAKNIEKHIAASSATLLFPNSHFDLVRIGISMYGLWPSQETHDAWHAMQPPSSSSTPPSSSSSNLEFRTLRFHSGQALNLELFPALTYQTKIMCIQNVPAGSLVGYGGSYRTRLPSRIATIPVGYYEGLP... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 399
Sequence Mass (Da): 43919
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A0A2R7KGN8 | GINIEFVQDNQSFSKKGTLRGLHYQNPPFAQTKLIRVLDGEIIDIVVDLRKDSPTYRKSFRILLSAGNKKQLLVPQGFAHGFSVISQTALVLYKCDQFYNKESEGGIKFNDPSLNIDWGMNLNEAIVSEKDQILPFIDNCNSLF | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A453CTH2 | AFFFKFLEGDSEVHVYWKGAAELILESCTSWIDKDGSKQSMTPEKVGEFKKFIEDMAVASLRCVAFAYRPCEMSDVPKEDQRADWVLPEDNLIMLGIVGIKDPCRPGVQDSIRLCAAAGIKVRMVTGDNLQTARAIALECGILTDPNVSEPTIIEGKTFRELSDLEREEVADKISVMGRSSPNDKLLLVKALRNRGHVVAVTGDGTNDAPALHEADIGLSMGIQGTEVAKESSDIIILDDNFATLVRVVRWGRSVYANIQKFIQFQLTVNVAALIINVVSAVSSGDVPLNAVQLLWVNLIMDTLGALALATEPPNNHLMQ... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 500
Sequence Mass (Da): 55296
Location Topology: Multi-pass membrane protein
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A0A3B8JHK5 | MWDSIIKPALVLFLVCAVTTGALAVVNRATVDVIEQRTNAEQEEFRKQVLDNADSFKQIELGSGNEAVKNVYAGYRDGELEGYVVNITAKGYGGDIGMIVGVDKNGTVTGVIIGDNEETPGLGTKVFEPDFINQFEQVGVNDELTVVKQNRKSTNEIQAVSGATITSRGVTQGVQAALDITKKLMEEGN | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 189
Sequence Mass (Da): 20299
Location Topology: Single-pass membrane protein
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Q0C904 | MGFLSRLRKRSKSQSRVRRNPSWDLRFESHDPLPPLPPSGPDYTQKLPRPVLRRIFASVCPHTVDNSYDTSEESMTDDGCMLCDMRDLAHCALTCKRWFTDARELLYTHVRIDPVHYCELEVELAAKRKRRSFFDRNGDPIDAPLVRLNLFMRSVRQSQGLGNMVLSLRMPYMTREASKADIARTVSVLPNLRYVDLPAGIYSDDQSCLALKQELMARCPDIRRMSYRHGAEGSFSQIPSSHLWVNLEVLELSSLHIEPNILRFGLGSFPRLRDLTLSDLPWLDDPAFAPSQSLPPFPPVQRLTLRDTPNVTASGLAGYF... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
EC: 3.2.1.22
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and ... |
A0A432R4Z0 | MKSAHLEAPSSQTQKVLNPLSRKLHYYFSAVVFLSVCSVLLGIIVIQLQEPSSSGGTIPQLLPQSTSQIILYSLAWGVIVSCLASLGIFFLSRKITAPLTLLSRVTEKINHGEFYSQAILDSEDEIGLLKNAITEMSTQLHELKQDNKDCTEQFDGRTKSAKLMHDRLETIFKTSLYGFWRVDNDLITQEINQRMVKMLGGQTSDFIGKTITDFMGTPNRTTFHKQIHLGKNLLSTEYEVELKQLDGTFIPCLFNATPLLDENGNKHGSFIMVTEISTLKKTEKELLKAKSLAEHASHVKSSFLANMSHEIRTPLNGIIG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 827
Sequence Mass (Da): 92150
Location Topology: Multi-pass membrane protein
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A0A3R9KZH3 | MAIRMWSMFISATFVKKSTRVIPSPISRQSAGQVICSRRRKMKLKTKIHVFTTLLAVVIFAVMNGITYFLFEQMSYSGAAAPLRADAQQAVAKLSTTDSLPEIKTILRAYVPANGAIQLIHPDGKMLASVETTEGLHNIHVEISPDENYTLTQQNGQRIMTIHSTALLSDGSVAALHIHQELKEIGVTLNLLKKIVLIATLTGAGLMFLSSFILGRQVTAPIHRLIQQMRENRIAGAYERIKLNEHEKDETAQMGREFNEMMKELEEHFGKQEQFVSNASHELKTPLTIIESYANLLKRRGVENKELTDEALTSILSETE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 483
Sequence Mass (Da): 54060
Location Topology: Multi-pass membrane protein
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A0A969Z959 | MIFEKIKKIIVDELGVSEDKVTLEARLSEDLAIDSIDAVEIVMYIEEEWDISVSDEEAFALKTVGDLVNYVEGLVESK | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
U7UBD9 | MIELIIGKIEEINENSILVVNQGIGYCIFLNGRESKNLAIHEDIKIYTSMIVREDDISLYGFLSKDERKIFKLLITVSGIGPKVAMGIMSELTQNDLRNAILTSDINKLQSAPGVGKKTAQRIILELKDKISKINFENPLESFISNENDFDITSSDNEVVEALVSLGYNNNEVRNALRRIDANLPIEIQIKEALKIIGR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
C0GFY8 | MRMVQVPLGERSYDIHIGENIWPAINEIWPQRLKPGQVLLVSDENVFGLYGGKLIAALHEAGFSVTPAVVPAGEQSKTLKWADTLYTAAIEAGLDRSGFIVALGGGVVGDLAGFVAATYLRGVPFVQVPTTLLAQVDSSVGGKTAVNHRLGKNLIGAFYQPQLVWIELETLSTLPKREYLAGAAEVVKYGVILHEPLITLLEKQWDGFIAGETPVLTEVIGDCCALKARVVAEDEREGGLRAILNFGHTLGHALETATSYKYYLHGEAVLAGMVLAVQLAQRRELLTEEEARRLLRLFARVGLKPAPPGLQAEAVLGALK... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
A0A7V6HRS3 | MNKRYRLKRNEEIARIVRGRKRVSSPSFTLYYQKNNLKTNLYAISVGKKYGSAVERNYAKRVVREIMRPLLDVLPHVSVLIVVKEGSKTLKFLQLKEELTQLINQINQKINIEEN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A7X7LSJ3 | PKIAKVVLPSFSTLAEIGSDEVGTGDFFGPVVVSAAFVPSEAITKLVQMGVKDSKQLDDDIIRKISASTKNSISHVVLVTPPKKFNELVQSGYNLNKIKAYLHNHAIRKLAQKHNNEFQSVIIDEFCSESNYYRYLADVEAYRKVTFVQKAESSHIAVAMASIFARASFLEEMEKLNDLTGLILPFGASAIVDLIGKRIALEKGLDFFEKIAKINFKNMDKIKAMCP | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
A0A7V6LLW5 | MIMNYALQAITRIINEGAYCNIAINEVLQKNQLSDHEKRLFTHIVLGTVENKIRIDYYLAPLIKGKRIKPYLKNTLRMGVYMLDEMRLAPHYVVNALVQMIKKQDFKGSRLVNGVLRTYQQLPKPDLTKLPQKEYLHLKYSFPRDLLNLLMREYPDQVEAILAEMQKPTPNYYRINTLKIKPEEVAKILQTEKSEFQVLEDCLISQTSLINHALFEEGKIIAQNPSSIKVAKTVNPQPKEAVLDICCGLGTKSMHLAGLMDNQGEIVACDIYPHKLRMVEDSATKLNVKIIQTVLADATVYQFNRLFDHVLVDAPCSGLG... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 415
Sequence Mass (Da): 47625... |
A0A453C0B1 | MPKTKKCLEDIDCFIRENHPKECGIIYCLSRMDCEKVAEKLREYGHQASHYHGNMEPSDRAAVQRLWSMDKINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYNYSDYIRVKHMITQGSAEQVRSSSSSSHGQALATHKENLLCMVSYCENDVDCRRLLQLIHFGETFDPSHCSKTCDNCKKGLRWIEKDVTNIAKQLVGA | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 223
Sequence Mass (Da): 25392
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A0A1H8S959 | MAHPSLAPELDDALRGRAAGIQLLALDVDGVLTDGTVYYGADGETLKAFNIMDGLGLRLLERAGIRTAIISARQSAPLQRRADDLGIGFTYFGQHDKPAAWAALLERTGLTSAQAAFAGDDLIDLGVLHRAGLAFAVANAHPAVRAAAHYVTGRSGGDGAVREMAELLLAAHGALDGVIADYASG | Function: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.
EC: 3.1.3.45
Catalytic Activity: 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate
Sequence Length: 185
Sequenc... |
A0A352TTS7 | MKTTIIRIQNLNEKILKKLDHQHMPIAFPTETVYGLGAPYDNETTIFNVFVLKGRPLNNPLIVHVATYEMMLPLVKEMHEDAQRLMTHFFPGPLTLIMKKSDQVSSLVTAGQNTVGIRMPNHPVALELIKKIGKPMVAPSANLSGKPSGTTALDVYEDFQGKIPFIIEGKTSEVGIESTIIDTTREPFVMLRPGSITKEMIEKVLKKSLASTINHDVVAPGMIHPHYEPDHPLYILRGDDAHIINYVNQKKDALFIGHERFLPFIDIQKLSLGSDTDDMLRYLYHVLRQSNHMDIKAIYTHEIDHEGYMNRLLKASKNQI... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
A0A7X7R5Z3 | MGYRALYRVYRPKDFTEVTGQKHITITLQNALQNNKVAHAYLFSGPRGTGKTSIAKIFAKAINCEQAPVANPCNICPNCLGIQDGSISDVIEIDAASNNGVDEIRELRDKVKYLPGYVRYKVYIIDEVHMLSTNAFNALLKTLEEPPQHVIFILCTTEPQKIPLTILSRCQRFDFKHITVGEILMNLHEVIRKEEIVIDEDALEQIAIFAEGGLRDAQSLLDQVHAYSPEYIKLDDVNQVCGAISVEKQIDMAKAIIEMQPTRAIQSMNELIIEGKELYRITLNLLDFFRNMLMFKNVGITGVANSILSNEQFIQLAKMT... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 628
Seq... |
A0A2M8GDD8 | MFGIGIPELILIIIIALLVVGPGKLPDLARSLGKGLAEFRRAADDVKGTLKETLEVDEVKKDMDEIKNSLLYAEKGNGKDHNKPSSSSEGKENSSRSFTPST | 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: 102
Sequen... |
A0A2G9XIL4 | MICIPVVAATQSEALQFIERAAKLADVLELRMDLLSDGNVKELIEAAHSFSTRLKVLVTNRIMEASTPRDEKKRIGVLLDAVALDADFVDLELFTALPWIETVRAAIAARHNRTALIISHHDFRKTPSRRTLNRYFEDSVATGANVVKIVTLAKTPADNLPVLSLIPYAHRRNMQIIAFCMGEQGKISRVAAPLLGSIFTFASLERGSESASGQFSIGVMKQLLEILGEKSES | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DH... |
A0A8J5KRQ4 | MSSDWVSETSQLTDDIANLNISQDIEEQEAAHVNTTQLQALEQLEYPILRRLMQNTKEKAFTSTSDSAISNYKQPNEPLMGQINYPPAQGTTPQFPDNGQYKGKFKGKSMEHQTWTLPSAQQNTRAMLVLPDDIGIYAFLSGEGKEGGNIQFSQGQKINTTAKILERRTEGTAGYDLFIDQDIEIPAKDRRLAKTRISIEFPEGHYARVTTRSGAAIRLKIDIGVGVIDANYRGEIQLLVINHSNNVISLEAGDSIAQFILEKIITPQIEEVDFLSTTT | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A651DJ51 | MSVRSVNNRPLILGLTGGIATGKSTASAYFKAQGLVVVDCDEIVKKLWQEDKTMVKEIKDVFGFAVDAPEARRRFSEIIFEDASKRKALNTIIHPLVFNEIEKQLLQHRHEPVIIIDMPLLYEVKYQSKCDQVMLIYINKKTQIERLMKRDGLSRSQALKRLASQIPIGEKKAMADIVFDNSGTQEQLIEHISTFIKELQDEKQ | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A0S8HCS0 | MRVGEQAQAAIAGGADVLHVDIMDGHFVPNLSMGPGFVRSAREFTDHPLDVHIMVTDALRFAEAFAEAGADSVTFHVEADCDPVKVIQLLRDRGLGVGMTLRPATPARAIQPFIESVDMVLVMTVEPGYGGQEFREDQLAKVRQVRSWLGAGRRVEVDGGISVQTAGACAEAGADVFVAGVNVFRSGDIAGAIAGLRSAAGAPRR | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 205
Sequence Mass (Da): 21596
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C3MHV7 | MAALELDLFLCRTDNFGVLIHDPASGATASIDAPEERPILEALERRGWRLTHILTTHHHGDHVAANVSLKQRFGVTIIGPKGEASKIPGIDKQVAHGERFDFAGHPVEVIETPGHTAGHISFHLPEDKLLFAADTLFALGCGRLFEGTAETMWQSLNRLMALPDDTSVYFGHEYTLSNAHFAVTIDPENAALKERAAEIEETRSDGGFTAPTTIGLEKRTNPFLRAGDSKIRAHLGMEKASDAAVFAEIRKRKDNF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
EC: 3.1.2.6
Catalytic Activity: an S-(2-hydrox... |
R6E6U2 | MTEQMKKKIEQFCIANDLLHKKDGIVVGVSGGADSVFLIYFLKEIMERWELRLHVVHINHGIRGKEALHDEQYTKELSKRFSIPCTIFRENIPKRATEWKMTEEEAGRTYRYQCFEKVRQELGFDAVAIAHHQNDQAETVLFQMLRGSSLRGLGGIRPKRGYIIRPLLLCNREEIENSLQEEHISYCTDQTNGQNDYTRNAIRNCIIPAMQKYIQPKAAQHIAKSGMYLQEVMEYLDRERDRIYERIVTQLQEEQINGYRIRRSDFVQLPSVMQKEIIMKLFEQTAGRKKDITTANVEETVKIFLGETGKKAMLPYHMIA... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A1V4QKM8 | MRISALRPGDHVGWLYHTAAEHRQVLQSFLRQGVERGEKVIYLRDNCPPEAVLGYLGQDDMAVAGYLQRGQLSIQEAVQVYCPEGRFAPETMIQWLQTQTDQALAQGYVALRVTGEMTWACRKLTGTAPVLEYEARLDQCLSDWACLTLCQYDRRYFEAAWLLEILTAHPLLIIGTEIFSNLYHSPRREVANPELAPVRLANRLYTVIRHKRSEQRLQESEEKYRNLFENAQVGIFRTRISDGKILEGNRRAAEMVGYKDFDQFIKEFVAAEHYINPADRDRMLASFQDGELKNFETRFYRKDGDIIWVLFSGRIYPERG... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A3C0X764 | MAARSFHALVTAMRIPFASLVLAGALCTPPVLALAAPPPAVLQVGSLRIGEGSPRTIVPITGASAELALQQAAAIAASTHTDLAEWRIDYLDIATDGSKLVALGKRIQATLGGKPMIVTFRTKAEGGAKAISDRDYGALYATLLRGGFAQLIDVEMFRDPNVVQALVAQAHKAGVKVVMSNHDFQATPPREEIVSRLLKQQAMGADVLKIAVMPRDAGDVLALLDATWQVRQRSDKPLLTMSMGGTGVVSRLAGETFGQALTFGMIGTPSAPGQVEVEQLQDVLQVIHASSQAGR | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DH... |
A0A2V1P0T8 | MKILVTGGAGYIGSHTLVVLLAAGHDVVVLDNFSNGSREALRRVQQLSNRDFNVVEGDVRDRSILDRLFADHEPAAVVHFAGLKAVGESVEDPLSYYDVNVGGSMRLLEAMSKASCKRIVFSSSATVYGTPEYLPYDEDHPTRPVNPYGRTKLAVEELLGDWCAASPSRCAISLRYFNPVGAHPSGRIGEDPKGIPNNLMPYIAQTAVGRRERLQIFGDDYDTRDGTGERDYIHVIDLAEAHVAALERLENMSAHTALNIGTGSGMTVKELIGCFENILGRKLPTSIAPRREGDLPSFYANPSRANEALDWKARRSPEDM... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 341
Sequence Mass (Da): 37464
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A0A8J5KJB4 | MLWHLVWLLEFKQLLGLLQTMVKSFEVTELPVRSAKFVARKQWVVAGADDMFIRVYNYNTMDKVKIFEAHTDYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWMCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTVKIWNLGSPDPNFTLDAHSKGVNCVDYFTGGDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHTHNVSAVCFHPELPIIITGSEDGTVRIWHATTYRQVNKVEGVAVMDEVEGVEAMDKGEGVRLENTLNYGLERVWAIGYMKGSRRVVIGYDEGTIMVKIGREVPVASMEGSGKIIWAKHNE... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
A0A0A1H9C1 | MKQMMNLPRRFLGLPAPAKLNLFLHVVGRRDDGYHELQSVFVPVDLCDTLDFVWRGDGQVVRSGDLTGPEDRDLAVRAARALQATIPGDARPGVEIRVEKRIPVGAGLGGGSSDAATTLIALNRLWGLGRSRDELAALALGLGADVPFFLGRGAAFVEGIGERCVPVAAPDVAYVIVFPGVPVATAGVFSDPKLTRDHKRTTISGFSAALSDPAAGLFGSNDLEAVVRRSVPPVNAALQALEQHGPARMSGSGSACFGVFRSLDAAQRVAGSLRDAVPPGQQWSVWAVPGLPEFALADW | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A7C6J0N4 | MKELMIYQEAVSAITQVINQGGYINIVVDETLGRISVSESERRLFTKLVYGTVENKILIDYYLRDYTKQKRLKPYLKNTLRMAVYGLLYLNMADHFIVNTAVEIVKKKDYKGSRLINGVLRAFLKNPLPDLTKLNRLEYLSIKYSFPRFIVELLLKQYPEKAETILNTLSEESQKALRINTLKGTTAEVEARLQTDGISYLIDGNVLYTNQSMINHQLFEEGLVTYQDPSSQLVSEIVDPKPNESILDACSAPGGKTAHMAALADNQAKIVAVDVHEHKLKLMEENFERLGVENVELILSDARSLGSLFAPRTFDKALVD... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 418
Sequence Mass (Da): 47442... |
F5LDX9 | MITKHTISILVNNQPGVLQRVSGLFGRRGYNIESITVGESEEAGLSRMVIVTEGDDNTLEQISKQLYKLIDVIKVIDLSKNPMVARELALIKVNSEPAQRPEILGIVDTFRAAVVDIGPSSLIVQTIGDSEKIDAMIELLRPYGIRELSRTGVTAMIRGAIK | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Cata... |
F8DYD1 | MASSPDSPGSPSSPSAPGTQSLHASSFATQVPELAQPWRSASFPDATLAITNDDLRNEVPVQDWDLAEGMEGWATAYSGHQFGHFNPVLGDGRALLLGETTNGREVQLKGSGPTPFSRGGDGFGTLGSMLREYIVSEIMHYAGIPTTRIAAVFRTGTEILRNGRPEPGGIAVRVASSHVRVGTFQFSRLLDEHESGKQQKDKGKATDPVLPRLVNYVLRTIVTDSSITDSSSTASSIAELSGPASIITHAVRTQASLVASWMKVGFVHGVMNTDNMSLAGETIDYGPCAFVDNFDPAAKFSSIDTAGRYAFGQQPTIAMW... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
EC: 2.7.7.108
Catalytic Activity: ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate
Sequence Length: 457
Sequence Mass (Da): 48748
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A0A173Z8J6 | MNKEIILTGDRPTGKLHLGHYIGSLKNRVKLQNTGKYESFIMIADQQALTDNARNPEKIRNSLIEVALDYLAVGIEPSKATIFVQSQIQELNELTMHYLNLVTVARLNRNPTVKEEIKLRDFKNSIPAGFLIYPVSQAADITAFKANLVPVGEDQLPMIEQTREIVRTFNSIYGDILVEPKAMVPEDTLGRLPGIDGKAKMSKSLGNAIYISDEADVVSKKIMSMYTDPNHIKVSDPGKVEGNTVFTYLDAFCKDKEAVCSMKEHYKQGGLGDVKVKRYLNEVLQAELEPIRKRRSEYEKDLDYVYKILREGSIKAREVA... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 337
Sequence Mass (Da): 38050
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A0A7C6CB48 | MRVVLVGNQNSGKSTLFNLLTKKHQKIANYPGATVDFMEGYTKDKSIHFTDLPGVFSLTPYSPEQEITLNYLLNQDYDLILNVIDVTQLERSLYLTTQLSDLDKPVVVALNMSDILKQNGENIHLETLEKRFGMSFIKISATKNDGIFDLLCLISSKDYLKHKHPLYPQEIETEITKIIPSLNTDNKRYYALKLLENHESFNDVIAESHANIASFTTDLYEYLAHHRYNFIEGLLKRAFVKLTKYDKRTAKIDKILLNKYLAIPIFLLIMFFIYTFSVGFIGSRSVDFMETSIDNLSNFLRTWLSGLNASSWSISLLVDG... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 648
Sequence Mass (Da): 73220
Location Topology: Multi-pass membrane protein
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A0A3A6NKP7 | MIRRPSNALHALILTLCLGVLLLAGCAKKAPPAPGEPGRPRGKPYQVWGTTYYPYLSARGFQETGLASWYGPTFHGRRTSNGERYDMEDMTAAHKLLPFNTFVQVTNQRTGQQAVVRINDRGPFVDGRVIDLSRAAARKLGVLGPGIAPVKLVAVGYQPQPSAVAQGPPARPPEIKLGPFTVQVGAFTVESNARRLAALLRSKHQEVQVVRYDRGDMIFQRVRVGKLDSLEEAQKLQARLREAGYKQAFVVAW | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 253
Sequence Mass (Da): 27841
Location Topology: Lipid-anchor
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D5EGI2 | MKNLLKRMDNVRLLLEKEAFPGMAVPGLIYADHYIETMLEQDSALEQVAHVACLPGIVGYSYAMPDIHWGYGFPIGGVAAFDVNEGIISPGGVGYDISCGVRLLSSYIKLADIKPVLDALTTALFSAVPSGVGSSSAIRLSLKDLDDVLRKGARWAVKEGMGMQDDLDRTEEGGCLDGALCEFVSSRAKERGKNQLGTLGSGNHFLEIQVVDEIFDKAAASQMNLESGSITVMIHCGSRGLGHQVCDDYLKVMRRAMAKYKIDVPDRQLCCAPIQSEEGQQYIGSMKAAANFAMANRQIIGSVVRDVFAQFFPGKPLFPV... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.-
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: 464
Sequence Mass (Da): 50457
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A0A354TWP8 | MNTKPVSRRKLFPHTDPRRAGRLRVSSLHELYWEDAGPVNGIPVLGLHGGPGGGASAEMRRFFDPRHYRVVLFDQRGCGRSSPYSSLEDNTTWDLIEDIEKLRKELGIEKWLVFGGSWGSTLSLAYAVTHPERVSGLLLRGIFLLTQRELRWFYQEGASHIFPDAYDRYIAPIPEDERDNLLEAFYKRLMSDDKQARLEAARAWACWGGEPPAI | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 214
Sequence Mass (Da): 24430
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A0A955LCL1 | MATLPLTYKDRDPILREEAKSVDAAWLRSEVGQQLVEDMIETMYHERGVGLAAPQIGESIRLIIVDPGHGRAEVIANPELEILNEKEDVGEEGCLSIPGNWGRVPRAKKLRVTGLDRNGNDISFVVKGFHARVYQHEVDHLNGTLIVDRFLSDD | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
D5EF20 | MGRILALDIGEKRIGMAVSDPLGCFAQGVGFIPMNKEWLLKLDESLISLNVEMLLIGNPLRTNGTAGPETDKIKNIAAELKIRYPHISIVLWDERFTTSIAQQVLLEGNVSRKKRKEKVDQLAAALILQNYLDHTRGV | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15366
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D5EFE5 | MQYTLSSDGKLNLTLRITEKRGDGYHNLVSLFLRLPAMESLTISTYKDNNVREIATTGHIVIDGKNIVEKTIECLESKGWSLPGLHVALAKQIPPGTGLGAGSGNAASFLRWARLFEGSEVTSDILEKIGSDVSFLYSRSFLSLVVGKGEKSACRGPLPPMQIVVAIPGWGVSTSLAYAGVDAFYGVDKGGSFPCNEWTGLAEVEKIYQSLLRGENVGFLPNDFYPWLAEQHPEYEAFFNECESSNALGYGLSGSGSSVFALFPANGKPVKLSQFEKMEWIQQILFWSDDR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
D5EF13 | MKIWFIGTGSFAAFCLEHLVSKCNMHFDRIITGMPKRGGRGMGERPSYVEETATKLNRSVFRTDKLSKDEELKRVLLESPPHCVIVVDFGQKVQEPFLSTPLWGCLNIHPSILPQYRGAAPIQRALMDGQKATGVTVFRLVEEMDAGPVLGQTQIEIGPDETSGDLFQRLAEEGSNLLKVVVKSCNEGTNITTLQNSKLVTYASKIEKRETQLSWSFDAQRFHNTVRALNPQPGAFIFYKKRRLKIWKTSVCEGTGKPGEVLGFIEGNPLVALQEGAVLLLEVQPEGRRVQSGSEWSRGIRLKKGDNFVE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A174IKK3 | MILVFGGAYNGKKDFIKEKFNINEEDIFYCSDGEIDFSKKVICGLHKFTYNNTLKNKSSLEYIKENINLFKDKIIISDEISSGIVPLKKEDRMWREETGRCLQYLSKESSCVYRVFCGISTIIKS | 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 = aden... |
A0A453ABG1 | EEFDYYADVCFKAFGDRVKYWTTFNEPNLFTRLAYVLGKYPPARCSAPFGTCESGNSHREPYVAAHNMLLSHAAAVHNYKKNYQATQGGSIGIVIAMKWYEPLTNTTEDILAARRALSFEVDWFLEPIFFGDYPREMHKLLSSNLPKFTSEEKSLLQKNKADFIGINHYTTIYVKDCISSPCDLKAYEAYEANALVLATGERDGVAIGRPVRTASI | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 216
Sequence Mass (Da): 24408
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A0A7C7ERW4 | MMTYRRLYNELKEKALAAGKEESAIKIILMETAGFTFTDLVMNFDSPVPAGILDRIIKNSDDYIENNIPVQYIFGVAYFYGMRLMVNGAVLIPRPETEVLVEIAIERLRSFKNPRTIDIGCGSGAIALALKKHLPGSEITAVDISEAALSVAKANAKALDLDIDFILSDLFSAVVGEYDAIVSNPPYLAGEEEAEPIVRDNEPPGALYAPDGGLHFYERIFREAPRHLKKPGLIVLEIPTDKREKITALATEAGLYRRIGVEKDLSGRDRVMIIEYE | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A7X7LSG0 | GSYPQGILGILVLAGIALVAFLGVFVCYFISGTIYIILNTKTDPKNMGKHRLYNEIGSYLFRVLLRVRIVASGLENLPKNNCFVAFANHSELSDPVYLKQILKDYPMAFLAKEELFHYPILKQLLISAGCIPLFRGMDRKGLQAIIDTIKAIKNGQPMGIFPEGTRSYSNQMIPFKAGAFKVALKAGADICPVCLYNMQGVLSLKRIRCHTAYIHVCPLIPYESIKEMDTSSLAQVVQERIQIQMDQFEAIYGQQPKAEGQGSC | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 264
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
S5ZXJ7 | MFFNYKLNAGILIFACLLDFILGDPYSFPHPVKLIGKLIRIEEKAARKICGSYGQGLRLSGFFIGLFNTAAAFCVIFFPLELIRAHRFIYFCTSVLICYTCIAARCMHKEAVKVFRSFKNGIKEARKQVSNIVGRDTENLDEEGVIRACVETVAENSGDGVIAPIFFIMFFGAAGGMAYKAINTMDSMLGYKNEKYSDLGFFPAKLDDAANYIPARLCALFMFISACLCFKSEFNLKNGFKIWRRDRLKHASPNAAHPESVAAGLLGVRLAGPNYYDGFLEEKPYIGDALKQIEKNDILKTVKLMYVSEILSVLLYALPC... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 323
Sequence Mass (Da): 36123
Location Topology: Multi-pass membrane protein
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A0A452XX74 | MMRQELIDAAEASGLSQYAIGPNNSRNSRNDGYSFTGWNSMKMLTNKDLVEKKSNPAKYYLTEKGKETARDCLARSRLDGPAGPLTAAGHPAVVLSDSDSDEYDGSSPLIGINKGSERSGLPNSKAGSSSSFDNGHATNSPLSSRGMFGQQSFSAMSSAEMSLLAMPSHQSNESFLKAYEVVLILDDRDTFGPRSRRKVVDNIRSQFNIPVEVKHLPVGDALWIARHKELDTDYVLDFIVERKNVEDLLGSIKDNRYKDQKLRLKKCGLRKLIYLVEGDVNTVDGSESVKTACFTTEVLGGFDVQRTTGYADTEKKYGHL... | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A7X8X197 | MIIVYGGTFNPPTVAHQLIANKVIENFKPKKFILLPVGENYPWKSFYVPFKQRFEMLKLAFNDEIFEISTLENKKTYKGTYFALKRLKKTYKSSVYFLLGADNLSYLNEWINYESLIKEFQFIVIKRKGFNLEEIIKKYHPYEEKFHILEMDLEISSSLYRNNPKEYEHFIPVDVLKYINENELYEV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A7X8WHB4 | MTIKGTISRIQYHNPANGYTVAVIELAPDEYKTAREKSRLIGNNITVVGVFDRTVFPEEEYEFEGNFVNSPRYGMQFQFTSFTRLEQTNEQGVINYLSSELFPGIGLLTAKSLVEALGVKAVEKIQEDETVLDSLKLSKAQKKSLIEGIRNNANTQAMMLFLMNNGITIDMAHKIIATLGSDALEKIKAMPYCLMQAVPRFGFKKNDAFALRIGVEKTAPVRIKAVIQYVLNDWIFNSGNSYIETQELFRLVNKYLNDELDYNLYRQMIEELSKEGIIILHRNNFVFDAQLYQQEITLAKQVARRIKNEQQRIESFDINQ... | 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: 772
Sequence Mass (Da): 87745
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A0A7X7LQD4 | MKQLLIASNNFNKIREFKEILANSPFKLLTCADLNAHLDIEETGMTFRENALIKAKAFYDRFRIPTIADDSGLEVIALGNRPGVFSQRYSPSGTDEDNLALLLKEMHGVEDRRAQYVCELVYYQSPETVVFFSGILKGQIMDKPISGNGFGYDPVFYIPSLKKRLSQCRPEEKNAISHRGQAIRQLLDLLRSHS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A453B9Y9 | MYAKFIDWDEEIYDQETDTPAHAANTAISEDLGQVEYILTDKTGTLTENKMIFRRCCIAGTLYGNESGDALKDIELLNAVADNSPHVIKFLTVMALCNTVIPIKSPSGTISYKAQSQDEDALVNAASNLHVVLVSKNGNNAEIHFNRRVIQYEILDILEFTSDRKRMSIVISDSQSGKIFLLSKGADEAILPLAYCGQQIKTFVDAVDKYAQLGLRTLCLGWRELSLEEYLEWSRLFKEANSALVDREWKVAEVCQKLEHTLDILGISAIEDRLQDGVPETIEILRQSGINFWMLTGDKQSTAIQIALLCNLISSEPKGQ... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 576
Sequence Mass (Da): 64303
Location Topology: Multi-pass membrane protein
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A0A345RGJ4 | MNEPNFKPIGLSIRDMTQHEPRFLPDPNGPAEQTTAPFRADFRTLLLTLWRGKMIISAASVVAVLLTTYYVFAVATALYTSSVVVIFDTRQTSVVALPSVIAAVSGEPSSVTSEVEVLRARTLMTDVARHLHLMSDPEFNADLREPGLKTRLRSGIESVLGGGQSFGPPATDDDRTGRDLDRIVNVLLSKVSVRNIPGSHVFRISVTTQSPEKSAIIADTIARLYIDNQMNEKQHATEHAAKWLASRVAELQSQLEDAEAQVAQFTAATALISAPALQVLERQLKELRARIAAAHTRKAKMQGLLGKMVDAQTPHDKVAV... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 729
Sequence Mass (Da): 79591
Location Topology: Multi-pass membrane protein
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A0A7G6E0J1 | MFYKVIHALVSFYLRLFNRWEITGEENIPKSGPVVLVANHISLWDPPFLACSIRRPVHFMAKEELFKIPILGRIIKALGAFPVKRGKPDRNALRLAAKYLEKGEILGLFPEGTRSKSGELLQPHPGAALFALRSGAPIVPVGLIGTRTTFPLTIRGNVRVKIGKPVVYPGLYNNKITNEDLERVSAEIMLKVKKLLEEK | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 199
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A5R9BVN6 | MTDQKNSARNIAVNILEKVDDGSFSNIQLNQDIKNSNLIDVDKNLLTELVYGVLQHRLTLDYYLSDFVRKPELTPRWVINLLRTAIFQMEFLDRIPDFAIFNESIEIAKLRGNDGIRKMVTGVLRSYQRNGKPDFSRIQNPVERLSVQYSVALWIVDQLSYELGVEKCTSILESVNQPANLSVRVNRWNKSHADIIKDLEYDYQVTSSKIAQDGLKLSKGPSISESRSYIDGDITVQDESAMLVAETMQLEPDQVVLDACAAPGGKTTQIAEKIGQNGKVLAWDVYDSRVKLITQNAQRMHLTNIDAEVQDAEKARPDLN... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 444
Sequence Mass (Da): 50340... |
A0A1V2M5Y5 | MNYSKKIREDNDDEKMSSRELKRAGLIGFKVFLVGLLIGAFGVCGVGLAWLLKIIKDAPDVSKLELKPKYNYTTFIYDIYGNEIDRLTSNKGEARIYATLDEIPYYLQKAIVAIEDARFYQHNGVDIKGVMRAIVVNLQEGDIVEGASTITQQLIKNNILGDDKTFKRKIQEMYLALQFDKIYEKDLILEYYLNTLALGHGMNGVQAASDRYFKKDVSDLTLAECVVLAGITQSPTAFSPINHPEANWAKAKLILSNMVEQGYITEAERQEALLEDPYKGIPDINEAYIETKVSPHTSFVDAVIDAVLRDFVEEGGMTTI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A6L5XFZ8 | MAKAKILTDLEESYNELVHKVSWPSKTDLANSTVIVMVASILMALVIWAVDAIISWGMENIIYRV | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 65
Sequence Mass (Da): 7293
Location Topology: Single-pass membrane protein
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A0A1F4XKY6 | MSISLEEVRHVARLARLKLTADEEARFAPQLANIIDYLGMLQELNTDNVPTTSQVTGLTNVTRADIISCAPRQDELLACSPLPKEDHQLLVPSVFS | 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 ... |
A0A7G6E4T9 | MSILVTGGAGYIGSHTVRKLTDIGYNVIVYDSLEKSHKESVKDIPLIVGNILDEQLLDSTMKKYNIQSVIHFAAYSLVGESMAEPEKYYVNNVCGTVNLLKVMLNNNIKRIVFSSTAAVYGEPQEIPITENSPKNPTNVYGKTKLMIEEILKDYDLAYGLKYISLRYFNACGADESGEIGEDHTPETHLMPLVLQSALGKLPEIRIFGTDYPTPDGTCIRDYIHVNDLAEAHILALEKLLADGQSAVYNLGNGNGFSVREVIRAAEEVVGKPIKVVEGERRPGDPAVLVASAEKIKRELGWQPKYQGLKEIIETAWKWHQ... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 332
Sequence Mass (Da): 36913
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F5LC06 | RVTVALTRKGISEVDRYDPAEIQAKYGLVPAQIIDLKGLMGDSSDNIPGIPGVGEKTALKLLHEYGSVESVLEHADEMKGKMKEKVRDHADSARMSKEIATIYREVPMDTDWSSLAFSGFETPELAAMFRKLEFKSLLERLDFSGAGGTDSPEGAEPGPAEELVVRLIDADNITDLTGALKDVSALHVEAVGDNAHTAELVGAAFHTPEAGYYVPAGVLTAPGAEALHAWLADERAPKSTWDRHRAELVLAWNGITLAGVAFDVMLAAYLLDPTESSLTLSGIADKYGALHVAPDEAVFGKGAKFRLPETEAVAEHLVRK... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 746
Sequence Mass (Da): 82871
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A0A016QK03 | MRWPPLGLIAALLALEGLLKAWAAANLTPGVDRVLLPGLLHLGFTLNPGMAWGLLGGFTAPLALLRLIVGLVIVAALLSGRLPRARRWPLALIAAGALGNAVDGLARGAVVDYLTSPLLDVVTLPLTGRPFPIFNLSDVLVCTGTLWLLLHAWQAERRAGHSASDRRATSQPKENP | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A8I6S3Z7 | MESLVQGTNDSSIVSKLSMVQRGYFEDEFLQYFVMKPTRRAPLINIGYFVRSLVVQTAVKYYLDSNYKQVLSLGAGFDTTYFRIVHNYEGVTHFEIDFVDVVKNKISCVQACDKLKQMLTNIQEIADPVGVTSDRYNIFAQDLSDVQMVERHLMKCGFDFEKPTIIFSECAITYMEENRSTELIRWSAHKFKNVVFLNYEQINPDDGFGQVMKRHFIKIQNPLKSLDTYKTPESQEERYLKCGWEHSRSVTAMVIFNRLLHHEKQRQIFNLEPFDEWEEWHLKCSHYTLSIAINGCCNYPQFLTKSQTKKGAEKHLNVET... | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 2.1.1.290
Catalytic Activity: 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-homocysteine + wybutosine(37) in tRNA(Phe)
Sequence Length: 644
Sequence Mass (Da): 73796
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A0A453GM75 | QARALSAAYSGVCTAKEPVRTAGDLARLKGVGGWVVDVMKDCFPGSSLDLSPPRSNTPGETGKKRKRNKPYVPQLNSAAYAIVITLYREMIRGTEVMKKQELIDAAEASGLSRKAIGPNNYKSKHGNSGSDFYTGWSCMKNLTEKDLVVKKSNPAKYYLTEKGKETARICLAKSGLDDPAGPFMATGHPESVMLSDSDSDEQEGSSPLIGSENFSERSGLPNSKAGNSSSFPTSMLSLQIILCSINKILLSTDIFS | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A1H8U091 | MTHSKRFAPWLLAAAFALVLAGCATPGEDEERVEDQDDELTEEEMAALDEEERREAEARAARERGALEGEALEAALDDPDSPISDRVVYFAFDSSDIRDEDMEILEAHGEFLSDHPNQEVTIEGHTDERGAREYNLALGERRAESVKRILVLSGASEDQLEVVSYGEESPVASGSDEEAYQQNRRAELVY | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 190
Sequence Mass (Da): 21162
Location Topology: Lipid-anchor
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A0A2X0VQJ1 | MQQAQGTLSFTELIFNASFLVQLVMLFLLILSLVSWTIIIQRSNQYKIAKRQAMEFEDRFWSGIDLNNLYQDCIKRQDSLIGLEVIYAAGFKEFVRLVNSGPADQEVVMDGTYRQMKVASSREVEALESHLPTLATIGSISPYIGLFGTVWGIMHAFVALAAVKNATLNMVAPPIAEALIATAMGLFAAIPAVMFYNRFVTKVEALENTYLNFMDEFSTILNRRLVTIRSQLLKNDKDGGQSAAHHQNVHGTAAAPVKTRAAMTQSTMSEGTVPQRTMSQSSMSQSSITHNTMAQSTARQELSGHTGAGHSQSAAQTAVK... | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell inner membrane
Sequence Length: 425
Sequence Mass (Da): 45917
Location Topology: Multi-pass membrane protein
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A0A7X8VTW2 | MNEQILVRYGDLILKGKNQKHFIKTANERVREKLSGLMVDFDFRHDRFYVILNNTPAKEVFDRLCLIPGLYSFSLVTKTTTVYHEIASQAVSLIKEQTKGKATSFKVETKRADKSLKDTSTEISQQISKMILPNVPNLTVDVHDPELTLNLDFRRDGCYMYIGQIMGLGGFPIPVSGKVVTLLSGGIDSPVAAYLAMKKGMETELVHFESTPLTSIEAVQKVLDIASELAKFAPRDRIRLHLVPFAELHQEILNKVPESYLITIMRRMMLRISTRIMRQKEAMAIVTGDSIGQVASQTLESLVAIQDVTDALILRPLSHL... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarb... |
A0A453QBM9 | IISSSNYLPLLHSCLSAVSAPATLLLTSLSVLLIRRVVRKYRKRVCRLDRMASSKLQAFWNHPAGPKTIHFWAPTFKWGISIANVADFAKPHEKISYPQQVVIACTGIIWSRYSMVITPRNWNLFSVSVAMSGTGLYQLSRKMRKDYFSGAEKEAAAASLELEV | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 164
Sequence Mass (Da): 18403
Location Topology: Multi-pass membrane protein
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A0A452Y4H5 | GAGGQGCQICGDTVGVSASGDVFVACNECAFPVCRPCYEYERKDGVKCCPQCKTRYKRLKGSPRVPGDEEEEDVDDLDNEFNYKQGNGKGPEWQLRGQGEDIDLSSSSRHEPHHRIPRLTSGQQISGEIPDASPDRHSIRSPTSSYVDPSVPVPVRIVDPSKDLNSYGLNSVDWKERVESWRVKQDKNMMQVTNKYPDARGGGGDMEGTGSNGEDMQMVDDARLPLSRIVPIPANQLNLYRIVIILRLIILCFFFQYRVTHPVRDAYGLWLVSVICEIWFALSWLLDQFPKWYPINRETYLDRLALRYDREGEPSQLCPI... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Glycan metabolism; plant cellulose biosynthesis.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
EC: 2.4.1.12
Subcellular Location: Cell membrane
Sequence Length: 608
Sequence Mass (Da): 68902
Location... |
A0A160PVV6 | MTTPDRIKSTQIALDRDLREQAILLLKEVRAVDGVDALSEQFVRGLAEPGLGHSHLIVTLNEKIVGLAATDDETTELAVHPAHRRQGIGKALIDATPTSSIWAHGNTQAAQALASTLRMKKTRELLVMAIEGPALEESAVYKDPEGITHSSLANAPMEKSAAEAKWLQANNEAFDWHPEQGGWNTHRLAQAQKADWYQDSDVLFLWDGEEIVGFHWVKQHSVELQEIYVVGLASAYRGRGLGDPLMRLGLHHMRGQGARKVILYVEADNAPAVAAYEKLGFTVAERHVVYEK | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
EC: 2.3.1.189
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Length: 292
Sequence Mass (Da): 32232
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A0A970DJV9 | MRYKCTCRYDGALFHGFQIQKNARSVQEEIERALLLIFKKPTRIHPAGRTDAGVHALGQVFHFDADLEIKTSSLIRAMNSRLPEDVHITAVERANDDFHARYSAKSKEYHYILDFGTYNPLFRNYRHYYRYPRVDYRLFEEAMLLFVGRHDFRYFSRSKAAENTTREIYRVGFEWEGSAVKVIIVGNGFLHNMIRIIIATALEVARGKKTLDDIRKSLAGKAPLPAPKKLPPNGLYLVKIDY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 242
Sequence Mass (Da): 28105
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A0A7S3CWI0 | MSVNLKERDWLDACYRGDVEKVLELVQTNDKELINTRVSSETAGFLAPRATASDLHILIGSSGIHLAALSGRRVMVALLQRLGASVWTKNACDWTPLHFAIFGWHIELCRDIFEYPESIPEKDDLKTSSFHSTGNDNSEEREAEDSGKKIESKISQLEGPFHFDERGVGPTVFDLLLRGCKKRGENEMNALLFCLIHYLPNDPIFAPLVEFSDLLNDKGRPVNVSESSIEHKGAAEIARARHLGQSETSHSYRARAYPLHYVFRSITLSDMQPDVLTRTPSEIEGMPNNDSEKKGQSEKTSSPEFDGVTDYGKASAKPIV... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 617
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 69805
Location Topology: Multi-pass membrane protein
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A0A1H9NYV9 | MAECNVKTLQEVLRWASSFLREQINYTEEDSLVIAKRLICHVKDWSMSTLYCHLSDVYENYQEELLPYLKQLELGLPLQYVMGYEEFFGRNFMVSEATLIPRPETEELVQLALDYLAGKSSQQVVEIGVGTGCIIETLALECPDNLYLGVDLSAEALAIAEKNRQQFELTNLMLKESDVFSGVPVVTEGYDLVISNPPYISEDETSVMDQQVIDFEPHMALFAEEDGLLIYRQIAEQLESYLKPTGIALFEIGFQQGESVKQLFQKHTTKRHVEVVKDLAGLDRMIKVSEKKN | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A8H5FVD6 | MLSNFSKTFFESILLLWLNIPTIRPFPDKSINHTNLLTDHETALSAVRNLNNVDVGGRPLRIDLADSDPFLEGKTTVRGELVDGGVPGPAEPRHRGGGGRGHDGDFMSHLPPGVHLPKGTDSLDYITKTLAGMPPSQLMEVLAQMKAFIITHHEQARQLLVKHPQLSYALFQGLLLNNIVDPAILYRMLEQTGNQSSSGTSATPPRAPPVPPPPQMSQPPFVPPSTHMPFQAQPPMAGMPPPSSLPPASAMFPPTGAAYYRPPPPTGASPASMQAPPAPTAPQPPAATGTPAINESQRAMLMQVLALTPEQINGLPENDR... | Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Nucleus
Sequence Length: 1022
Sequence Mass (Da): 114413
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A0A3C0GRP1 | MSATQAAPARDRLRIAIQKSGRLAEPARNLLSACGLSWRESRDKLFCYGESLPVDLLLVRDDDIPGLIADGVCDFGIVGRNELDEQGAARRRIGLPDAYQALRGLNFGQCRLMLAVPEEWQWTGVEQLAGKRIATS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosyn... |
A0A2X0V5V5 | MKLKRFVAKDMREALVKIKDELGPDAVIMSNKRIDDGVEIVAGVSTINDSLTQKVKQVQRNDMLKDRESLEQILKMAKARRESRKVLADDSVSISSAGATRALDDINASLESLKNARQQDVSEEDNSLDAFLDSVRNAPNVKNDRTDKFANSLVEILERQQNDAKKTADGAASQKTVAGSPFQEPPPSLSENSEFDSLFKKSRTKLEKEQHENESGIDTYRDKNPQIDDTNIQAVAEEVQVIRKLLQFELAGLMQESRNRQEPVRAMIERLLVSAGFDQDLSSELVSKVSVDASFNFAWRELSDILEKKIIVGNDEIVKQ... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 527
Sequence Mass (Da): 58505
Location Topology: Peripheral membrane protein
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A0A847YHV6 | MVVGIGIDLVEIHRMKRAVENPLFVKRVFTPAEQAYCTSRGRQGAASYAARFAAKEAVMKALGTGLANGGTWQDVEVLPDAQGKPVMSLTGYFENLAREMGVQRIFVSLSHAQEYAVAQVLLWRGEQE | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 128
Sequence Mass (Da): 14057
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A0A954B4Z9 | MTKINRFCAARRDLELMDPHLLPFAERQAPRYTSYPSANHFDASVDAEIYRRWLGAVDDTTNLSLYLHVPYCRQLCWYCGCNTFLTRGGDIGDFVTTLMMEIDLVASALGARTVAEVHWGGGTPNVLSAAEFLRIVHHIDFWFDVRPDLRHAVELDPRYVTTELAHAYAAAGVGRVSLGVQDFNAHVQEAMGRVQPFEQVRESVRMLRDAGLETISFDLMYGLPRQTAGDLARSIRLAAELKPSRIALFGYAHVPWFKRRQRLIDAKALPGASERFDQAELATRMLNDLGYLSIGLDHFARSHDPLATAAREGKLHRNFQ... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Catalytic Activity: coproporphyrinog... |
U7UKU7 | MKLKKLAAITLSLLMIGSIATGCGKKENKPANTNSKPANTEQKNDKKDSEKKTSDISGSLTASGSSALLPLCQDAADKFKESYPNISVTLNAGGSGTGLKQVADGSVDIGNSDVFAEEKLDAAVAKDLVDHKVCTITMAPIVNNDIASQVKDLTKQQLIDVFTGKIANWKELGGPDEKILLVTRPDSSGTRALFTKYALDGNQESSTASYLETDNSGELLETVKTNKGAIGYVALSYLVNNKDVAPISIDGVAPTLENTYSGEYPVWGYEHMYTKGEPSEAAKAFIDFMMSDDYAQNMEAQGYGVASKMKVDR | Function: Involved in the system for phosphate transport across the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 313
Sequence Mass (Da): 33434
Location Topology: Lipid-anchor
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A0A6L5XAW0 | MPGSKIIIKLKNTTMMKLYKFHGAGNDFLIADARRDTVNLSQEEIVHLCDRHTGFGSDGLMVIGNSNDTAFKMKFYNPDGTSGMMCGNGGRCISAYAAMTSANDERHFVFEAPDGLHESWIEAGPETDALGDCTRVVRLKMSDVKEFKKYDDTSYFFNTGARHFVTAVDDVDHTNVYANGRAYRYFDTRFAPEGVNVDFVQVRDGVLHVRTYEKGVENETLACGTGIVATALAAYMMGVQPESVENGVVRYAVQARISLLHVEFEPEKKASGNITFNNIYLTGPATYVGEIEVDL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
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