ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A6V8P9E4 | MESRIEKTFKKTRAHGRLALMPYLTGGYPTLADCLEVPKLLADLGCDLIELGVPFSDPLADGPTIQRSIQVALSQGVNLDHIFELVRDLKTYADIPVCLMPYYNIPYRYWLGKFARKAAKSGVDGVIIHDLYIEDAESWRKVAWKEGLDTVFLATPTSSLERIKRISQLSKGFIYCV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 177
Sequence Mass (Da): 19941
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A0A836SRZ1 | IWNLVFIQYNRRGDGSLTPLPRKHVDTGMGLERLVAVLQGVRSNYDTDLFAPLIRRVEEISGMKYESEAAVAMRVIADHIRALAFAIADGVLPSNEGRGYVLRRLLRRAARYGRKLGFKEPFMCHLIPVLEEIMADDYPELVRHRSRILDVLQSEEESFANTLDRGIGLFEEVVSQVVGAGGSVFPGREAFRLYDTYGFPLDLTRLMAEERNLVVDEDEFGRCMEEQRERARAARGSAMREREKEVVSSLVEKALKSAFCGYETTETETSVVALADETGLVDRLPEGKEGEVLLAETPFYGESGGQVGDRGMIRSSAAEF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6... |
A0A354K7V9 | MSELVIVESPAKAKTIQKYLGTGFEVVASMGHVRDLQKSKLSVDIEHDFQPTYIEMKGKEDVIRDLKSRAKKSDRVWLATDPDREGEAISWHLAQLLGLDINQNNRVEFNEITKSGVQSGMAHPHKIDLDLVNAQQARRILDRIVGYQLSPFLWRKIRRGLSAGRVQSVAVRLVVDRENEIRAFVPREYWSIDAKLTAKSSRKIFTAHLAEVGGKKAELASGEEAQKILDRLEGAAFTIKSVKKRVTSRQPAPPFITSTLQQEASRRMGFQARRTMKAAQELYEGVEVPELGAVGLITYMRTDSLRISDEAKAAAAEYIK... | 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 ... |
A0A166J629 | MINKTFRELSKDFGLLSNGLTLHAESTLLLCEKANTTLNIGTSQREGIEIHVTQFDGTRFCDVMFEQTNIYCPDVIAHSINKRKAEYFVGRYLVANRLNELGFEYCTLESNIDRSPRFPCGAIGSISHCTNLACVVVTPSCCPDRENLGLDVQELISSDVCRDIESMIVAEQEVDLAVSVELTKEQAITLLFSAKEAIYKALAKFSTRGLNFTDAKLKQINQKTMEFELSESIKLRTNTLKEISCEYWYLAQHKAFLTLCYYSRDC | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A0A7LD20 | MADHKVVCWDCSSVVDDPYVNNCPKCGGLLTVKMDLRPVKEMRPEDLRKENIGVWRYAPFMPVDPSNKVSIQEGGTPLYKTDRLSKELGVSQAYVKFEGLNPTGSFKDRGMTIGVSHAKELGAKVVGCASTGNTSASLAAYAAKADMKCAVFLPSGKVAAGKLAQALFYGAKVLSIDGNFDDALDLALKMAEERKIYLLNSINPYRPEGQKSVLFEIMDQLRYNVPDRIILPVGNAANIWAVYKAIQELKEVGWISKVPKLTGIQAEGSAPVAKAFAAGKKDFIAEEHPETIATAIRIGNPVSGRKALHAIYDTKGFSTT... | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
EC: 4.2.3.1
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphat... |
A0A7C3IPR0 | MTSLRKQQRGSSKPKTDIVPLPKGTQVPNHIAMILDGNRRWARARGFEPWEGHKAGYEAVKKIAKAARDYGVHTFTIWAFSTDNWSRPKEEIDAILDILRQGLKEFLKEAKKEKIRLVHLGRKDRFPKDIADLLTRIEAETAHFDKNILNLALDYGGRDEILRAVRKIVEDKVPPEAIDEKLFESYLDTKNQPYPNPDLFIRTSGEQRTSGYLPWQMVYAEYYFEQDHLPDFTPDKLRLAILDYSRRRRRFGGNDKEKHFTFKPEVVARLELSWWRLSKVPEGTRFRDFVISYLKEQYGISKSLAKEAGKHLIEALTSGD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 438
Sequence Mass (Da): 51211
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M0II19 | MYVVLGDFDAVLHEDASREKQLQLLRAHPDLGERTEMTDASEAEQASAGLDSLSRSQYETFQRLNETYRERFGFPFVMAVKDENPDAIAAAMERRVDHSESTEFRTALDEVHTIAELRLAERFSSG | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 126
Sequence Mass (Da): 14327
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A0A1B6EIS6 | FETASSTMAFCLYELACNPEIQDKLYQEIKEVLAKHGGKPTYQALQEMPYMDKVINETLRRYASLSILNRTCIETYKVPDSDLVLEKGQRITIPTYAIHHDPEYYPEPFKFDPERFSAERVRERHPYVYLPFGEGPRMCIEVLFWWAKISKMKK | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 154
Sequence Mass (Da): 18208
Location Topology: Peripheral membrane protein
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A0A922HJJ2 | MIDPVGKIVLITGCDSGFGNRLACRLDRMGFHIYAGVLLPDGDGAKQLQQKCSNRLKIMQMDVTKPEEVNNVVEQIKQSGMPLWALVNNAGIGISVPFDWGNDIDVYRKVFDVNIFGVVRVTKSCISLLRQSNGRIVNVASLAARITSPLSSHYSMAKHSVRVFSDALRREIGSSSKMKIITLEPSFYRTDIINHDSMNRMRRKIFDETPEDIRENYGEKYFRIFDKSNQMTESIIKNDYEAVIEAMIMAVAGENPKLYYRCCNYYEVIAFWALSHMPEIIVDYSTLANDIPAWYKFMKHNMSSLSSKNQHYVGRAIQLE... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 591
Sequence Mass (Da): 68774
Location Topology: Multi-pass membrane protein
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A0A0G1W9P0 | MSSQKSKAPKEEKAAEEAGYASFLDKELRPSSWADYIGQQAVKNNLNILIRAATERGVPPEHVLFYGPPGLGKTTLAHLVAKETGRNLKITSGPAIERVGDLASILTNLSAGDILFIDEIHRLNKTIEEVLYPAMESGVLDIIIGKGPSARTIQLELPPFTLLAATTRVAMISSPLRSRFSGGVFRLEFYTEEEIAEILRRSAKIIGVNIEKGAEKEIAKRSRFTPRTANYFLKRARDFAQVESRPFDTETVNLSLKLLGIDEKGLSPADRQLLEVMADKFGGGPVGLGTLAAALSLLTVTNIWVKKCRPISRKNFYKRL... | 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 ... |
A0A915UG10 | MEHHTLWIVELVNRLLGPVVAPLLGKTYAPGLVVIPDHLVMCGLIVLAVTVFCLAVRSSFSVDNPGKLQIVLEDIVGFLVGLLKENVGPQGPKFLPLVGSIFIFIFLANAIGKVPGLMSPTANISTTLGCALTVWVYYHLQGIKAQGLVSYVKHFIIPPGVPLFVAPIMAPIEVISHMSRVMSLSLRLFGNVYGEELVVLIMASIVPFLVPLPMMFLGVITGSLQAYIFTLLTIIYLSGAVHVEHGHDDADHDDHHAHGDSPAHAHAAA | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 28923
Location Topology: Multi-pass membrane protein
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A0A1I2SPJ4 | MSKLVKSGIIVFVITALSKVLGFLRETFLAYQFGTSFETDAYFVALTPSTLAITFALSVSSVFIPLFVKNMYDRQEAHRFANNIIIIFFLVCIGLYLCLFLNGKAFISLIAPGLPDYAETLSIQMLKILFPLVFVSIAIQMYTDMLNSYERFSASAMSLLPNNLLIIFYLVIVGKDFGIGGVAYITLAAFLIQLIILYSLLRKEQYQFRLSQKVFDIKTKEFLILVFPVIISSAFSQVNAIVDRFIASNLSEGSISALMYSFRLRSMITGIFVTAIITVTFPKISKLALKLNKEELVNLTQDSLKMILLIVGPISAYLML... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 514
Sequence Mass (Da): 57847
Location Topol... |
A0A223PLB8 | MTNNSTKLLFLSTLMMGTILSISSNSWFGVWMGLEINLLSFIPLLTSNKNMMMNESSIKYFIVQAMASTMLLFSILLIQMKYPMGWETEFIPSMMISSSLLLKIGAAPFHFWFPEVMGASGWNNCLTLMTWQKIAPMMVLSYCIQLSTFIWTIIILSIIIGAMGGLNQTSLRQLLAYSSISHLGWMISSLTVSENKWXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMVVLTTITLYYYMRISFSALIMSYTENSWSMKMKSQKSSIILP... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A7R9I8C3 | VHHKFSETNADPHNSNRGFFFAHVGWLMTRKHPEVIRRGQQLDMSDVINDPVVAFHHKETVSLEALKSLKSPPRETLSLEALKSLKSPPRETLSLEAFKSLKSPPRETQSLEAFKTDRADVVHEAEWLHEVVVEPLHRNSKRLLSSHNSKRLLSSHSSKRLLSYFTSLKLLFCFFLPIMIPPFLWGESWYNSIMAIGVVRYVLSLNFTWLVNSAAHLWGYKPYDK | Subcellular Location: Membrane
Sequence Length: 225
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 25986
Location Topology: Multi-pass membrane protein
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A0A7R9K9W7 | MVCVIVPETLRKYTPFAFLERVCSKDYLEPVTGTVIEKGTTVYISLHGLHKDPEYFQEPERFDPERFSEENKRSITPFTYLPFGDGPHNCIGSRFGLMSVKCCLTHILAEYEVSKRPETPFPLEYSNKSIVLASSGGIPLKFKRVVAP | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 148
Sequence Mass (Da): 16807
Location Topology: Peripheral membrane protein
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A0A1B6GAA4 | GARQLSLDSVVPVVLLPALGYIAAQGVWISVVVFTTLPIFLTYVHYIIMRTSSQSKFFYVWTLMSVALIVTVFEVPVVVTLDIAPEEHKIFLLFTVVMVFCGVKTRLTAEQSHVKGDVKSDECDLECTVCHKSVLPRTFHCCICHTCVVKRDHHCAWLDCCIGESSLATR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 170
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 18992
Location Topology: Multi-pass membrane protein
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A0A543AT54 | MQVRVVSATLVASTVLVVVFGLVVASTIIGGMVQTKVETAINQVENSRTVVKRDLATVATAKEPNLDGQMKGLVRELAGEARQSGAPTVVLRTRGAEPIVVAWPAEPSVAEEQLPQDLRDKVLAGKMAIQYAGLNPDGGQERPFLAVGTPVYTDQLTYELYFLFPLDAENQMQTLVRTTLVIAGIALVLLLGVIAGLVTRMVVTPVRLAARTAQRLSAGLLHERMDVRGADDLAKLAGSFNLMAENLHQQIVRLEDMSRLQRRFTSDVSHELRTPLTTVRMAADLLYDNRDDYPAPAARSAELLHNELDRFEDLLAELLE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 510
Sequence Mass (Da): 55067
Location Topology: Multi-pass membrane protein
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A0A059CBJ8 | MRESSRRPNKKIRWSNLYTFPCFRPPSADPEPIKSLIGQPGFSRVVFCNKPHLHRMKPHKYPTNYVSTTKYNVVTFLPRSLFEQFRRVANFYFLLVAVLSCTSLSPFARLSQFIPLVIVVGISMLKEAVEDWHRFLQDLEVNSRVVKTHIGEGVFVEKPWQQVSVGDVVKIQKDQYFPSDLLLLSSSYEDVVCYVETMNLDGETNLKAKRCVEATLNLNEDDSMSKFEATIYCEDPNPNLYSFVGNLEFQNESHPLCPAQVLLRDSKLRNTEYIYGAVIFSGPDTKAVRNSMKSPSKRSRIEKKMDHLIYVLFSMLFLFS... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 663
Sequence Mass (Da): 75664
Location Topology: Multi-pass membrane protein
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A0A059CLB4 | MVSMFILPAMLHAFSSFGWSMAQNSHHRPHHIHVGAILDMESPVGEMAQQCMTMAISDLNASPSHINHPLKLILHPRNSMGQPLKALSSAVELLENEQVDALIGPQTSEEAELLGELGDRVPIISFSASSPLLSREKNPNFIRMTTNDNSQVGAIAALVQKFGWRELVIIHEDSSYGNGIIPDLLLALHEGNARVAHRTVLPPQARDIYVEAQLYKLMALSANIFIVHMSASLASRFFIKVNELGMMSTGYGWIVTDGIVNELPVMDRSVLDSMQGVIGIRPSIPPSERLHNFSMKWRNNFFTNQHHQIPEVNVYCLWAY... | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 828
Sequence Mass (Da): 91832
Location Topology: Multi-pass membrane protein
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A0A090P7A8 | MTDFAARLEKVARNPEVFKNFGRGVERETLRYKQGGNLATTPHPSGLGSAYSNNWITTDFAESLLEFITPVSQDIDTLLAQLEDIHHFTQTKLEGEKMWPLSMPCYVSDEDIINLAQYGSSNSGKMKTLYREGLKRRYGSLMQIISGVHFNFSFPEAFWDALHGEQDEEARQATKSAGYFALIRNYYRFGWLIPFFFGASPALCSSFIQGRETKLPFENIGKTLYLPQATSLRLSDLGYTSSEQSVLKIGFNSIEEYLEGSTARFVYLQLSLLRLALKWMASIVSSTVTCYKLKTNCMRQFALNA | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 305
Sequence Mass (Da): 34566
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A0A0M0T248 | MTYKAFTEQDAIDRVRTLGLIGNGPVEAEEIGDGNLNLVFRIREGEHRLILKQALPYAKVVGESWPLSLERAWIEQSALREFARHAVPFVPRVFHASHEEAYTVMEDLSHLTIVRSGLLAGEQYPLLAEHIGSYLARTLFHTSDFALGPVEKKRVARTYYNPDLCDITEKLIFTDPFHDAETNEIEAGLEEEVAHLWADDTLKREVAKLEALFITKGDALLHGDLHTGSIFASATETKVIDPEFAFYGPFGFDVGQFIAHLFFAAYPDYPALRDARIRDIDTFWLTFASTFRALWEREAVEPFQTSGLVDDVLSTILQDA... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 2/2.
Function: Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
EC: 2.7.1.100
Catalytic Activity: 5-(meth... |
A0A8T4IIF4 | MPTTGETAPTLGVEEEYFLVDAHDGGVRASASRVLARVAAPLSGQVSGEFTAYQIEAKTPPCRGLRELGDHLVRMRAGVAAAAAGEGLRIVASGTPVLGAREPVPLREDPRYDAGAREYRALQDDFAFSALQTHVRVPGRAEAVLVSNHLRPWLPTLAALAANSPYWAGRDTGYASWRTVALGRWPAAGPPPYFDGVDHYDRLVARLLDSGAALDEHNVFWDVRPCPHLPTVEIRVMDVNAGIAETTVFAALVRALVAEALERVRHGDPGPRVDQEVLRAAYWRAARDGCSGHGLEPLGGRLLPVAELARRLLAHVRPVL... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 697
Sequence Mass (Da): 74803
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C0RM75 | MTKNSSTVFTHARIATLEEKAANLGLIEEAALVVKDARIVYAGPENKLPDEYASFEKIDCGNRLITPGLIDCHTHLVHAGNRAHEFELRLQGATYEEVARAGGGIVSSVRNLRAASEDDLVRETLPRLDALIAEGVTTVEVKSGYGLDRDSEIKSLKAARRLGEERDVAIRTTFLGAHALPPEMNGDKAAYIDRVINDMLPAIAEQGLADAVDGFCEGIAFLPDEIARVFDAAKAHDIPVKLHADQLSNLHGAALAASYGALSADHLEYTDADGAAAMASAGTVAVLLPGAYYFIRETQKPPVEAFRAAGTKMALATDNN... | Cofactor: Binds 1 zinc or iron ion per subunit.
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is t... |
A0A5B8XHT1 | MIEKIDWQKCNNLIPSVIQDAKTLDVLMLGFMTIEALNLTISTNKVHFWSRTKNRIWMKGEDSGNILRLENIHLDCDGDSLLILVNPVGNTCHNGTKSCFNYKANFLSQLEEIIDDRVKNQVDESYISSMQKKGINKIAQKVGEEATEVIIAALNEKDVDFIGECADLVFHLMLLLKYKNLTFNHVISKMKERDKRKLKDENYEK | 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)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Subcellular Location: Cyt... |
A0A3B9T2M6 | MTEIFTAPTLEEAKQKAADAFGVPLSDITFQVIDEPKRSLLSGIFGKKEEYRVEARYTAPAVPETAAAAPVEAEPVSEPEPEIAETEVQAEASDEPEVSPEIQLEKMQIGAAYLESVLAQLAPDVTCEGRLENGISFTLQGESAGSLIGRRGDTLDALQYLTSMVANRGDKDYVRLTIDTCGYREKRKNALQELARRISKSVLRTGRSVALEPMNPYERRIIHSAVTEIEGVSSHSSGEEPNRKVIITNDAAPAYKKDDRNARGFRGNGRFDRNDRGGKRNDRGRRNNDKRDRKPSAEGPRKLDLSTSFEKDYKRPKPED... | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 332
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A0S8DA11 | MANFSYSKPLIIILLGPPGVGKGTIAVALEKKLNIPHISTGDLFRENLKNKTFFGEKAKNYMEKGLLVPDELVEEMLYKRLKKEDCNKGFILDGFPRNIPQAQYFAKIIKNKKITVINLEVKKNILIERITGRLVCKKCQATFHKTFYPPKKEGICDLCQGELYQRNDDKVEVVNKRLLEYENKTKPLIEFYKKNSNFYSVDGSFDKEKILKDILSKIKQIEFK | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A351ZEK8 | MDLCKMTVSQLREMLLARKISASELLSVHLERIERSQLNAYITLNDKAMEAAREVDRRISSGQELPPLAGIPIAVKDNISTKGICTTCASKMLENYIPPFDAGVVEKLRSAGAIIIGKTNMDEFGMGSSSENSAFGPVRNPRDPSRSAGGSSGGSAAAVCAGEAVLALGTDTGGSVRQPSSMCGVVGIKPTYGSTSRSGLIAFASSLEQVGAIGRTVADAALLQGVISGPDPMDPTCVIKAKPKYSIQGTLSGLRIGVPKELFGEGISDLTKDVVMRALSFMERHGAKLIPLSLPELRYSVSCYYMIASAEAASNLGRYD... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A960M1J4 | MKHTRKIGLLGGTFDPPHLGHSIMALDALEAAALDQVMFLPAAVPPHKRDRVLTEAGDRLAMLNLAVAGQAGFLVSDLEFQRGGVSYTIDTIRQLREMHPDVTWAWIIGADTLPELHTWKEIDQLLDLCELLTVYRPGVDSTTREPSSLRLSSSSAEKATRHWIQGHGIGISSTDIRARVRKGLPIDSLVNPAVAAYIEEHHLYR | 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... |
A0A8C8XBW9 | MKGFLFLLLTISLLVMIQIQTGVLGNTTTAATTSPSAASGGSVLLFLANILVQFFYLS | Function: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Subcellular Location: Membrane
Sequence Length: 58
Sequence Mass (Da): 6095
Location Topology: Lipid-anchor
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A0A655VYZ2 | MPYQSPITFQEPQLTVESLKQQLESFTEYQKQEFFDHHPVTDLVLGRSEYMDLLLHRLWQFFGFDELVEVSLVAVGGYGRGELHPLSDIDLLVLSQQPLSEQVANKISQFLTLLWDLKLEIGHAVRTVEQCAEIGKADLTVATNLQEARLLCGCEETFHRLKMVIHSESFWPSEIFYQAKVREQKERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLYEMSRFGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQVQVARHLGYFGEGNRGIEMMMKEFFRTLRRVAELNKMLLKIFDKA... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A8C8WQV6 | MYLFLCMLAVADLILSTTTVPKALAIFWFHAGEISLDGCITQIFFIHATFIAESGILLAMAFDRYVAICDPLRYTTVLSHAVIIKVGLAVVLRSFSVILPDVFLVKRLPFCHSNVLPHTYCEHMAVAKFACADIRVNVWYGLSVLLSTVMPDALLILVSYTLILNAVFHLPSRGARQKALGTCGSHLGVISMFYLPGIFTVITQRFGHHVPLHTHILLANICTLAPPMLNPIIYGVKTRQIRECVVSTLSSQ | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 27827
Location Topology: Multi-pass membrane protein
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A0A955KQL6 | MTVFQALLLGLIQGLTEFLPISSSGHLVVAQHFVGLAEASLPFDVFLHFSTLLAVIMYFRHRIIALKSKDWMMIAIASVPAVILGLLLKDWFEVVFRSYYIVLGTLFITGVINLKLGHMLKHSPVEASSEVTPKKALVIGLFQSVALLPGISRSGSTVFGAITQKLSRVEAFSFSFIMSIPVISGGSMLQLVSVYTSGELATIEWVPFLLGGAAAFLAGVVSLRVFRYVIEKARFEWFGWYCVGLVVVLVLFDIVPVL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 258
Sequence... |
D4YMD8 | MTTTTFRTEPFTCPSCVAKIETAVGRVDGVEKVDVKFNSSRVVVDHEEARASAASIRKIIDDLGYPVKSVS | Function: Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA).
Subcellular Location: Cytoplasm
Sequence Length: 71
Sequence Mass (Da): 7717
Location Topology: Multi-pass membrane protein
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A0A8J6E142 | MTVDCQRTHTMSKVLATLGPNTTKEDIRAYFDAGLDLVRINCSHLRDKDAKMAELITAIRQISDEVGVHIGILVDLQGPKIRCGSFANGPYVLEREQSFTFDMDLDTPGDRTRVGLPHPEIFKAIEVGHNILVNDGAIAMRVDAVDRENLVIETTVTQEGEINNRKGVNVPDTILQLSAMTAKDRRDLAFALEHSPDWIALSFVQTASDVQECQAMVQGRARVMAKIEKPQALENLVEIVETADGIMVARGDLGVELSLSQVPAAQKRCIKLARSHGKPVVVATQMLESMISRPVPTRAEVNDVACAVFDGADCLMLSAE... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 510
Sequence Mass (Da): 54922
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A0A0N5AZM7 | MPAVQRKTIDLTPLKKANIPIFFIVGGPGSGKGTQCDKIVAKYHLTHLSSGDLLRAEVKSGSARGSELNKIMENGELVPLEVVLDLIKEAMLSAVAKGSKGFLIDGYPREVKQGDQFESEIQEAKLVLFFDVSEETLVKRCLHRAETSGRVDDNIETIKKRLHTYITATQPVIAHYEKKGKLVKIPSEGTVEEIFKVVEQHLDKILH | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: ADP + thiamine diphosphate = AMP + thiamine triphosphate
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence ... |
A0A1V5TYA9 | MNIAILGFGTVGSGVYDAAQRTNGAVNVVRILDLRTFAGFEQLLTSDIHHITNDASIELVVETMGGVNPAYGYVMQSIEAKKHVVSANKQLICEKYAALTGAAAENGVQLRFTASAGGGIPWLHNLRRAKRCDEIGEVSGIVNGTTNFILDAMDRLGEDYGRALKSAQKLGYAEADPTADVNGFDAQRKCAISASIAFDAIVEAEMVLTEGIQHFNQAAASAARELPETKGRAVKLLMRAGRHEDGIYAYVAPALVRADSLEASVPSNYNLITLQAKYAGVQSFFGQGAGKDPTGTSVVQDILDIVEGCGRGAPRAARPR... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 369
Sequence Mass (Da): 39301
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A0A1B0UFF5 | GALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPM | 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... |
A0A401XJ19 | MTLFLTKELSNEFKIAILSRGYGRVSKGFLWVDDTSAFLEVGDEPLLLKKNLPNIPVAVCERRVDGVKKILQKFPDTQVVILDDALQHRAIVPDIKILLTTWNQPFSADALWPIGTLRDVKSRAKYVDAIVVTKTPVAATTAEKEKIISSLQKYSNAPIFFSHNHNYFFPPLPENKRDVVIVTTIANPSYVLNFLSQWNLKIIEKFLFKDHYPISHREWEAIFETCNRKDALCIMTDKEYVKLPSVLAEKFNNTIYVLKLTVDIENKIEFLNLITKKLSYD | 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... |
A0A1E5B4X7 | MFIPMSKPTQFFDNELRAHLPSLGVRFNINITSFDHKTFDSSWFKHTNIHQPVKISRSVKTRQAEYFAGRYLAAVKLKTLNKEDHQLTSYPDRSPAWPSETIGSISHAEGVLAIVVETSLQNNKENIGIDIQPKISRVVAEEIGSIVATPEEVDVALKQGWNMEDAIALLFSTKESIYKALMVFSETTLDFKSVRLCAIDKASMQFELSSEVTLKQGGLHSLCCDYQYLESHQVYLTACYCFLE | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A192IHY6 | MVSSGHPSSSCTEPAETDPRRPKPGSGLYVVATPIGNLGDISERAREILASADLVLAEDRRMAARLLQHIGARTTVANYHEHNAARARPDILRRLAEGQVIALTSDAGTPLISDPGYRLVDEALEAGVPVRAVPGPSAVIAALSVSGLPTDRFMFVGFPPPKQAARRSFLAEVAGIAATLVLYESPRRLPDCLRDMAAVLGDRPAAVARELTKLHEEVRRGGLPDLADHYAAEGPPKGEIVIIVGPPAAAETDWAAIDRELADRLTRESLRDAVDAVAAGSGAPRKAVYRRALALKDGDGGA | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 302
Sequence Mas... |
A0A401XNK3 | MNVNSNGYTFTFAAVMVIIVAALLSFTAISLKDKQQKNIDLEIKQNILKSIGVNVERSEAEKAFDQYIKKSLVVKNGQEVEGVDALKVDLADEIKKPGEQRLNPLFVAEKEGKTYYIIPLRGKGLWGPIWGYIALNEDVETVYGATFDHKTETPGLGAEINTAGFQSQFANKKIMKGDEFVSIEVRKGDASGDYQVNGISGGTITSVGVDAMLKDNLRNYIGFLKSYNK | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
A0A922IE72 | MSSLVWSSLRNQTLNSSSFEEFFFRKDKRKSLYVCFQLFIILDQFESIESNQIKSKTCRMKINHHQDNCFTNCLSSSLPSSSSGGGQQQTSDGFHPIRYSFQKQPFVIGVAGGTASGKSTVCSKIIKRLGPIDPKSIYLSHEKRVVRISQDSFYRKLTDEDRQMVDKGMFNFDHPSAFDVDLMVRTLRDVCDGKMVRVPIYNYNENEISDKEEIIYPADVILFEGLLLFYFPELRQMFHMKIFVDTDPDTRLSRRVIRDVKERNRDLSLVLAQYLNFVKPSFEEFCLPTKKYADIVVPRGPDNEVAVNLIVTQIHSVVDP... | Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 637
Sequence Mass (Da): 72143
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A0A836STW6 | MFRVLQRYRSRRRLIALWKECRHFVNARGDICDPVVLQQLESAMDQLRDALQRKNGAGAIDAATRCAFLLGKACPRKPFARLRENAEVLAVALAVAMGFRTYFLQPFKIPTGSMQPTLYGITVTPAERPHFSDRFPLNIIKLAFFGERFVSIRAKTSGIVSANDVRFEIRTRQIVFYIARIPHKIHRNMIRHFQLGQYVHRGQILATGRMHYGDHIFVNKVAYNIRRPRRGEIIVFNTDHIRYPGVMTNTFYIKRLVALPGERVSISPPNVLIDGHRLEHPPVFTTLLHDVRAGYSGYQLPNPIPGAPPPVLGTVLDSLT... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 372
Sequence Mass (Da): 42517
Location Topology: Single-pass type II membrane protein
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A0A1V5TXS2 | MQFLLWSAVAAAGYLAGSANFAIIITRWFLHKDVREHGSGNAGTANVARVFGPWIGLLTLAGDVGKTMAAMWFGSALLGTGGMCAAGAACIVGHCFPLYFGFRGGKAVAVTAGVALMLDWRVFLILFALYAATALIIKKVSVASLLAALALPLVMLLLGGFAAAEVLLAAFAALAVWVMHRDNIRRILQGEESRFRFGKRKE | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A8J6AXD0 | MLSRVSSSFTSGAFARFASVKYFTKTHEFIDVEDKIGKVGITQYAATHLGEIVYAELPEIDAEVTKEEVLCAVESVKAASDVVMPVAGIVTGVNSELESRPAMINEDPFLGWIAEVQISDLEELDGLMTQADYQEYLQHCDH | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular Location: Mitochondrion
Sequence Length: 142
Sequence Mass (Da): 15635
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A0A833D4D4 | SPLYKNTILQSDALQKLLGDDFDLHIAMRYWHPRAEDIIEKLKKNPPDQIVLLPLYPQFSTTTTGSSVDEWMDLQRKADLDIPVHYICCYPEDKGFVSAQAALLEDTLRANQKAVPYRVLFSAHGLPKRIVDGGDPYPKHVELTARAIVERLDQPSLDWRVCYQSRVGPVEWIKPYADDEIRLAGREGVSVVLVPLSFVSEHSETLIELDVEFKKIADASGVPLYLRVPTVGVAPSYIENLKDLVFQALVDSPLAISPKSTLCKKCISPCKGAYCA | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 276
Sequ... |
A0A922L681 | MSIVERLEMAMAITILNGNLMPRIRLIIFICLGLWALLFLLNSFSLVNRNLINYYSIQYMPFINDTTIVVDKNGNVTTEITYHQLTQYVQLSSDKVQNFRIILFWTKYFDQDLMYQMKKSLNGDTENLLFRPKPCYYRYPNCLVTTNRDFIATAKVIIFHWRDFHYNDLPAQRNSNQLWTIYNLEAPPNTALLPDRDDLIFNLTATYRHDSDIYVPYGQLIARNHDFDLESNIDIRYKIKPVVWFVSNCHTQSHRENYVQKLSRMVQVDIYGKCGKFQCPHSHECYQKAAREYLFYLSFENSLCKDYVTEKLFNVLNYDI... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 425
Sequence Mass (Da): 50332
Location Topology: Single-pass type II membrane protein
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A0A1I8ISR3 | VSSTEQLGPLAESLLDTLRSASRDASAKIEATRQRTREEKKRLAMAQRQKALQNLKMSTNSKGQVRASLSAVGTLAEDVKEESGLVCCICREGYRHQPVKLEELEARPRKTQGISTVTAFTVIHIECHVSAVKHSRERGEWDSAFLHNGNVRCNGLLPLYGPAVQALGFASCLSRHHSCLQRSFSDETLGGGRQSNAQLLPYLLHLGLHLFSAKDGEAKEEPLQRQYLEAPAKSWLEASWTLDGPYYRCAMSFFLHGPRQWAANRLRHLRRLLYHAHAAATTPVGSAALASTEPRTGSPEDYRTVYKPALMFFGLIDSYY... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
A0A655U9S2 | MPISTPQEIIEDIRQGKMVILMDDEDRENEGDLIMAAEHITPAAINFMATHGRGLICLTLTKERCRRLGLNPMVQDNNAQYTTNFTVSIEAAEGVTTGISAADRARTVQAAVAKEAKAADLVQPGHIFPLAAQDGGVLTRAGHTEAGCDLARLAGLEPASVIVEILNDDGTMARRPDLEVFAEKHGLKLGTIADLIEYRNHTETTIERVAXXXXXXXXX | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
E... |
A0A151JVP1 | MYLNIYRLLSRTCVRQIHTSVSRNLMKDHSDNMFRKKLRSTAFYWSGVGVLVVGLSYSAVPLYRMFCQAYSYGGTLSVGHDASKVSTMTPIRNRKIKIMFNADVASSMQWNFKPQQKEITVIPGETALAFYTATNPTDNQIVGISTYNVLPFEVGQYFNKIQCFCFEEQMLNPHEQVGVLDIDICGPSQPRVLGALGEQVHQSGSGWSPVYIEDNLSLMSIGFLLSSPSDAVIWRGPKKNDLIDNSAEIFPALSGGARTMSNELNVEFLGSIPLDPLLARCCDEGKNFLTEMPDSPTVNVLNEICKSIIRKCEEKENCPN... | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 323
Sequence Mass (Da): 36051
Location Topology: Single-pass membrane protein
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A0A8J6AVL1 | MDRPRDSQKTTRDKTETHFVKWREYNMADISMKKTPLFNLHTRLGGEMVPFAGFAMPVKYDGVGIIESHLHCRNNASLFDVSHMGQVKLGGKDREKFLEKITVCDVTHMAPHQTKLSVMTTPEGTIIDDMMITRHDDHCFLVLNAACFAKDSAHIKNMIKQLGMDVTFDDISPDRALMAIQGPKAARSLQNIVKANLAQQPFMSQRSDEFKGEEILVSRCGYTGEDGFEVSVPNALAEDFAQSLLDQDGVAPCGLGARDSLRLEAGLCLYGNDIDTTTTPIEANLTWLITKRRRAEGGFIGDNVIIPQINDPKLVTRRRV... | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
EC: 2.1.2.10
Subcellular Location:... |
A0A510ZIU3 | MSVMRFVGETSREAMRKVRSALGDEALILANRPTETGVEILAMADEAAETMVASTLPESTAPAPAEPASRPPSEPAPTSAAPDGGGLEAMSERLLREMQDMRALLARGAASPAAPTTSSSAGRETLAETLRDAGFGRVVIDELLQGLPAELAGAEAEPAAAQAWLSRRLAGRLPVGIDPETFLDTPGILALVGPTGVGKTTTTAKLAARCVQRHGAEHVALVTTDGFRVGAHEQLRIYAELLGVPLHALSPEQSMDELLAELAGRRWIIIDTVGMSQRDRRIIAQASQLQGGAERVRMLLVLNAASQPGTLEEVVTHYRQ... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 743
Sequence Mass (Da): 79315
Location Topology: Peripheral membrane protein
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A0A182JNR9 | MIAAFQSYLERLPAETKLKILRLYPDLAGKMLDTNQLSEDSTNEHASVGLDNLSPEDKKKLTDLNESYKTKFGFPFVVCVREASKFEVILRSVSERIHHTVEQELEIALEEVKKICRLRILQLVDNL | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
Function: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (... |
A0A9D4SHS2 | MFIVLSKSFLILDKDEVVSSQDNNNGQKALIVYDLKRDSSKSIQIDWCPSTEMTKNDADDVKKNAKEPIVSFNTGTFSNLHDFVAISDDLKNVIIFDHNFHKINQFKIKKNAQKMIFTKNEEKILICDKAGDIYEFDVKQSSSSNEENCGRLLLGHCSMLLDFLITDDQRYIISADRDEKIRVTHYPNTYNIKTYCLGHSQFVSSIQLINQQTLASGSGDGKIKIWNYLNGKILYTHDFHEQQQQQPTSATNGRNKSAVKSDFAIKSMTIDRPNNGRYICVSLLSQSILYLFKIQYKNDDEHQFESLDVITQLRFNQIPL... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Location: Nucleus
Sequence Length: 418
Sequence... |
A0A836WMY4 | GTQEQVLEKLRLFGLRTTSRYWKCRDIDGCLRGLDELRSLKEEFPFQIDGGVVKINERELYHILGSTAKSPRWAVAYKYEAEQAETVLKDIIVQVGRTGVLTPVAILEPVAVSGSTVSRATLHNEDEIRRKDIRIGDHVRVEKAGEVIPAVVAVIKEKRVGKERIFHMPRKCPVCGEPVTRREGEVAVRCENLQCPAQLKRWIGYFAARGAMDIEGLGEVLVDQLVDAGLVKSPADIYRLRKQDLLKLERIADKSAENLLRAIGQSRNRDLWRLIFALGIPHVGVRTAQVLEEEFGSLDELAGADLARLTRIPDIGPVVA... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A1B6GEA6 | RLIKHLLIVLLFLTAFTMLYGFYIHSFKYQRGTEIEIAMKEETQQNKMKVTSPLIQLRNTINYINMMQEIKNFDGHLTDRTVLLVIQVHKRIAYLRGLIESLRSVKDIRSAILIFSHDYFDEEINKLVNSIDFAPVMQIFLPFSIQLYPDEFPGLSHNDCPWNLGIEKAKQLGCQG | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 176
Sequence Mass (Da): 20565
Location Topology: Single-pass type II membrane protein
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A0A090P4W0 | MGCCDAPGLMPIEEAMDKMLSRIKPIQTTLQLPLAEALGYVLAEDILSPIFVPPFDNSAMDGYAVRINDLAESNTLPLAGKSFAGQPFEGEWAQYVRAYHDGSKNP | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 106
Sequence Mass (Da):... |
A0A1B6EN97 | MSLSRCLLATLPLLLLAYFPAVTVSQENLIDDGSDASPPIFCYQCNSGVDLDCANLQANSTNSVHYKPCSDLGEYKGAKPFCRKIEQTIFERNNMVRIIRKCGWEKHPKLDCYNLANDDHVEIVCQCFLDGCNSAHHFSAAGAAMAMLLGLCHILVS | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A0A384XV07 | TKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIERVLGEQDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEALFKAQAETGEIKGHYLNAT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 237
Sequence Mass (Da): 26530
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A0A928KVK2 | MYTAIVVVQALTVAAGIMVFAELLMKTKPVFAGKFLYVAFACAVFDSIGYLMEITSVSRGGAITAVKIEYVGICFGMLMLLIYIFQVCKVKSIMWFYLLLFILNVATVGIVMTCEFHDFYYTSIEFETDWLYPHLVLGKGPWYGMHFMIMAIMVFSIIIVAARRYIISAKTEVKESSFLSVIIFVGVVVIFLIIAYLMGVLGYFDPTSMLFVWVCIFIRYNILDITPSAVETVSDVIQESLIVVDKNYIYVDSNREARNVFPEFEAKKFERMKIGDYSSLLEDIFTCDSEREFKIGDRYYRSNVVPIYGNNKNITGYTAC... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A443J101 | MVIYMDVIWLLNFLADSLLLWITAIFLKRQVKIWKVLAGGLMGSCLILFALTPLASVASHPVMKMGISICMVLTVFGFKRFKSFLSCLLTFYFSTFLMGGILMGTHYFLTYDLKLRTAVSLEGLRGFGDPVSWLFVAAAFPIAWHFSRKRVEDLTISSIEYDVLIDVTIQINGLDLQLKGLIDSGNQLYDPISKTPVMIAAVSTFKDQLPEEILQLSDKNNNPIELADKLPEIWSEKMRLIPAKTLGANNRLHCAFKPEAIYLQMEDERKAVQKALIIFTDQELSSDGRFQCIVHPAIVEQAVVQTAS | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
... |
A0A8J6AV05 | MYNLELERAVAFIEESKLEDGAKVALQLPDGLVAHSGTIIAELSSHFPQLRFIVIANTVYGACCIDDAAAVALNASVLIHFGHSELVPSSMLLLPVLYVRVTIAVDVPAIVQAISAFFPSDKPLALLSTAQYLSALADIHAALPWTTVPRTPGLSAGEMLGCTVPPIPDGNVLVVCDGRFHLEAIGIAYPDATLYRFDPFNHKIYREEFESGGLAPRVEMVERLRGRPLGKVGLLHGTLGRQGSLPLQRKLVNLIHRKGGEAVVVAMSLTDVDRVQGIAQGLDLIVLLSCPRLAIDWGSQFESVGVPVLTNMEFAALVDE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which ... |
A0A922ICY7 | MANDDQNNDVLEREFERIVKDCVEKSKKQSNRSTLIASIFYLSVLFLIGLPIWYRTTTPERWPLPDISWLMVRSQTLTHYYKISIIHLNESDESFQNIDLRNYLHANHHTRISFDNSLSFRQEWTVRSAFNNELMAFKSIRNQDSFELNDLDQLLSADNIQSINSIMFYILPRNIHTDRFINAGRYRSYFIDLNHLDNICGQVDIVECLGEQINQYVHQVQMLITRFYSHQADKQEQNIVLLMARDFDFLFDIIYEDDHVDKNLNLNERKERHRKWIKQIDQLLERFYTHRFSFSQYFRINFITQVLHYVFPRDNFIQSK... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 573
Sequence Mass (Da): 68279
Location Topology: Multi-pass membrane protein
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A0A448TUE6 | MFFHSWSDFINMGGYGFYVWLSYGLSFLAIILLIAEESWRRKALIKEMQRAEQREKRQKMRGSV | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 64
Sequence Mass (Da): 7708
Location Topology: Single-pass membrane protein
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A0A9D4SHV0 | MTRISGHKSLVYKECQPQFSIFDWELNSSLKWMEENWHYSVYVSIAYMLVVYSIQQFMRQREPFKLRNCLAFWNLLLTIFSMAGSYYMLPEMYDTFYMKGINHSVCISSTNSIAQYWMWLFALSKIFELGDTVFIVLRKQKLILLHWFHHVLALIFTWYSFGQNISLGRWFVTMNMVVHSLMYAYYAFRSMQIYIPRQIAMTVTSLQIIQMIFGFYVSGYAFFSKLSGNYCEIPAKTATFGFISSSARCYISK | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 253
Sequence Mass (Da): 30010
Location Topology: Multi-pass membrane protein
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A0A951SV43 | MSSSTGKLFKITTYGESHGPGIGVVIEGCPAGITIDQEWIQRQLTRRRPGQSSLTTQRKETDTFQIQSGVYEGKSLGTPISIFVPSTDIKSGDYYKWADVYRPSHADYTYHAKYGYRTPIGGGRASVRETIGRVAAGALAAQILKQEFDTSVIAYVDSIGTISGNGYENPPSSIEEVDSSIVRCHNSKISDKMITEIEAARKAGDSLGGTICVIVRNVPPGLGEPTFDKLEAELAKACLSIPACKGFESGSGFAGTRLRGSENNDVFLPKNDTSSTTELNVDLSADSFTEDTEKVGPSYKPNPVHGIANVPEVTTKTNRS... | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 325
Sequence Mass (Da): 347... |
A0A517YYU6 | MLTNLTTLALTSEQLTGGIVLMIVGMGVVFSALILLLWAIKLMHAMLNKPAPAPAVAAASVPVASAKAASDEIEPETLVVIAAAVAAIVRKPHRIRRVDSLTAQQAGSNWARHGRRAIMTSHRPTRR | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 127
Sequence Mass (Da): 13477
Location Topology: Single-pass membrane protein
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A0A2H5VX30 | MIYERVTEELKERFREAWAVAVLTGAGVSAESGVPTFRGGGGAAVWRGMPVEKIATPEMWRADPVTFWQWYAYRREVIGRAEPNAAHRAIAAWERRFERLTVITQNVDGLHQRAGSRNVLELHGSLWRVRCPQCGVKMEDRRVPLPEIPPRCPSCGGILRPDVVLFGEAVPEAVFSQAVAATATCDLFLVVGTSAIVYPAAALPVLAKQNRAFVIEVNPETTPVTEIADVTILGRAGEVLPRLSPEGNGGG | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysy... |
D9USA0 | MRARGGRAGPRPRPGGGREPPRPPRGDRRARPDPARPGRGRGAAGPRRIGGGDGRALLLTGPAESAGLPVRTRGRCGKLDIMRTAHRVETVRAAETLLMDRLPDGALMARAATGLATAAAELLGRVYGSRVCLLVGSGDNGGDTLHAGAALARRGAGVSAVLLSPGRAHAGGLAALRAAGGLVLEAPEAAGESEVPGEVTRRVREADLVLDGIVGIGGNGGLRPVAARLARTAYEGRPAILAVDLPSGVDADSGEVNGDAVRADATVTFGTYKPGLLIDPGREHVGALRLVPIGIEPGAADLEALQYADVAALLPVPGVE... | 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 is a result of enzymatic or heat-dependent h... |
A0A7R9JXT5 | MGVKVNDLIPMHSREPTITMMTGGGEGTKQGKAITNVTKAHKGCPCSSEPSPRRGTNNAHLDPTARTWMMPKTNKDVFQRSWGDVGNETMDPYKGNETPESDNGRWLALKAAPRLVKKETRHHVPGATPGIPTMIIYMSYKTVDLVKTRRHFTQAKCVRLSWDVVSDVSDVSDVSDVSSVSDVNDVSDVSDVSDVSESWYDYKLQWDPKEYGGVEMLHVPSDHIWRPDIVLYNNADGNFEVTLATKATLNYTGRVEWKPPAIYKSSCEIDVEYFPFDEQTCVMKFGSWTHIDEVKDTNIVEIGVDLSEFYTSVEWDILEV... | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 476
Sequence Mass (Da): 54027
Location Topology: Multi-pass membran... |
A0A1I8IXC5 | SDESFIAYAAAAPNLALIKYWGKRDSRLVLPLNNSISVTLDDQLMRTVTMATASPEFAEDFVELNGKPVEVTDRMRAVLQSLRQRCQRGQDLASWKVRVATRNSFPTAAGLASSSSGLCAFAVAVARLADTLRWLSTVARLGSGSACRSLFAGFAEWSAGQRPDGVDSTASQLASAGHWDLRVLVCVVGAGAKSAPSTQAMARTVATSSLLPARLSCLPDRLAAVREAVAGRDFASLAEMSMRDSNCLHAVCADTYPPVHYLTDASRAIIDFVHRLNEASGRVVLGYTADAGPNVCLLAQPADVHLAAGCLQRAFDIGQV... | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Function: Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and s... |
A0A840I1F7 | MIADHVSGQPFPDLSDQERSLLSRFDELLVETTAHTNLIANSTIADRFSRHYSDSLQLLPLIPDDARTLLDIGSGGGLPGIPLAIVASARRPDLQLTLCESIGKKANFLRTAIGELGLTNVSVENRRAESIERRFDVVSARAVASLTKLLPIVRRRLTKGGLAILPKGQRAELELEEAKKEWRMNVERVTSHTDPNATIFLIRNLELCR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 23... |
A0A0N5ATL0 | MALYAMSNHYKFLTLLKHLWPLTVRRVSSFGGDLPDSEVLVPRHPCKSRINQDLVEEPPEFDQELVNHLERMSLVRFSNEEAVAHLRMAVRYANQLMQLDIENVKPLETVLEDLECPLRDDIADETLDRNDVLSNAEVTFEGYFVTPPGNIPLQEVSKLDLEKVNEWDWHAMSSQADSNKAS | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
A0A075JLW0 | MYIVTANEMYDVDELSIKEMNIEGKLLMENAGRAIAQEVEGLTSSEGFICILVGPGSNGGDGFVIGRTLLNKSYPVQVVQVVPNDKITGDALYHKNLYINCGGNVTLLEETENISTCLDNAEIVIDAMLGIGIKGKLREPLASLVSILNNKASCVVSVDIPSGLPADEGIQDFAAVQAAYTFTVGAPKMSAFLQHTAAYYGKWANVEIGLPRKAFNASGREVWEQDQFQKTMPPRQLNDHKGDHGRGLVIGGSSEMPGAFAMTLKAALRTGAGLITGATSEKVRSAIAGQTLEATYQILPEANGALTNEKSIDLAMYDAI... | 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... |
A0A1E4CKA8 | MKSSTKLLQSSPVAFGLVVMTVAMLDLWSKSAMIAWLTPARRTVEVTPFFNLRLGYNPGISFGLFPAESDLSRMLLIGFALLVTLLVVWLGLRSRVWIERLGFALIAGGAVGNIVDRGSDGLVTDFLDFHAFGWHWPTFNLADVAITGGVLVLLAASFIGDRFAQPSQDQTR | 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-, ... |
A0A7T5RP82 | MHESIQLTIDFEKFDSIEELPQDEQLLITSAREAMNNAHSPYSHFTVGAALGMKNGDIVIGSNQENAAYGSTICAERSALVAAGSLGRKEDIRKLAVIGTSKDFQTSAPVTPCGACRQVIKEYEDLSGEPLVILITGETGPIHRFVGIESLLPFAFGPKDLNK | 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: 163
Sequence Mass (Da): 17579
|
A0A0Q7PZM2 | MTSALLTEITALDDEVLTALQRIRAACATGDRQDPLDESATLRLKNRGLEGSRLWLIGDSGFALLHDEGVDLAVAPSARGAGFGTTLAAEAAPLTHSAWSHGDHPAAAVLAKRHGFDRARELWVMRRPVSSELPASSSTVEIRGFQPGDEAELLRVNAAAFAHHPEQGSMDAENLAERMAEPWFDPAGLLVSFDGDHMLGFHWTKRHSASTGEVYVVGIAPEAQGRGLGKALTLAGLEHLADRLTSDGEVILYVESDNLPARAVYEGLGFTHAPSDTHVQYRHPH | 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: 285
Sequence Mass (Da): 30644
|
A0A655Z0W2 | MLLFISSILVIVVIAMWPEIRTIQEGTKPIGMDMVIQMIMLCFGGIILLATKTDPRSVPNGVVFKSGMVAAIAIFGIAWMSDTYFQYAMPQFKSGIVEMVTNYPWTFALALFIVSVVVNSQAAVARMMLPVGLGLGLEPALLIGLMPALYGYFFIPNYPSDIATVNFDNTGTTKIGKWYFNHSFMAVGLISVISACCVGFVLSKIIIG | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 208
Sequence Mass (Da): 22641
Location Topology: Multi-pass membrane protein
|
A0A2R6KR17 | MPNWGDIGAVDASLAPVAHVTGTAYSGMDRRRAQLLSAGAFGLGVVVLWLTVDGGLEPVAGVGALACFVAAGYARSVQSARAGVVLAGGVVVALGTVGLAATLAPLSNVLLPDIGVLGPYTYLATEFVFGSLALGLLLRAGRGSLRRAARTIAVVYPLAYVWDWYTLEVGVFAIPLRTGVELVGIPLEEHLFMVVVPALVLGIHETLGERTEDP | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 214
Sequence Mass (Da): 22104
Location Topology: Multi-pass membrane protein
|
A0A1R0IQJ7 | MTNQRRRGYLEFIETVILAVVLAFLIRTFVFESYQVEGISMLPTLHTGERVLVNKLIYDFETPKTGQIIVFRSPVIKSQDWIKRVIGVPGDTISVKNNVVYINGKRYHEPFLKYRGSMNVPPTKVPPGYLWVEGDNRPKSFDSRYFGLLPMKNVKGEAFVVWWPLSDFHLLH | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 172
Sequence Mass (Da): 19961
Location Topology: Single-pass type II membrane protein
|
A0A8J7T3D3 | MAKLPKNQMRYWTLDDVEVAGKTVLVRCDMNVPVHKETRQIMETFKIEAHKETLTELSERGAKVVVISHQSRPGKPEFISLRTHTEVLTNILKKEVKFVEDIHGEKAKTAIGELKEGEILVLENLRFQEEENIQGEPEERAQTRMVKELSKLADLYVCDAFACTHRSHPSMVGFPHVMPSVVARLMEKELSTIETINGNPSPPMGYVIGGAKLEESFLIMENAIKKRLADYMLLTGVPSIVFLKAKGYDIGDSNEKFLAKNKYELAHKTAEKILRGNEDKIYMPLDLAIDKDGRRVEVDVDELPLDYPIKDVGSKTVEEY... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 423
Sequence Mass (Da): 47033
|
O84761 | MRPILLEEWSSLLLGMEIPRSGKKVTGVAIDSRFVLPGDVFFALPGNRTSGHLFLKQAAQSGAVAAVVASDYHGPSYGLQLLRVADPREALRAAGRTQGALFYGEVIGITGSVGKTTTKNFANQLLSSVYKVFMSPKSYNSQLTLPLSVLMADGDEDFLLLEMGVSEPNNMKNLLEIIEPTIGVITHIDVQHAVHFLDKGAQGIVEEKSLLLERCGLQLIPKDSSWFQFFAKKNSAADRFSFSMSNETADFYYRAIHSEGVLISAPDGDIELPAVFPYSPAYMNFIIAVALAWITNVPMDRLEQVSQSLFLPAMRFEQQE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A655TFJ9 | MPTQAPAKAEQTAALDVSDLNPVMDLNLSTAMEGVAVNAPQFGDFAVNQQVMPLHRVEPNYPAKALQRGVEGYVILRFTIDELGKTRDIEVVDANPKRYFEREAMLALRNWKYQPKIVDGQPVSQPGQTVRLEFKLNK | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A7D5QDI8 | MSKLNLAVIFGAKSAEHEVSIVTTFQAWEWIDKKKYNPFLIYIDQNNNAYLCPPLRKESYKDFINKVLEQNRRIDFVKGGIEMKGGILLKKRVNIDVALLTMHGLYGEDGKIQGMLDFFDIPYTGSGVLGSALGMDKVLMKEIFEKLGLKVVKYFWFYDIEYKKDKSLFFKRVDKELGYPVFVKPANCGSSVGIRKVKNRKMLDGAIKQAAKFDHKILIEEGVSGAKDINCSILGGYDPQTSVCEEVLTDEEFLSFEEKYLKGGKTKGMLGLSRIVPAPIPDKATKEIQRQAKMVFKELGCWGVARMDFLYQPKSRAIYP... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 375
Sequence Mass (Da): 42... |
A0A655YP92 | MRILVNDLGGCNPYLEKKLNFQRILLVRCFFSQIRAQSLILASFYFVLSCAYCIFAFLILNRMIEPIMSPYLTFDRQHWAQLRNSVPMTLSESDLKELQGINDHLSMTEAVEIYLPLARLLNLYVAARQSRNGVLHQFLGNTESAPPFVIGIAGSVAVGKSTTARLLKALLSRWENHPKVELITTDGFLYPNKVLTERGIMHKKGFPESYDIRRLVEFVSEVKAGQPNVTAPGFXXXXXXXXXXXXXX | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Sequence Length: 248
Sequence Mass (Da): 28070
|
A0A059A7I3 | LAAASDFSVARTFEALGGGGIRGGVRSGAVAKMIDDRDLGFLANFLGIFIFALVIAYHYVTADPKYEGN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
A0A0D8IF72 | MEKKRIVIIDGNSLINRAFYALPPLTTKEGQHTNAIYGFMTMLFKVIEEYHPQYIGVAFDKKAPTFRHKEYGDYKAGRKKMPPELAEQMEPLKEVLDALNIYRIEIEGFEADDLIGTLAKYCEGQDFESLIVTGDRDALQLTSSSTKVLFTKKGISSLEIYDDQKVVEDFEVTPLQFIDLKGLMGDKSDNIPGVPGVGEKTAVKLIKEFGSIENLVQNTEKISAAKLREKIETNIQQAILSKRLATIVTDVPVEIQVENLKVEEFQKEKVLEVFSKYEFNTLINKLVGAQKEEDIKEDYQEESSVDVIDIKGFEALSQMI... | 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: 896
Sequence Mass (Da): 102740
|
A0A0G0UMG1 | MTITVIGAGYVGLVTASIFAELGNKVFCIDIDQEKVDRLNRGIVPFYEPSLAEYINRNAKEKRLQFTTSYSQSVPKSQVVFICVGTPPRQNGEADLSFLFSAVEETAKNLAGYTLITIKSTIPIGYEDDLEAAVKKYARAKYEFASSPEFLREGTAIEDSLHPDRIVIGTSSQKAQKILLELHAPLPGERIVCDLRSAQLIKYAANAFLATKISFSNALSCICERTGADVSKVVQGVGADKRIGHSYLYPGVGYGGSCLPKDVLAFIAQARNFDYDFELLRAVDAINTGQIANFINKIRVALNLTEKQGKNLNGVKIAIL... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 434
Sequence Mass (Da): 47660
|
A0A9D4SLI1 | MSTIKPLIYLTRIEKFSSAHRLFNQHYNDERKNVDTFGKCTNIHGHNYTLEVTIKGPVNERTGMVMNIVDLKKIIEDNVLNLLDHKYIDKDVEYFFDNGQSPVISTSENICIFIWQQIVKHLPNTVKLHCIKLHETDKNKVKYYGESV | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Lengt... |
A0A9D9L3X2 | MKIRGIFLDREKSTEKSVTIAVPLPEKVIIPMTQCKGQECTPVVKQGEWVFAGTKIGDGSRMAPIHSSVSGRVAEIRNMYDSWGNECSAMVIEADSEQKTAPSSIPSCTDRTSFIDAVRASGCITLDGTAQDTAALLEKAHDADTLIVNGTESQQYITNDLRCMMDNADDILSGIKLIMQFMGIQNTVIALSADFKDAVSAMEKLAQGNEGISVMPLRADHPNGAEPVLVNNVTGRQIHHGETAADQKVLVLDTSTVAFIGEYFRTGMPMIKRRITVDGDLVRTPCSVEIPIGMPISEVLAFADTNLEAAEKLIIGGLMN... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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: 433
Sequence Mass (Da): 47134
Location Topology: Peripheral membrane protein
|
A0A090PCZ9 | MSEQNQSTDLALSGSSSDGALVAHNDLDHEGQNPDLDEKSSSKFDLAVGDLDLMRQIVLVLSISICVALIVMLFFWVKEPEMRPLGAYETEELIPILDHLDAQKTEYKLEGNTILVPTSEYNNLKLNLARAGLNQATEAGDDILLQDMGFGVSQRLELERLKLSRERQLSQAIEEMKQVRRARVLLALPKQSVFVRHNQEASASVFLTLKTGSGLKQEEVDSIVDMVSSAVPGMKPTRVTVTDQHGRLLSSGSQDEASMARRKEHELERKQEQALREKIDSVLIPILGFGNYTAQVDIELDFSAVEQTRKSFDPNTPATR... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 357
Sequence Mass (Da): 39855
Location Topology: Multi-pass membrane protein
|
A0A2I0LNS4 | MVQRHSSGDASTSPSLARATASKELDEQARKNIPGKNRGKRKADPSSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTLVIGSGLSMEEMIFEVADTHLFFNDLEECDQVHIEDVASDDNGQDLSNYNFSTDGFSGSGSTANHGSSVGVQGGVDWMQLVVKRWLSVSDLPRSAGNTRVVFLPGLLSPQKREALQRLRTDIEVLTDSWLETALKSLLLIQSRKNCVNILITTTQLVPALAKVLLYGLGEVFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEVAAKQHNMPFWRITNHADLVSLH... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
EC: 3.1.3.48
Subcellular Location: Nucleus
Sequence Length: 328
Sequence Mass (Da): 36361
|
A0A090PA17 | MSDQIQNDPFADRESENYENPIPSREFILEFLAQAGVPLNRNDLFEALQLEGEEQYEGLRRRLRAMERDGQLVFTRRQCYALPEKLEMVKGYVIGHKDGHGWVRPEGSMKKEDDIVLPHHQMKNIIHGDFVLVQPTQNSKRGRKEGRLVRVLEERNTQIVGRFFLEYGYSYVVPDDSRISHDILIPNDQKAGARMGNVVVIEITDRGSRSRGMMGKVVEVLGENMAPGMETQIAIRTHQIPHEWPEAVDKQVANLGEEVPEEAKVGRVDLRQLPLVTIDGEDARDFDDAVYCEAKKGGGWRLWVAIADVSYYVRPETALD... | 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: 540
Sequence Mass (Da): 61361
|
A0A833D0Q7 | MVALIKTTIRSCLVDAKSSLENAGIEEPLKCARLLLSYVLERPLEFIIGHPEFEISEKTCRDYRAVIHRRALGEPPSKIVGHREFWSRQFYVDVHVLDPRPDSETLIEAVEVFFPTLKSPQTILELGVGSGCLLLTLLLNHPTLIGFGVDKSINALQCAVRNVHHHQLESRAHLIQGDWCSALQGTFDIIVSNPPYIPSGDIRNLSPELSYDPLLALDGGGDGLSCYHLLSQQLQSLVHQDTLIFFEIGMGQHGDVEKLMSQQGFKCHQWFKDLSGLERIGVFQLK | 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... |
A0A2X1ZUX7 | MLLAIDIDNRTTDFAVFSQDDLIDKFSITTDKNRSVVEIKLTIKLILMDKNIELSDINEIIISNVVPELSSSYEIISRELIGKKPIFISAGVKTGLNIKCESPREVGSDRIIKAVAATRIYTENIIIVSASSITTIDYINAKKEFLGGLILPGINLLQDSLVRGSAKLPHVELKRPDDVIGKNTEKAIQRGLYYGYKKAVLGIIDEIVESYSLAKENTNILITGPYGHLLKLCKYDLIRDDDLGIYGLKIIYDLNKNKAS | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A951VX09 | MTLTEILHPLTSDDFIVDRKLTYIIGCSGGVDSVVLAHVYFGLYQAGKIDKLPVLFHLNHGLRLSSNRDQQFVKDLAMKLNLPFYTDTVQLNKIVRRTGLNLEEAGRLIRYRRMLKISQELDNSIAVTAHHADDYIESVILKILRGGTDRSFLMPAVTWLPIRRNKAVQVFRPLLKVSRSQIESYSARNSIDFRQDETNFSLDYRRNRIRQTIVPLLKEEGLEPATLWQQVNGSNQRFGKTNLKKDLSKVDFYKNDFNSIDYLCLPTELLNGVSATELKWVIDVAFHRLELGPIQGNYKSGVLFEILNQSKRGRIFIQTN... | 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)... |
A0A1I8IDJ0 | MNSIRVAQWLLSNGDSRSSATGFLGAVGTDEAGQLLFDLAGRAGLQARLERVSSKPTGICAALITGQNRTLVTRLGAALHFSDAHLASEPCQSLVNQARMLYIGGFFFSSNPGAIARLVKLEGPLIAMNLHATFLCENFANPEVSMV | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity... |
A0A090P5M8 | MFGAIFLLNTLKHTGAITTIRNGFTDISEDRRVQAIIIAWCFGSFIEGASGFGTPAAIAAPLLVAIGFPA | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell inner membrane
Sequence Length: 70
Sequence Mass (Da): 7341
Location Topology: Multi-pass membrane protein
|
R5VDV4 | MPWRIYLFFTYTQKSFWDIYRKSAPFTETNYNPTLGFGHNFVKDKRIAGVAFLQFEHESNGRDSIWSRSWNKISFMGLYAFKRNYTLQAKFWIPVMVAKENKSLPRYAGVGLLAATYTSNNERLNCSVVMIKRAEWNLSANWKIEVAYKIFKLDNQYVFLQFYNGYGESMIAYKYFQRCVRVGIVIKPNSFTIF | Cofactor: Binds 1 Ca(2+) ion per monomer.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Cell outer membrane
Sequence Length: 194
Sequence Mass (Da): 22997
Location Topology: Multi-pass membrane protein
|
A0A059DGG9 | MKKQSKNILCSSFTLFFLLALRSVAASSMPGEVEDEREFDYIPKSKKGPRHWGELRKEWEACKKGEMQSPIDLSSRRVKVIPKLGEIKRSYKPSKAILKNRGHDISLQWDLGSAGSIKINGTRHFLQQFHWHSPSEHTINGRRYELELHMVHVTTDPDVKNKIAVVGLLYKTGQPNAFLSKLMGNVRSMVDKKGERKMGAIDPREIKMGGKSYLRYMGSLTVPPCTEGVIWTINKKIGTVSKDQIKLLREAVHDYAEKNSRPVQPLNRREIHLYQPNEEATPN | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
EC: 4.2.1.1
Subcellular Location: Plastid
Sequence Length: 283
Sequence Mass (Da): 32331
|
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