ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A3L8RMI5 | METPHEPYGPHEPYGPHEEVSGRRPWVVGVSGASGTPYAASVLRALLAAGEAVDLVVSRASRLTLLDETGIGFRDAHWRDDLCRWLARGADGTPDAFEVPAEVADVSHWAPGDLAAGPSSGSYPAKGMLIVPASTACVAGVALGLSKDLLQRAASVTLKERRKLVVAVRETPLSGQTLKALVTLDEAGAVVLPASPAFYAGATHIQDLVDFVAGRVLDAAGVPHKLYRRWEGELGGDRDRGAA | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
A0A497SP54 | MSKNEIYIQILKQEENLMEFIIRNISSAFANTLRRIILSEIPILAIDEVVFLENTSVMFDEMLAHRLAMIPLKIDLASYEYFYECWLEGKADNCIVVFKMEVEASDKPTTVFSGHLELIKPAYEDLLKLPLKIEPVSESIPIVKLAPGQRVSLEAYAKLGTAKEHAKWQSVATVYYRNLAKIIIKQEKCDKSCEECVKVCPHNVLEFRNGKIIVINELACDTCRACMEACPDIIEVDWDKNSFLFTIEGIGVLPVSYILNIALNLLERRLIRFKERFNEIKL | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Cytoplasm
Sequ... |
A0A1C3JTC9 | MSKPKVVCLMGPTASGKTGLAVELASQHGYDIISVDSALVYKGMDIGTAKPDAETLAKAPHRLIDIIEPTESYSAADFLSDVQREVEDIVAQGKTPLLVGGTMMYFNALQKGLAPMPSADPAIRAEFDQHAAKFGLASLHEQLKEIDPVAAARINPNDSQRLQRALEVYRLTGKTMTQLWAEQEAQELPFELVNIAVMPQERSVLHQRIEQRFHIMMEQGFLAEVEGLHQRGDLTIEMPSVRCVGYRQLWQYLEGEDTLDEAVFKGVVATRQLAKRQHTWLRGWDDLVIFDSLHKDLLGQTLKYLESEII | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
I0HSA7 | MKFRSTLAQLRAFDPPAALRDTTRPLLNLALNENSLGSSPAVAAAVAAALPQLHRYPPTFSDALRQALARRHGVAADRFLVGNGIFELLGLITQAFVAEGDEVVIPTPSFGWYAISARAAGARIVAVPLAAHAIDLDAVAAAVTPATRLVWLCNPHNPMGSLVAAGAIRRLLERLPADVAVVLDEAYAEYARPADLPDSAHWIDEHPNLIVLRTFSKAFGLAGLRVGYAIASPPAVRELGKLKSPPNVNSLAQVAALAALGDEDFLRRSVATVHEAARAYPGFCASRGLGYVPTHANFVMIDLGQDGDAAATEFLRQGIV... | 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: 363
Sequence Mass (Da): 38649
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A0A2M7NX67 | MKDFEFTSESVGDGHPDKVCDRISDGVLDAILKYDEKKGLKPYKMKDGDARGSRCACETFISLGLVIVGGEITTDAWVDVRAIVKQALIEIGYTGSEYGFDYRTCAILNVIGAQSPDIAQGVDCGGAGDQGIMFGYACDETENLMPAPLEFSHALVRKFKEVRASKEIPYLGPDCKSQVTVKYVDDKPVKITKVVVSSQHTSEVVEQKGARRVMKQLAREEIIEKVLKASLPADLLKGLDFKKDCFVNPTGIFLVGGPQSDTGVTGRKIIVDTYGGMIPHGGGAFSGKDPSKVDRSASYAARYVAKNIVAAGLAKKCILE... | Cofactor: Binds 1 potassium ion per subunit.
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequenti... |
A0A1H5EJV1 | MPHHNDPKMLQLLKPEEREIERADYVSPDQMFAAALGFVRRQYPIFLVTMLITLALGAAYLVITRSTYTAQATIIIDTRKLQPYSSQNSLFTEVPVDSPAVDSQLELIKSDNIARSVIRDLHLAQEPEFSRYGGGFVGNLLYYFYQLFEPGDESQDEIERRALREFSNNLSAKRVGVTYVIEISYRSALPERAAQVANAVAEAYINDQLDAKYQSARRAGDWLSTRIQELKQQAISADRSIVDFKSKNNIVDAGGRSISEQQVAELNSQLLAARTVTADARARLDRIEQVMKSDVRDATVTDTLRSDVVSKLRTQYLDIA... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 753
Sequence Mass (Da): 83255
Location Topology: Multi-pass membrane protein
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A0A497SIH4 | MNFFPYALREKQEEFISFVNKNVMKNVICVEAPTGFGKTPALLAALLPYVLDGYRVIWTVKTGNETDRPIEELKEINKKLGTNFFGLSYRGKKDMCLLARERKLKTDYDGATFFCNMKRKECKYYANLAGVDIDMFLEKPLLYTELVGICKNLNLCPYFLQRILAEFASVLSLSYNYIVNEGIAWGIKSLIPFKNSILIVDEAHNLQFITSNVNSNRITTRTAINALKEWREFVGDDGREKLFITSLIEEMRGIYKYMKESNECEIRLNMDEFLSKVLAKEGLGFDEMFEILSKIKKVGTELRRQQIEANKSPRSSLYRL... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 630
Sequence Mass (Da): 72285
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A0A6I5X4J3 | MSTALYRRYRPESFADVIGQEHVTEPLMQALRTGRVNHAYLFSGPRGCGKTTSARILARCLNCEQGPTPTPCGTCDSCVALARGGTGSVDVIEIDAASHGGVDDARDLRERASYGPAQSRFKIYIIDEAHMVTPQGFNALLKIVEEPPEHVKFVFATTEPDKVIGTIRSRTHHYPFRLVPPGQLTDYMQRLCESEGVAVAPGVLSFVTRAGGGSVRDSLSVLDQLIAGSDDEGLTYESAAALLGFTDGELLDAIIDAFAAGDAAGVFHQVDRVIETGLDPRRFVEDLLERLRDLIVVAAVPDGASSVLRGVPEDQLERMR... | 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: 691
Seq... |
Q8D3A8 | MSYYLYCIRSKYKMKKKINKILYLLILIPIFFFRLFIFERESLHINNNALITIKKGSTILDLKNLMEEKTFNNHLYLLPWLIKLYPKYKYIKAGTYFLKTEYNIKDALNIFVLGKEKQFSITFFEGSTLQDCLIILKNSPYIEQDLINVNIYNLSEKLGYKYKFPLEGSLYPDTYLYVKNTKASEILKRAKRNMDVILEKIWDNREYDLPYKNSQSLLIMASIIEKETSIKKERAIVASVFVNRLKNKMKLQSDPTVMYGLRNKKTINHNDLTIPTKYNTYIINGLPPTPISMPGFESIYAAAHPKKSNYFYFVSNGYGS... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 348
Sequence Mass (Da): 41125
Location Topology: Single-pass membrane protein
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A0A4P8DN95 | MITSQIMVLTLMGLSMILITTALSISKKNNQDLEKNSQFECGFNPLTHTQVSFSLQFFIITIIFLIFDVEIALLLPSLLSISETPSLLWIMLMTLFIIILTLGTMYEWKDNMLSWK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A1C3JSX0 | MVEQAQFSKALLHPKHWILWLGIGLGRLVSMLPLNWQMGIGKGIGRLMMKFAKGRVHTARRNLELCFPDATAEEHQQLLERNFEETGKAIFDTVSAWWWSDSRVQRHMDITGQEHVQRTLESGQGVILFAVHCLPLEMGARIFGQFNPGIGVYRPHNNPVMEYLQVKGRLRSNKALIPKRDVRQMVRSLRAPDVIWYTADQDFGRSSAVFIPFFEMPEAATITGGTMLAKLGKAKVLPFFVERNADDKGYSIKISEPLGDFPGESELADAIRGNHIIEDLISRNKAQYMWLHRRFKTRPNQDEPSLYSK | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Function: Catalyzes the transfer of an acyl chain from an acyl-[acyl-carrier-protein] (ACP) to a Kdo(2)-lipid IV(A) to form a Kdo(2)-(acyl)-lipid IV(A).
Catalytic Activity: a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA ... |
A0A257GQY3 | MRLFDEIRRIGQTAGYSLAGWQHAWRAEKSLRQWAYVNLAAWVALIALRPPLWACAMIVAQGLLLLAFELINSAIEATIDYISTARHPLAKAAKDTGSAAVAVMGLAYIATWVFVLLALF | Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosp... |
A0A7V4QCL6 | MKRVVVKVGSAVLTKGGIINKERFSNLVSFVAAISQKYQTILVTSGAIATGATVLPNISNKTTAGKQALAAVGQAKLINNYQEEFKNFGITVAQILLTADDFDSIRHSENALNAVNFLLDNGVLPIVNENDSVIVDEILRGDNDSLSAQVAHYFDADILVILSDIKGYYDKDPNKYPNANLQKVVSELSIGELEQEHSPNDAFATGGIVTKLRAANYLLSNDKMMFLASGFELDGAKDFLLNGVHNSGTLFSKE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
EC: 2.7.2.11
Subcellular Location: Cyt... |
A0A972VUA4 | ILGPDISHRRTLIQSMMSSDAVRAAIEKEARHKPSAINKIEKKALDYANEIASHQSYRVIRFFHAILTWLWNKLYDGVEINNINQVKELARNNEIVYVPCHRSHIDYLLLSYVLYHNGLSPPHIAAGKNLNMPVVGPLLRRAGAFFMRRTFQGDALYKAVFDEYLHLMFTRGYSVEYFIEGSRSRTGRSLQPRTGMLSMTMRSFQRDASKPICFMPVYFGYEKILEDTTYLDELSGAAKNDESIMDIFRVLGSLKNAFGKVTVNFGEPVHLRAFFDQHLDNWQQVESVDPADFARTCSLLATRLSQGINAAAAINPVSLV... | Pathway: Lipid metabolism.
EC: 2.3.1.15
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Sequence Length: 617
Sequence Mass (Da): 69311
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A0A1L8QT77 | MAKVTSNLLVIHGGGPTAVLNASLYGVITKASQSEKIHKIYGAKNGTGGLLREELLDLTNRTPEMLNTLLTSPGTAIGTSRDALEEKDYRKMIAILKKFEIKYVLFNGGNGTMDTCGKLFQLCQKEAVDIQVIGIPKTMDNDIGVTDHCPGYASAARYIAQSVKEVCCDVKSLATRIVIIEASGRNAGWVAAASALADESGVYAPELIYLPEVPFDENRFLADVKQKLQVKKGFVIVVSEGLRDATGKPIGQSGEHSTGRAAQFGGVSFYLADLITQKVGYRARAEKPGLLGRASIALQSEVDVKEAILVGVEAVQAITQ... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-depe... |
A0A8T4KN34 | MSHVLIITEKPSASRAVSEALADSGTLKKFGDRAFWYEFMKGNEKYVVAPAVGHLFALKQASKGWTYPVFDVKWIPSFEASKTAEFSRIYYENLTNATKDAKDVIIATDYDDEGEVIGYNILKFICGMKNAQRMKFSTMTHEELIDSFEHPIKLDKKLIEAGITRHMLDWYFGINFTRALTLSIKNASQRFKILSTGRVQGPVLHMLAKHEKKIRAFKSKPFWELKLKLKIGQQEFEADYEKDKLWNKKEAESLRKKADVKSGIVKDITIKIYNQQPPVPYNTTALLADISRYFGYTPQQGLNIAENLYQSGYISYPRTA... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
V5WGL4 | MLFHGADLYINPEVNTMKNLSKKNHALFRLPRLMVIAVCLLLAPALFASGGEESRESDSGQHRAPEVDYMKDIPENHEIATLGGGCFWCVEAVYEPIEGVYGAVSGYAGGELENPSYQQISTGRTGHAEVVQLYYDPEKISYEQVLKLFFKAHNPTTPDRQGLDVGPQYRSIILTHDDSQAETARKVMKEAQEDWPDPIVTEIEPLTAFYPAEEYHQDFYEKNPNYGYCAAVIRPKMEKLGLEGEDKINVLELDL | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A0A0NP89 | MGDGTGIQHGRRHGDQHGSQHGSQHVSQHVSQPGHEQGIERARKTAEELVYASGFGNEHSSEAVPGALPIGRNSPQRAPLGLYAEQLSGSAFTEPRATNRRSWLYRIRPSAAHPPFTRVAGGALRGAPFTEAAPDPNRLRWDPLPEPPEGTDFLAGLWTLGGNGDATQRAGMAIHLYAANAPMTDRVFSDADGELLIVPERGGLLLHTEFGLLRAEPGHVALIPRGVRFRVEPLEPSVRGYVCENYGRPFTLPDLGPIGANGLANPRDFLAPVAAYEDVERPVEVVNKFCGNLWAATYDHSPLDVVAWHGTHVPYVYDLR... | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6.
Function: Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring... |
A0A3P3E1D2 | MNVSWYDQSRFIPSHGRNLDRMVFVGTCVAALVASSILALITLFLISESWPFLSDVGVLRLLSDEEWAPKGDVFGLAPMLVSSVLLTIGALLLTTPFSIGFAVYCSFYSRKHIAAGLLRLVDISAGIPTVIYGFWGLVVVVPIINSIAPPGASILAGILVLSLMIFPTITVITQAAIEAVPKTYIYASTALGVGRAATIRHIVFRQARAGVLAAMTLGAARAIGETIVVLMVCGNVVQMPSSFFDPVRTLTANIALEMQYAMGLHQAALYATGLTVLMVVALLVLLSGLYAQRQAREDS | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 299
Sequence Mass (Da): 31903
Location Topology: Multi-pass membrane protein
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A0A0G2B6S1 | MSEISNGVNLPILYEDADVVAVNKPAGLVTHSDGRTTEPSVAEWALEQYPALREVGEPWVSPQGETISRPGIVHRLDRGTSGVMILAKTNEAYAFLKKQFEDRSTEKRYRALVYGHPRKDAGVIEAEIVRIRSIPPRWGVARATEKRKHRAAITEWQVLSRGADPITGEKISYLEAHPKTGRTHQIRVHLKHLGHPVICDPLYARGRPCLFGFTRPALHAESLSITIPSGERRTFEAPLPDDFKRALAQHQI | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 252
Sequence Mass (Da): 28211
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A0A0L6TVX7 | MNNYYILAINPGSMSTKIGVFENENEVFTASVEHQSRDLETFPTINAQFEFRKNTVMEILGSHNFEIKKLSAVVGRGGLLPPIQAGGYTVNAAMKKLIWEGNLSQHASNLGALLADTIAKPLGIPAFIYDAVSADEMEDIARITGFPEVQRKSLCHVLNTKAMGRKYAMALGKRYEDLNLVIAHLGGGISISAHKNGKIIDVISDDMGPFSPERSGSIPLFAVVELCYNNRYDKKAMLKKIRGLGGLKGHLGTSDCREIEKRILAGDKKAEKIYEAQAYQIAKGIGEIAAVLKGNLDGIILTGGMAYSEKMTAMIGEYIS... | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
EC: 2.7.2.7
Subcellular Location: Cytoplasm
Sequence Length: 356
Sequence Mass (Da): 38801
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A0A9D9XLV1 | MWMRALVPLYRLLACLRALPYRMGLLRAVRIPVPLVVVGNVSVGGTGKTPLVLALVEFLRKRGWNPGVVSRGHGGSERGPRLLDETATPHRVGDEPCLMHRRGVPVAIGRRRDHAALLLPSIGVDVIIADDGLQNPALARDLEICVLDGARRLGNGHLLPAGPLRESPERLARVDFVVCNGQGAGRNEIAM | 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... |
A0A497SMS5 | MVQKDYHSLQGLWVKLYVNIKRDLRKGKGVKKEKRKRARRASLLDKKSVYEHLEELRARVIRVFVIFSAFFLFSLFFIVQKLFDIFSHALQALNIRLVSIGPIDYFMALLNMSTFIAFLLTFPVLILEAYMFLYPALKPNEKRLVIFAFIASFLLFFFGVAFGYFAIVRISMQFFSRIAAASGIENIWSTSLFTSFVLWSCILAGLSFQMPVLGALLSKAGLLSSNKMKEGRRYFILFIFILAAIITPPDPLTQILLALPMILLYEVTLFFIKVFGQ | 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.
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 31914
Location Topology: Multi-pass membrane protein... |
V5WKZ1 | MDILVASNNHHKIEELSLILPGHHLIPVNRYLEDFDPEETGSTFLENSLIKSRSLFHRLSPEDREILAVLADDSGLSVDALNGRPGIYSSRFGHHEAGRTLSSEEQNSLLLEKLAGLPPSRRSARYICCMSLILDSNRIYTAQESWEGRIAATPSSAAGGFGYDPIFWLPGKECTVADISAEEKRLLSHRGKAARAIAAMLPDNP | 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 ... |
A0A9E9P377 | MAFHRTPAELLADAFSAYVTTWAKERDVDETAQDWLCGLAYWLSMAVSTGHVCLPLEEQPDFDRWPPIADVRALLFESGLVGTPDAPGNLPLILDAGNRLYLHRYFAYERTLARRIQALKTVMPVDTAAARLALDRFFGKAEAKTADWQRLAAALAMRGCLTIISGGPGTGKTTTVANILACLLSQQPAQRIMLAAPTGKAAMRMLEAIRAQTARFPADVQAKMPSEAFTLHRLLGMTSTAGVFRHHADNPLLVDTLVVDEASMIDLAMASHLFNALPAHARLIMLGDKDQLSAVEAGAVFSELSADPALTPACRADLAD... | Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA ... |
A0A1I1YBY8 | MEKKILEMIAELCGDEIVLEDGDINLLENDLIDSLDYTDLLVQFEEEFGIVMSPSELTREQMDTPNKIVEQVMARVA | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Pathway: Cell wall biogenesis; lipoteichoic acid biosynthesis.
Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl c... |
A0A497SD60 | MKSAVDRTPFHNRWISRNLSKKLSGEVRLLKRFAKALGVYGSDTRVQGFSGYLCELLIVRYGSFEALVREAAGWEPGKVFIDVQNHHKGKLPDGLKKKFEGQPMVVIDPVDRNRNVAAAFSPANFARFILACESFMKKPSIGFFFPAPRKADLNKIRKTMLSRGSKFIMVKFQRPDVIDDVLWPQLRRTAKRLKDIMLEYDFLVLDWAVHSDFSGVGEPAKGLSSYIMLELGVWKLPRIRKVTGPPVFIRPRAAEFRKKYQKLGKVWVEDDRLVAEVKREWLDAVEKLRDSLSDPLKDLKAKGIASHVAESVARGFRLVE... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
A0A142I9Q2 | SSGVEAGAGTXWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAASQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGG | 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-cytoc... |
A0A5S9PG67 | MAERPARNIAIWVGGAFVAALLFDVATKWLIINAVMVPPRVIEVVPFFNLTLGFNTGVSFGMFQDVFLEHPLVLAGIKVAITVGLLVWAMRTRRTIEATALGLIAGGAAGNIVDRVHQGAVTDFLDFHIGNWHWPTFNMADVAISIGVALLLAGSLFSTQPVLRTQEPLSNGKR | 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-, ... |
A0A1M5C1J8 | MLDDIEALKEEIAHVTITNEEELETFRLEFLSRKGKVPAMFSRMREVPNEEKAKVGKAMNAVKNLAEKTYEEHKKRLQRKETAALSAKDDLSLPAPPYAAGSYHPLTQTLEEMKEIFYRLGFSIADGPEVEDDFHNFTALNFPPNHPARDEQDTFFIRKSDDPETEDLVLRTHTSPVQIRLMQDKEPPIRTIMPGRVYRNEAVSPKSYFLFHQVEALYIDTDVSVAELKETLISFAQLMFGSDVKYRLRPGFFPFTEPSLEMDIWWETNGSGRWLEILGSGMVDPNVLKAVDIDPEKYTGFAWGMGVERIALLRHQIDDI... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 335
Sequence Mass (Da): 38754
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A0A1A5YS84 | MNEASFSSAPAYPVSLRIQGKLIVIIGGGRVAERKLNGLMDGGADKVTLISPYVVPGIAEQAEAGRLTYICREFVPDDLEGAYLAFAASSSAAVNLAVMNEADKRGIWCNRADQGDEGNFITPSVLRREELTIAVSAGGASPALASLIKEELEARFGEEVGAALRRLRELRQYAKTAIPDRELRRSVLRLAAEEALEDWSKAIHPQQWLNELLTRTEGRLNRDE | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 224
Sequence Mass (Da): 24465
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D2RIH6 | MGTGESIQQIREKLKGRPEPAELERWRQDSRAGVRKLLETYDRKQKAQAEERERLERFQDLERAFWARGMDQVAGCDEAGRGPLAGPLVTAAVILPHSIWLPGLNDSKKVTAARREILYGEILEQAVSVTVSILGPREIDRLNIYQAAKTAMTLCLTHLKVRPQAAVTDAMPLEIPGMEVEDLVHGDSRSAAVAAASIIAKVTRDHLMEDMDRQYPQYGFAKHKGYGTARHIQAILDCGPTPWHRRSFEPLKSMDLEEESVSENQLLQLK | 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... |
A0A5R8V2I6 | MTSTSTAERPAITLTIAGSEATGGAGAQADLKTFQELNTYGIIALTCIVSFDPKDNWNHRFVPVDAQVIADQLEAVQACYAESLDTVKLGMMGSPTTIDTVANALKKQAWKNVVLDPVLICKGQEPGHALDTDQALKANLLPLATFVTPNHFEAEQLSGISISSEEDLIAAAKKIHEASGAAVLAKGGVRIAGEDAIDVFYDGTTLEVLRAKKIGDVAVSGAGCSLAAAVTAELAKGASPLEAARTAKEFVTEGIRHRVSGATPFDALWQGGRR | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A0G1JAT5 | MDPRDEIRSRVDIVDFIGESLQLKPAGGGSFKAVCPFHMEKTPSFYVSREKQIWHCFGCGVGGDVFSFVMQMEGMDFSEALRTLAKRVGVEIPRYSSTQSNENEILVRVNEFAAACFQKILADSPAAAEARDYVERRGITPELLEKFGIGFAPEAWDTLAGFLNKKSVPAKEAERAGLLLPRRSGSGHIDRFRNRLMIPLRDVRGQTVGFTGRLMPGAKEDSGPKYLNSPETPIYHKSELLFGLDLAKKAIKLEKSVVVVEGNLDVVASHKAGVENVVASSGTALTEQQLDLLKRLTETLIFSFDQDAAGFNAAQRGIRL... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 604
Domain: Contains an N-termi... |
A0A4V6NGI8 | MPCSATKLEEARAYERREGSAIPAQDRPAFHLTPWVGWMNDPNGFCYYQGAYHMFYQYYPYDTVWGPMHWGHAVSTDLLHWEHRPCAMAPDTDADAKGCFSGTATPTPDGRLLLLYTGVQDDGKGGTKQLQCLAEGDGNDFVKDAANPVIGESLLPEGASCVDFRDPKIWYEDGVYHCVVSTRDDREQGRILLYESPDARRWTYRTTLDVCRNEYGKMWECPDFFALDDRQLLLVSPQEMEGTPDGEFHAGFGTVALLGRYDKERAAFTRESVQPIDYGTDFYAPQTTLTPDGRRVMVAWMQNWATVNEAPRNHRWFNCM... | Pathway: Glycan biosynthesis; sucrose metabolism.
Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
EC: 3.2.1.26
Subcellular Location: Cytoplasm
Sequence Length: 490
Sequenc... |
D3RP32 | MALDIKKFLPRFTGEARDHLGRLAAGLAPLASGAGLDGETINELFRAAHTIKGSARMLKLTSIAETAHQLEEVLGALREGRTQPSPELGALLIRALDAISALVEQVESSAGQLAPPDESLCAALAAAAQGETAPSAPAPEAAPAPNDASRPTPTEAPPDEATRSTLTVLRAPDSVRVRMDKLDELIKLMGEVVSNQAKLRHKLLEARTLDKSLAALASMEAEPERERLTAQSHAMHGFTLALRDLVQEQERLTTELNDRALVMRMLPLAIVFEPIAPLARQLGRELGKEVNCEISGGEIELDRQLIDHLSDALVHLLRNA... | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 731
Sequen... |
A0A7T5R8P3 | MTQSPKGTQDFGPKEAMARGEMIGALRQVFQLYGFEPLETTSLQNFEVLSSKYTGGAEILKETYKLEDQGGRKLGLRYDLTVPLVRFMAENRSLAKPFKRYEIGKVWRDGPLKAGRYREFMQVDADVIGVTSVAAEAELLAMAQTFFKALGIDAVIKYNNRKVLNGLLKKFSIPEREWNGVLQSMDKLEKMGRAYVEKELTEKGVDKGVAKDVVEIIAKTKDLELLTGVIDNDVGRKGIEELLALQEYLVYLGVDTAEWDLSLSRGLDYYTGTVFEAFFTGGKVTSSIAGGGRYDKMIGALIGSKEDVPAVGISFGLDAI... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 421
Sequence Mass (Da): 46911
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A0A9C6SZ64 | MLQISTLDSILEEEEVSSKSVSGTTARSTIEEFHRSGNIQKSDGLSQIEQRKKEKSDALVLCELSPRLALSAEKVKLQSCEEKLEDSILLDNPLAQSSMIQSDEMNRSLSAAKKQIDELKQLRQLNSEQYETCRERTRELDDQSILEMRTQLRATGNQLSIARAQIVKLKKQISETNDAKVDRNTFEQYENIVIKSQQKVLTLQAQKDASELKLASQLAKAERDQELAQKNQELAKQQLEEIKAQVEKLKEEHHKEVGELQEQKGALETENEAYLKDISTHCESIKKFKRQVASLQADSIIRSRIQSEGKSAEEIEKLKS... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltr... |
A0A2M7VDV1 | MTIGQKIRSLFMKSQPIITRFAPSPTGYMHIGGLRTALYNYALAKKTNGQFILRIEDTDRQRLVADSIIDIINTLNSFHLHYDQGPITKDDHTLSEIGNNGPYLQSARLTIYQKYGQKLIAQGNAYYCFCDSDRLSQLHEQQTKEKKPTKYDGFCRHLTPATVADNLNKKKSYVIRLAVPADQKIEVLDEIRGQLIFDSNLIDDQILIKSDGYPTYHLAVIVDDHLMGVNHIIRGEEWLPSTPKHVLLYKYLDWPLPKYIHLPLLINRDRSKLSKRSGDVAVCDYLAKGYLPEAIINFIALLGWHPGQDLEKMTLDQIIQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-g... |
A0A4U0PWN4 | MVVKKFYGATTRDALRQVRDELGPDALILSNRQIAGGGVEIMAVADADVAALTSIQSTPIAAKVGPRAAQNGARLIHSAQHERTEPTPTPLNRALARSYAIADEDQEPTLDDVPAEEVPQVVRSNRPPRAPAAPAPQVAPPAPRNAPEPPRRALPNFSFEDDDAHDALSPAPVNGEAMEDIAREIRLLRGLLESQIAGMAWGELSKHAPEKLEALRQLLAAGFCPALSRQLIDKMPGGLTLDAGMRWVKAALAHNLPAMGNHDALIERGGIVALIGPTGVGKTTTVAKLAARCALTHGPQSVALLTTDSYRIGAQDQLRI... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 496
Sequence Mass (Da): 53456
Location Topology: Peripheral membrane protein
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A0A7J3KDF6 | MAEKNLKEKLKKISECTWEIPKEGNMRVPARIFLSEKLLEQVEEGAIQQVMNVAHLPGIFKHSLAMPDMHFGYGFPIGGVAALDFKEGGLSPGGIGFDINCLSPDSEILTRDGYRIKIKDIPKYINKIELVTRDKDIDYKNVLFVAERKQNGKVYKIVTNLGRELIASVDHLIFCVNKLKKVEELKIGDKVIINPFTGVEYQECDDLILDISDFEGCDIQIIKKLKENKLLPLKLSNEKIGAIARLVGYILGDGCIYKIKENGRERLLTSINGSKEDLENIRKDILLLGFKPSKIYSRKRVIKGINYYGSFVTINEESYI... | 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: 967
Sequence Mass (Da): 109611
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F7RUX7 | MTPANANSSLHYADIEFDQQGTPESMLFEDIYFSRKDGIAESDYVFIQHNDLPERFLQLNEYESFLIAETGFGSGLNFLLAADLFLRSAPKSAQLYFVSFEKYPLKHADLARILSYWPQFEPLSSLLLAQYPPLLPGLQRLRLHPQITLDLYFADVNEALPEWAALHPRHVNAWFLDGFAPNKNPQMWQPELYQAISVSMANNASLATFSANGDVRRGLIRAGLNIKKAPGFGRKREMLYGTINKLGQPEPPRAKSIAIIGDGIAAATLAYALRNSEKDITIFSSASEPAAGASGNPQGAVYPLLQAQWTPTSDFYSHAH... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
R6AVN0 | MAYKVLYRKYRPQNFNDLYGQDSIKEILKDSIINNKLAHAYCFNGPRGTGKTSTAKLFAKAINCENAKDGIACGECNSCKNFNENPDIIEIDAASNNGVEEIRELRDNVKILPSNSKYKIYIIDEVHMLSQSAWNAFLKTLEEPPKHVIFILATTEIQKVPITVLSRCQRFTFRKIPKNIICDRIQSIAKEENIDIEKSAAEYIADLADGGMRDALGYLDQLSKENKKITTELIQNCFGIIGDSTIEEIFLSAKEENLENLQNIFDDIANQGLEINLLISKILNYLYNEEIKILQNKSSVFNDQQTIKELAFEISNCYLK... | 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: 552
Seq... |
A0A8T3YDW4 | MRLFIAIDAGKAATDKIRRLSTGMEKSKSIRAIDPDNVHITLKFLGEVRDDDVGRVSEAVRTALSGFGSFRMAIEGMGYFGSARNPRVAWLGIGAGRETVIGMMQKLEQSLTFIRSESRTGQPHITLARLKAPAGAATLIDFVAKNKGVKVCEVDVKDVRLKRSVLTPTGAQYTDIEVYQLE | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 182
Sequence Mass (Da): 19914
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A0A8T4DWJ3 | MIGFGDMITRHLAREKRTKDVGRYYPSEIGGCLRKVWFSYRFPKDVDPEVIKIFHLGNMIHDFVAEVMKSEKNPEVTLVGEEVPFTIEDGDFTISGRIDDIVMLEGEDEKILVEVKSTKMTDILDGPKDEHVMQLQLYMYAMKIFRGIVLYIEKNTLKTKEFEVKYDQNSVNEVMKRFRALHANLKAETVPPAEAKENPDKRWMCKYCDYLEECQRAEIDGN | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A497SAZ0 | MKPTIIVNFKTYEQATGSRAESLAKLHEKVREESGADVMVAVQNADIHRVSSSVSIPVLAQHADPVSYGSNTGHDMPECLKENGAWGVLINHSEDRMPMEEIKKTIERCKEAGLKTIVCAENTAEGKDIVKMLPDYIAFEDPELIGTGRSVSANAPESVKGFSDMVDSFNREEGKEVVPLCGAGISTGDDVRKSIELGMHGVLVASAITKAENPESVLREFVA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A3D8IJH1 | MEIDLLLRIAVAFLKDMNLEDFQKLVYETSFLVSDINSFENDKIPKDSDNIQKNKYSSNLFSPEFHITSPRYEAEILLGFILNMTRVEIHANPKKEINDFNKQRYFKLLAMRKNGTPLEYLTNRVSFYNLELYVDKNVLIPRPETEILVDKAIELMNQHNIASFVEVGVGSGAIITAILKNTQNTYGIATDISKEALNIAKHNAEVLGVKNRCDFIESNLLDSPYIMLQKPISLLIANPPYIANNYPLNQEVLCEPHIALFGGEKGDEILKRLIMQARQKNITHIICEMGYNQKASMQEILHYTNYEVAFYKDYAGLDRG... | 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... |
A0A401Z928 | MNTEATESALLTPHATTSNRHPHQPDIDHLLPYTPGESLQTFSQRTGIPANKVIKLNANESPYGPVPSALQMLRDHDWYNQYPDVQAQVLTEAISRYTGVEGAHVVLGHGSMEVIRLLWSLFLSPGDEIITCSPTFSLYTSATRERRAHLRNIPRRADYSIDLAAVLAELTPAARMIVLCSPNNPTGNPLPEEELLTLLKTGLIVVVDEAYVEFSSHPTGYAHLVPHYQNLVVIRTFSKWAGLAGLRVGYGLFPEWIVNSARQAQYPFAVNVAGHLAATATLNHLDEARERVQWIIEERERLSHVLASYPFLHPIPSEGN... | 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: 384
Sequence Mass (Da): 43040
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A0A8T4DYE2 | MKPVFLINCKAYEQGIGDNAVKIAKAAERVAREEKIDIIISVQPADIRMVSETVKIPVFAQHVDPVAPGSHTGHVLPESVKGAGAKGSLISHAERRLDFKTIENTIKRCKEIGLVTVVCAPNVKYAKKITSFGPDYVAYEDPVLIGSGKSISQTKPDSVKRFVKEVKKINPKTIPLCGAGVSTGKDAESSLKLGTSGVLVASAVVKADDPYRVIKEIAGGLR | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A7G9R2P9 | MRHRGPRTRGARRPRRWLPRPVPALLGRRPRGAPRARGVRRARPRRGLLRPARRVEAAPVSGGPLRLAVLVSGSGTNLQALLDAPAAPFEVVVVGADREDTGGVERARARGIPTFVCRVADHPDRAGWDAALARSLATHDVDLVVSAGFMKVLGPQVLAAHRVVNTHPALLPSFPGAHGVRDALAHGVRVTGCTCHWVDAGVDTGPVIDQRAVRVEDGDTVETLHERIKVQERAMLVEVLTRLASDRSWR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A7Y8HKD4 | MIYLSLEWIIMQNKTNLFDTWNNHKKQIHSIEKIIGFSLFEIVFMKIGTNIGYEQDGKGEDFLRPVLVYKKFNNRVFLGIPLTSKQSDDKFHFGFEYKKGRKSFAILSQIRLFDIKRAKYKDGKISKRNFKELQNKLLELIVTPLEDEGERTKAICRESISKEALNINILVTGSNGQVGSELKELSINYPYNLFFTDRETLDITHEDAIKDFITKNSINVIINCAAYTAVDKAESDFENADKINHIAVRYLAKIAKESSIKLIHISTDYVFDGENYKPYMESDITNPKSVYGKTKLDGEVAMQEINPQNSIIIRTSWVYS... | 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: 453
Sequence Mass (Da): 52404
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A0A2U1RKT9 | MSTSTEEVIILGSGPAGLTAALYTARANLHPLVIEGNETGGQLVLTTLVENYPGFPDGLMGPDLISRMRQQAERFGARFGKGDATAADLHSRPFTLTVDNEVRQTKALIVATGASANMLGLESERKLLGHGVSTCATCDGFFFRDQQVAVVGGGDSAVEEALFLTKFATKVTLIHRRDKLRASKIMQERTFANPKIEILWNRTVAEILDVSQGKVTGIATRRDGSTSAETLACDGVFVAIGHSPNTKLFAGQLEMDERGYIITRNGTMTSVPGVFAAGDVQDHVYKQAVTAAGSGCMAALDVERYLESL | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 309
Sequence Mass (Da): 33000
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F0KPJ9 | MTKRFNYVIGDVQGCFEALKALLKEIRFDPDQDFLWFAGDLVARGENSVGALRFIKKLAERGAAATVLGNHDLTLIAGARGLKEIKEKDRTQDVIDAIDGDELIDWLRKQPLCLLPNEHTILTHAGIPCIWDAQKTVTLAKEVEAVLANEDLSVLDAFLADMYGSKPDLWEDNLTGSARLRCITNYLTRMRLTNAEGALEFSFKDSLDAPMPDGYLPWFEFPSKAAQTHQIIFGHWAALEGRTINEQIQNIDGGCVWGRKLMAYRLEDKEIFSVENPVQI | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
EC: 3.6.1.41
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Length: 280
Sequence Mass (Da): 31455
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A0A426Q2Z4 | MRAEATLCRVKTTTTPGRQDPGHGPDHQTTDQHDRHDRTDGAPAPATVSDAVAAVIRERADHVFGVVGNGNIHLVSALTSAGFPYTAARHEAGAVTMADAFTRAGGGVAVATTTYGPGFTNALTPLTELVNARIPVVYVVSDIPSDGPRPIDVDQRAITAALGVTVVTATPTNATAAAERAFTVAARSRGPVVLFIHYDHVAAPLAADPEPVTDPGPVPPATAPSEDAQPASAFRGEETDTAAVARLLTGARRPLILAGRGVVESGTAADVLALGDELGALFVTSAMARHVVDSAWSLGICGGFLHTGYRRTVADADVVL... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 624
Sequence Mass (Da): 64920
|
Q7VR94 | MESMKLNHKYYGVYEWLIVRISAILTILYSVYLFNFINIDDNFSYEKWCIFFYDKKIKIFNTIVLLMLLKHTWIGMRHILEDYISSIILRRLSIGLIHIILYVYLLFGIAVVWGI | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 13892
Location Topology: Multi-pass me... |
A0A7Y8HMZ9 | MAKFTPILICATNTGVGKSFSTTKIIDYLNSINIDTVGFKPIETGVFDTAQDCELLLKHTKQNIKYKNLEVDDINCYKFSLPAAPYIAKDKKIKLKNIKTKLKKLEKISDVVMIESAGGLMTPIKKNFFMIDLANYLNAKVLLITPSRLGCINETMLCLELLKHRDIKYEWCINIMNDKDDFFNISYNYYHEKFGDVLFLDRDIKKIVERLLDK | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A3R8QS02 | MLKGFKDFILRGNVIELAVAVVIGSAFTAIVTAFTKGIINPLINAINGNVDASGLTVPLRGHDRADAIVDFGSVITAAINFLIIAAVVYFILIAPMNKLKEIQNRRKGIDPNEAAATETELLEQIRDLLIEQNRAEVGVESRVARDVGDVQQTSDAADVADPSTGTGRHSAN | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 172
Sequence Mass (Da): 18307
Location Topology: Multi-pass membrane protein
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R6BGU5 | MFENLKLIIKNAYTPYSNYNVACILVMNNNQEFIGVNVENASYKNGLCAEQVAFASAIAEGYKKEDFKELHVAGSGKEICVPCFLCRELLVEFMDEDASVFCYNNKGKCVEYKVKDLCPYPFVLEDNDDK | 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: 130
Sequence Mass (Da): 14753
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A0A0D8NG03 | KRQPRQQRMIQRQTQAVLDYLPLETVLTALRNRPLQQTVIITGRGCHREIIELADTVSELRPVKHAFDAGIKAQMGIDY | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
Function: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids... |
A0A940KVB8 | MSRQAERNVRRQAPAPKVAAEPRRARVPWRARLAAWRDQHLYSFFSSLGRLAARPWANALTVLVLGFALALPLMFYLLFDNARDLAGGLREAREVTVFLQPAIDGKGAVALAAELRARADVADVLIRTPEEGLAEFRQLSGFGEALDALHANPLPTVLVVTPGAQSDLDAPPLLADLKADRRVDLVQYDATWRRKLSDILHFGERIVAVIAALLALATLLVIGNTVRMDIQARTAEISVMQLIGASDGFVRRPFLYAGFWYGLFGGICALAIVIAMELALVAPAQRVIESYGGRFALHGVGVLVALAVIGASALLGWLGA... | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell inner membrane
Sequence Length: 335
Sequence Mass (Da): 36095
Location Topology: Multi-pass membrane protein
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A0A556N135 | MRQEEAIYKVRENEESAISLRDLLDKYLIHWRWVLSSVILLLVLGWVYARYQTPSYESTATVLIEQESKSGMASEELGMLKDLGLASGGGVLEDEIELYQSRSLMEHVVRELQLHWKYQIVGTTTGLVRSELYDSNPIRVRSVEADSLYYDKHYEFEITLTSANEYTITSGNELVGNMYKYGAVLQLSIGNIILEKTNEFKSPWIGKRILINVSPVSEVATEIRKNLSVEPASKDANILVLKVKGHNVGKNNAILNKIIAVHQENAINNKNEVVKNTTAFINDRMKFIAAELTDVEKKGEDYKSKHHLVDVTTDAVSYLE... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 795
Sequence Mass (Da): 90007
Location Topology: Multi-pass membrane protein
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A0A8T4KT78 | MDFAAIEKKWQDRWEKEHAFEPDLDPAKKKFFITFPYPYVNGAPHVGHAYSSLRTDAYARFKRMRGFNVLYPQGFHATGEPILGVIERLRKNDQSQIQTLKQFGATDEDIKKFKESPEYLVNFWIAEWKKAQKAAGFSIDWRRSFVTTTLTPQYSRFIEWQYNTLKKQGYVVQGTHPVIWCPHDQSPTGDHDRLEGEGESPVEYTAIKFRLGDAFLACATLRPETVFGVTNIWINPQGDYVKAVVNGEKWIISRDAAAKLADQLKKVKIESHVNPADLLGKRAVHPLDNRQMPILPAGFVDTGIATGVVMSVPSHAPFDW... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
EC: 6.1.1.4
Subcellular Location: Cytoplasm
Sequence Length: 922
Sequence Mass (Da): 104309
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A0A0F0H8V3 | MDSLRRWASLLSPLLATVLLAGTVLALTPTAASAATVDTNAWYVLVNRNSGKAMDVAAASTADGAVVQQWSRHDGANQQWQFVDSGGGYYRLKSKNSGKVLDVDNWSAADGGKVQQWTDLNGTNQQFRLADSDGGYARLINRNSGKTVEVTGQSTADGAAVVQNGDRNATSQQWQLVRVDSTPPGTCSLPSTYRWSSTGSLANPKSGLVSLKDFSNVVYNGKHLVYGSTVDSSGQHYGSMNFGTFTNWSDMASAPQNTMNLGTVAPTLFYFAPKNIWVLAYQWGPTTFSYRTSSDPTNANGWSSPQPLFSGNVPGNTAID... | Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 372
Sequence Mass (Da): 39642
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R6NXS1 | MKLTVNAPAKINLFLDIVGRLDNGYHSLFMIMQAVGLADTVTVEAAESGIELSCSEPKLPCGEKNIAYKAAKAFFEATGIKGGVRLHIDKRIPFEAGLAGGSADAAATLVGLNELYGLPLSERELCEIGLRVGSDVPFCIVGGTCLSQNTGGVLSYLKPLKQCSIVISKPVKGVSTAEAYSAADSVYLYHPDSMRMLDACERGDFGGICRYAGNVFEQVVEVVERVEIKRIMREEGAALAQMSGSGPSVFALFEDEAAAARCAERLRPICPQTYVTYPLERGAAVIKKGKGASK | 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... |
A0A3D8IP89 | MNINISEEILKIFYTSHNLLAFSGGIDSSALFFILQDYGVFFDIAIVDYKKREQSKEEISYAQSLAKKYHKKCYVLESKTIDSDFEMEARNVRYNFFHKLLLQYDYNALIMAHHFDDKLEWFFMQFCRGAGLNTLLGFQAVESRSVQQHHYYLVRPLISYKKQDLLHYNQTHAIHFFYDKSNADCKYLRNFFRHEILAKLQNFSQGMQQSLEFLSNERELLYPKVIICHDYNLLYCKISDCKGNKHIIHIIDTLSKKMDYVMSKNQKKELHALFSNNMAEYAECVMGDRIIIAKNTTYLFVGLQPKWLMKMCLLENLENQ... | 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)... |
A0A5B9T5G4 | GTLYLIFGAWAGMVGTALSLLIRAELSQPGTLLGDDQTYNVIVTAHAFVMIFFMVMPIMIGGFGNWLMPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHSGASVDLTIFSLHLAGVSSILGAINFITTAINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPSGGGDPILYQHLFW | 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-cytoc... |
A0A6A5K3R4 | MDPSTSYRGGGTFVAEIAWYKTTLHRSQFDSVKGLKGACHGVPRSGPGERSFSSGDKEWDKRLGTISDRNHFVEIQVVQESSVANQDHGFCRNDVDLFIYSESRGYGDGILKRYTVETCTRFVEGRANATKYTKEQDKSCQWAKTSRNLSNSTVYLHRT | 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: 159
Sequence Mass (Da): 17945
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A0A7J3CJS0 | LKKEALKYAKELEKEGNEVFISASPCFGACDIALEEAKKVEAEKIIHFGHSKLIDIKEIEVEYVEPKIEIEKELLNQLITEASQKIRFKKIGLVTNVSHISQLKEIKELFKRNGKEIFTANGERTKKEAQILGCDVSAATKIEKEVEAFVYFGGGLFHPLGALILTNKPFFVIDPFQRKIDEITNLREKYKKISNAKISIASQAKTFGILVSTKPGQFNLEKALKIKEDLKKIGKEGFLLVANTFDFNEISNFEVDAFINTACPRIGIEEGERIKNKPILSVEEFYFLFKLLNSKDS | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation f... |
A0A367YIB3 | MTSARAYSTTTDMPSSIKSLTTQLDSIAPRFLLKKGDIEIMNEPSVFYSTLLDKISTAKRRIFLSTLYIGTKQHELVQCISDAMAKNDDLHVYILTDALRGTREAPNPCSASLLAPLEAKYGKRIDIRMYHTPHLAGFTKMLAPKRINEGWGLQHMKLYGFDQEIILSGANLSQDYFTDRQDRYYLFKDKPLTDYYFKIHKAVASLSYRIVHTTQLKQGFKMTWPTTNASGEPHLNFQRFLSDSSHLLTPLLQQQKLNSFEEFENSPDHDTLVYPVSQFTPLFPQNQDQLTEKPAILRVLSYGDSPKNKWWFTAGYFNML... | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-... |
A0A367YIL3 | MAKKVSTPASKVAAKQAAIRSKQHEDVLTIDPLVDPIFQKGHIRDPQKRLLSTKEYWMLSSLLVVAFYVRMYKLSYPNSVVFDEYILGTFFMDVHPPLAKMLFGAVGAVGGFKGDLISSQLSSHMPHFLLIIENFNVTISRYILLDSPLLFFIAAAVYAWKKFEIQVPFTFGWYKSLIATGIALGLALSSKWVGLFTVAWVGLLCLYQLWFIIGDLTVSTKKIVHHFFARGFILLGIPIALYLAFFAIHFQLLYKEGDGGAFMTSAFRASLQGNKIPKDIIEPVGLATTITLYPHLDSNNKWLIEPFNGTIYNDTFVPLI... | 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 Locatio... |
F7RZ69 | MPVILHRPLPAIEELQAEGLAIAYTPNKKGKHSIGILNLMPNNAETERHWLRLFANLKESVEVHFIRLSTWRPKTAQAKHMAKFYEPLTLESDFDGLLITGAPLGHKEYEQVPYWDELKEIFDMSSYYATSTLYSCWAANAALHHYYNIPRRLRGRKISGIYEHRIVRRHPLVEHMEPGVQFPHSRFAEARQTQLFAHPEVRVIMQAPNAGAFYAVDEPRRRAYIFGHPEYEADTLQKEFKREFQKGLEPLPPEYYFVDSETFELPLPQWQEEGTKLLQNWINYWLK | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
EC:... |
A0A2N2FBE8 | MRQFMMGGLVESNAEVREGHYLMSLRLPLSFALPLPGQFVMVRLKGRKDMLLARPFSVSGFHRQAQDIRIEILYRVAGQGTRLFARLRPGDDLDISGPLGRPFEIPQNIRNVILVSGGVGVAPLRYLLACLQVQGTDRAPRIDFYIGAKTVDELLELETIRCLCDNLHVCTDDCSMGHPGLVTEPLEKAIKSYPLNDTLICACGPLGMIRRLSEILTQYPLACQVSLEERMACGLGACLGCAVAVRGQDGEKQYQRVCREGPVFNLRDLLWD | Cofactor: Binds 1 FAD per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate ... |
A0A211YYH7 | PTAVSAASILSRASAFDLADRFHLPVITFVDTAGAYPGVASEERGVAEAIAKSIESCLKVQVPSWPPSPPEITTPLSGPSSSNSSPTAKNPSSPSSPSCASSSSSPTPNSDLNPN | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
EC: 2.1.3.15
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 115
Sequence Mass (Da): 11595
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A0A4R1QTA6 | MKTRLLCAVMLLALAIGLAMPAAAQWDPPQGTTDKAQAVYLYQLDTETLVYAKNENERRAPASLTKLMTALLLVESGQPLDTPFTIPDGLQPEFNEILANYGTRAGLLCGETVTLQDLLYGCLLPSGNDAASAIAWYLGDGDEAAFLDQMNRWAAELGCTDTHFSCPHGLDSMDQGNYSTAQDMFRIARACMENETLMEVMCSTEYWMPLTELHTQADAGAPEGKSYRIRSTVVMQNPDSPLYRDYIRGMKTGFTDEAGRCFVSGAQQGGANWLLVVMGAQDGLAEDGVNYAFHTTADLYDWALEALAPTAAVNTETPAT... | 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-alanin... |
A0A6P8YVE7 | MPADKILSDKLDAQLDNESAKETLLQRHHSVHLLPNNEASNPSKPTSTHSRSRSMNPYHYVGGHLNRIIIRCILILCIISLILHLMPHHRLSTAISHKSNGLAILIWNESEDAPDWTPLQCGCLVTANRNYYKGNIDAVVVNVDRPYSLRQLKDIKHTPNYLMVLASTSPLSLAQNPLYDHANSPFNFTMSYRLDSDLVWSSHYFSKLGELNTRVQQFDVPNENFMETWTVQQQYDFRIKLKRKHLLAGYMMYAVNDYSLPESLYLQELRNHIELDAFMGCNQYQDCSHYKFMLIFDPSVCPDFVHPQFYMALANFVVPV... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 421
Sequence Mass (Da): 48949
Location Topology: Single-pass type II membrane protein
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A0A8G2A5A1 | MICPPCRRQPRARRSIRRWLAGQLLFSSWVSQGLLVLLTLVLTGWLLRRVLRPMRQLSALMVRREPGLLTPLPELLPWSETRLLIVAFNRYIDRLRVMISRQERFSADASHQLKTPLAVLKTQASVALASDDPQLWRESLQAMRTTLDGTIMLTERLLQLASVKGKEQGDRAFLAVDLQDIVQNSCFSRITQARSKNIDLGYEGERSAVMIAGDGVLLAELCANLLDNAIRYTPANGTVTLSLRRDGEGVVMEVEDSGPGIEDDQIQQALLPFQRLENVGDNPGAGLGLALVTDIARLHRSHPQLLRSETLGGLKVRLRF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 334
Sequence Mass (Da): 37157
Location Topology: Multi-pass membrane protein
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A0A485A913 | MEAGRLQIPGLHPETVGATRKLISVVIWLFALSAAYPFLPGANSLAFKGISVFFGLMLTLGSAGVMNHAMSGLVLIYSRALRKGDVIRIADNEGEVSEIGMLATKIVTRENYIVTVPNAVVVSGKNHQPQRTKQRKRP | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
Q9X658 | MCPLVTADIPSTGVRLSMWVPEDHFPMDPYKARCALSRLLLMNGPNLGILGRRQPEIYGTDTLADIEGRVAEEVTETRLEIEAFQHDGEAEMLRTIQADHDTACAIINPAALTTAGWGLGGVGHRLPARALPEKAAGS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 138
Sequence Mass (Da): 14889
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A0A1C7DJ54 | MMEYIIIAVIILLAITIIGFMFRKKHLAEIERLEQLKLQIQNKPILEELTKVKQLNMNGQTEEMFERWRNVWTEIMDVHIPKIDASLYDAEEAINRFRFGKATKIEQETEVKIDTVDQQMNSILVELEELIGSEEKNRSEIDLIQEKYRRARKNLLAHQHSYGAAAGPLEKKLESFIPMFDEYEKLTNEGNYLKAREIVISLSTEGEAAFLLVDDIPPLLADVQTKIPSYIAELRQGKNEMEEQSYYLGHLELTLQLDEMEEELKVLKMNIAQLVVEQTKIAVESMKDQIDSLYELLEKEVEAKHYVDEFSVDTERHLEV... | Function: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Subcellular Location: Cell membrane
Sequence Length: 567
Sequence Mas... |
W2P8Z6 | MRQGILMLAVAVVGLVSCNATPAVESMHNQVSLAASTQPTAVGQNEIASRRLLRTAETSEERGYESLKSLLPGMRMWPKDGKTLPTRFVKKMLRKELLRTKVFEDWTRADIDGPALREALGDMTKKGRAELLTRFTAFLGPQPGLVYHRRPFV | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 153
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 17081
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A0A5P6PE22 | MHRKYSQEARLGRSSPCGEVGAKRRQSQIPSGGPRMNRSERRSAAKRGQISPGQATSFTRALSTSAAEQFEAGIWHHQAGRLTEAEACYRQTLAAQPNHPDALYHLALLARQAGRADVALDLLGKSIKLKRTDPLYFLYYATTLQELERYDEALASYDRALALLPEHADIFYNRGLVLKALGRFDDALASLESALALEPDFAEAWNNCGVLQQQMQQFDRAIASFDRALALKPSYAEAFFNRGITLQELGRLDEALAAYDQALALAPDFAEAHNYRGVVLQRLRRLDDALASFDAALALRPDHADTHNNRAIALLEMKRH... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.255
Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
Sequence Length: 857
Sequence Mass (Da): 95049
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A0A4Q9B916 | MRYLILFSFLIFACKPNWRIDPAKVKEELQAQAAQNTERKIKVETRLGDFELELDDRTPLHSVNFIRLVKMGYFKDRYFYRNVYEIGIQGGGEYFDRLNYLVPAEYLDELRPERGTISMARYDEGNPLQSSSPTEFFIVTDSEQASRFYRKYVVFGKVTKGMAVVDSIKKEHSYDEKPVIPVKFSMSVLDPK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 192
Sequence Mass (Da): 22482
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A0A4Q3Z8V4 | MVNASKARSGTDMTLAGERGPLGRRVETAARLLAWSGGVVLLAVATVTFVSVIGRALDGVGLGAVPGDYELVAHGCAIAVFFFLPWCQLKRGHVTVDILTDRFPPRVQAVFGLMGDLLVTLASAVILRQLWFGFGEKFPYGSDSVRQWLGMGYKPFFPETTYELQIPVWILYGVALVGALVMLAVGLYTTWRAACWVRDGREGAA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 205
Sequence Mass (Da): 22182
Location Topology: Multi-pass membrane protein
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A0A066VPG8 | MSTNKLRVCILHPDLGIGGAERLIVDAAIGLQKRGHAVHIYTSYHDPGHAFEETTDGTLTVRYIKPPLPRHIFGALHILLAILRQLHLVITLLFLVYFGREKAYDVFLVDQLSACVPLLRWGMQKSVVFYCHFPDKLLSDGTVAAVEGVQATKGKGGIKALVKKLYRLPVNWVEEVTTRQADIALANSNFTSRVFKHSFPSIKTDPMVVYPGINISAYDSPPPSSDTKEIKQVKSDKTTLLSLNRFERKKNAALAIQAFALLPASGIRLVLAGGYDPRLIDNVECLRGLVKLCEDNGLEWDIVSPRELPQLPTPSPNKTR... | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-al... |
A0A066WEH7 | MGTCAYALHETSRPEPRPTKSAMSNNVFRIGDPELFPEAAIEIAVKTSKATALVRPHSMKKFTKREVVAATQGASTQAGSSPSDYKQYVELKRRTDYVVKLMESSTEEEEGEEDREKQEPQGEVVEKETLVKAFKYGSTWVPCEEGHFEGLHTRKGIEVISFTPENKYQRHFSMGEVQYIYADIGSSRAQVAFSSIVHAMFKKGFMAVVRWVNRDDSDPKMGVCKAEPGDVDYMMWVQVPFAEDVRRYCFPSLEQYISKKGEVLKEHPYIPTNNLXXXXXXXXXXXXXXXXXXXXXXXXIRTEWFDLTQSFNPAVHRIKQ... | Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and ther... |
A0A368C7I6 | MDKKKMNISLIGMPGAGKTTIAKLLATKLNLEFIDSDHLIEKRNNQSIQNILDSEGHAELRLKEEEVILSCSLDNTILATGGSAVYSNKAMNHLNNHSIVIYLDIPISLVMQRVGDYSNRGFAEPNGKSPQDVFNQRTVLYKKWCHLMIDGACDADIVAQNIIKAVSDN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A4U0Q914 | MQTAPQGRARQRFVQQLKLERWRVWFILTGLMILFIVLIARGFFLQIMDDGFLQQQGEARYARTLKLEANRGMITDRNGEPLAISTPVQSIWVSPRSIKLLPAGQKRPDHWEPSSEKEPVPMSRDEMSKLAKAVDMPVKVVESRLSTSRKSGDKPDFVWLKRHMAPQDAKKVLELNLPGVYAQTEYRRYYPAGEVTAHILGFTNIDGKGQEGFELTRQDMLAGKPGSRTVIRDRRGFIVEDISTIIPPKDGETLTLSIDRRIQYLAYRELKAAVEANKALGGGIVVLDARTGEVLALANTPSYNPNSRARIDPARRRNRA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
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.
EC: 3.4.1... |
A0A8U0UGW4 | MAGLRKPIQNQNCGVPLGWGKIGKEVHRQGLYHSQQLPVPHIIVTLSRTELLRKESAGAEFRWHPNAVIARAFKRLKALSASADHRKRTSPPFSNEYRQYKKSANANFEPHVSEEKVTAQRTFTLSDVFNSSIRARSYNMRWISDPEYLHEKDGSIFLHNLITGNNSEFLSSITFDQVAAYDYVVSADQKYVAFKSNWTKIWRHSFTASYSLYDFAGSTFLSTPDIPHQVHLFAWAPTGNKMAFVWENDVYVKTSPTAKAIQVTSNGKHNKILNGIPDWVYEEEMFSSYEAMWLPGGKYLAYAEFNDTLVQNIEYSWYGK... | EC: 3.4.14.5
Subcellular Location: Apical cell membrane
Sequence Length: 522
Sequence Mass (Da): 59168
Location Topology: Single-pass type II membrane protein
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A0A2H0BB34 | MKLSLGFSPCPNDTYIFDAIVNNRINLKGYGFDVEMADIEQLNRNAFAHIFDITKLSFHAFAHVSENYMLLPAGAALGFGNGPLLISKHRIYPDEVSFVKIAIPGVFTTAAMLLYVFWQPDKKNIREYLFSSIEEVVLSGEADAGLIIHETRFTYQKKGLLKIADLGEMWEKETHKPLPLGGIAIKRMFPDKIKNEIAILIKESIEFANRFPEASKQFIQKHARETSKQITKQHIQLYVNEFSTNLGTKGEEAINHLLKSGFEKKITPKVVEPVFV | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the conversion of cyclic dehypoxanthine futalosine (cyclic DHFL) into 1,4-dihydroxy-6-naphthoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.1.-.-
Sequence Length: 276
Sequence Mass (Da): 31261
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A0A1B0Y2H0 | SFWGATVITNLFSAIPFIGGDIVIWLWGGFAVDAATLNRFFSLHFLVPFLVAGIVLVHLLFLHQTGSNNPLGVKSNFDKLPFHPYFSLKDSLGIMVLIMILMGVVLWNPWMLGDSENFIPANPLVTPVHIQPEWYFLF | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a p... |
A0A066VRU8 | MLFTSLAVLIAGATSVRAHGYPQTVNIGGQTYQAWHPFTDPYAQPNPTTVVRKVPDDSPLTYNSPDLRCNKGGSVGNGVTATVAAGQSVTWAMNTWPADHKGPMQVYMANCGDSCDNFDGAGNVWFKVSSEGLLDPASFYWGSDKLVSQGNSWTQVIPSNIKAGKYLMRFELIALHSAGSPQFYPSCTQLDVTGGGDGAPTQSELFSIPGVYQQGDSGLFGSIWEQPQSWPQVGPNVAAFISGESAPAPAPSSTPTTPTSSDKPASTSKSSSTSKSAATFQVIPSNIKAGKYLMRFELIALHSAGSPQFYPSCTQLDVSG... | 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: Secre... |
A0A066VZ48 | ATRAVFHPKPIPWFVSDVTPRDWDAIFRALKDPSFFTTLEASMAHPESLKHMIDRWEGYVQTGVFTLGPKETYAFWVAPGGYWEIAPGRDGEVVGKVLDGSGLVIFKGDLNYRKLTGDIKWPNNVPWEEAIGPLAGRFPLLSLRTCKADVVVGLDPGVVEKLDADPKEKGWRAGGKYGLISFSK | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
A0A066W3I9 | MATHLRDRRRACISSSRHYYDTAPETHYHRVAHCVRSSGQSSTTHYTRALGPKQVKVRSYHPETTFKTYGITGIDHPLSKRGIHASSSDAAKSFLVSETGTHSDEVAHRTGYTSNGISNEYFHQRLNGIRVANAVANVAIKGNNGNNVLSYAGGTSGTTSQSSPTNIYDYIRNPNLTPSEGPNPDAARTNVFYIANMYRYGFTEKTWNYQQDNRGLGGLGNDRVEIEVQSNYPGLITVPADGRPAKIYLGTWSQGDGAFQNDITVHELMHGVVGRLTGGGTAKCFTTTEAHGLDEGWADSHGLDEGWADAFPNLIQRTSA... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 464
Sequence Mass (Da): 50859
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A0A833GHV4 | MPAMKQLLPDWLHPSLDLLTTAALVLLVLVLAWVLRRVLRGLARRLRERYQLSEQMMAVPLRVAGAVVNVGALFAILQLLGVSGAVLWTAFTGFAAVGAIAFFAAWSVLSNLFCTLLIVIMRPFRLHDRIELLEGGDKPGLKGEVVDINMVYTSLREDDGALLQVPNILFFQRITRRWPVPGVMPTAPVDNG | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A497TL94 | MDFESLIKEQNEMSKKIILKDCFKKPVKTVAGFDCCYRGNNQICAGVVLDYKTLETIEMKTVTGKETFPYVPGFLSYREGQGIISVYRSLKNNPDVIFIDGHGISHPRGIGLASYVGLILDKPTIGIAKSILTGVIKDDKLFLNGKQVGWVIRKGKRKVFISPGQKISLKTSRELVLHTIIHRIPEPIRLADRYAAKVKNEKLQSE | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-... |
A0A2U3K5C7 | MSWWSKKKPAEPAKAVEDRIRRRYQSFRDLLSLNNECLELMAAIQEDLQFVLPRRDIVGPRISGVYSKAEATVAALERLTGINFPQLHEAIHAQQDEVERYIAVRQELVAPNFSASLGEIDGASAAEVGGKAAALAEVKNRIGLPVPDGYVITAEAYRQFCGIPLWEKIRDATRNLDLNDLSALQEVSKRLAEMVMALPVPRAIEVALAERAHTLFSRGPTAGLAVRSSAVGEGGERTFAGQFLSLINVPQEQVVDAYRRVVAARFSERALFYRLSAGLSEIDTPIPVLCLRVIRARASGIMYTRDPGNPESDALWITAT... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 852
Sequence Mass (Da): 93742
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A0A220EYG3 | TLYFMFGAWAGMMGTSLSILVRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLMTSSMVESGAGTGWTVYPPLSSIIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDR | 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-cytoc... |
E1SKM8 | MIPTQLMQQAGVRRLAVISGDPAWCLDRAAAWREALPGDWLALSPAPLFSDESALHRQPGAVRTLLGREFHHAIFDARQGFHAEAFAALAGTLTAGSWLLLLVPSWQAWSQQPDSDSLRWADVAEPIATPHFVHHLQQLILSDDQVLLERQHQPCCFPAQRDWPQWHCQAPQQQQAILDQLMTLSSGVAVLTAARGRGKSALAGMLARQNSHCLVTAPAKASTEVLATFAGEHFHFMAPDALLALETPPPADWLIVDEAAAIPAPLLQALVSRYPRVLLTTTVQGYEGSGRGFILKFCAGLADAHYFTLDEPLRWSRFDP... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A8U0U4F0 | MLVSWVTFIQAFLILLVKGADQWSLRESSNCELNKKQSDLNSFLWTIKRNPPSYFYGTIHVPYTRVWDFIPENSKKAFQESNMVYLELDLTDPYTISALTSCQLLPQGGTLQDVLPRDIYRRLKRHLEYVKLMMPSWMTPDQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTEADIKTRGVPVLDLYLAQEAERMRKRTGAVEKVEEQCHPLNGLNFSQPSSNPQPSSNLQPSSNPQPSSSPQPSSNPQPSSNPQPSSNPQPSSNPQPSSNPQPSSSPQPSSNPQPSSNPHPPPTPNPPPAPNPPPTPSPPLTQTL... | Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading... |
A0A074VSC5 | AAPQTVTEEPKSTHQEHVIPTTQETFVTTTYPEIADPVDPCRNLTRNDLIKQRVVFSSNIFAINVAMLVFALFAPKNISGRWVLSFIVFIKSKDCISSIIGLLYLIYKAIKEFFKPPPPVESKWILSLIPAFSESEEMIRNCVFSLRDNDAQPHKQVMCIILDGKPRDVKQYMRITTTFKRKYVTSRFKRNEVVITAGFMEDVPVIVFEKVKNAGKKDSLILCHDLFNVMREDAPLYTKLLRKEIERNVLPSLVGESFPGFDMVFCTDADSVIHKGAVAGLANALVRDPKAIASCGLVLVELEAGAEWSYWNLYQQFQYN... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
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