ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A177DNS0 | MANVLQGGDGMMGGGAGGFPLEQWFYEMPVCTRWWMTAALSASVLVQCHIISPFQLFYSVRTVFFKSQYWRLLTTFFYFGPLSLDLLYHIFFLQRYARLLEESSGRSTAHFAWLLTFASTLLLCIAPIFSMAFLGSALSSTLIYIWSRKNPDTMLSFLGLLVFKAPYLPWVLLAFSLIMHGTVPKDEMCGIVVGHSTMVLPERHLPAAPPQPQPSIPTRLVDSSV | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 225
Sequence Mass (Da): 25289
Location Topology: Multi-pass membrane protein
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H9LEC0 | MLKETWNIGVILLLMVMATAFMGYVLPWGQMSFWGATVITNLLXAIXYMGNTLVLWIWGGFSVDQATLARFFVFHFILPFIIMGISIIHLLFLHETGSGNPTGLXSNTDKIPFXPYFXYKDLXGFXVMLXXXALLSLLTPYLLSDPENFXPANPLIXXPXIXPXWYFLFAXEXXRXXXX | 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 proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 179
Sequence Mass (Da): 20292
Location Topology: Multi-pass membrane protein
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A0A6V7VHG8 | MDILFAVVPYEKIPDLIDLNNQENKEIIKNNLNLMDSLINDMIKFNGIFYNQSILLLSGYRFIYRTNFYLIQPSRRQIFKYLLLAVKLWAKRRQIYSNMFGYLSGSILFVMAAKICLIYPFGELNFLLQKFFQIYSAWAWPLPLIIEDITNADPVKNFNDFWDFNKLKLNEESSKSGDKMPILTSLFPEQNTAHNVNEFTLKIILREIKEGCIFIVKIDS | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 220
Sequence Mass (Da): 25908
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A0A4Z2D8G0 | MLVLVLFLLVAPSLGVKNANVTRTIRFKGGVVKIHHDILLSETPAEYQFVIEERNWKHLAFISASMGDSKSPRKVPVKLTGKPYTYSLVLGNPSTQQAHVFVDIALTELLEPRPSEIYQADKQFVKFRENAYFYSPYSTDTQLTHIRLPKGQLLTYSATSIPPVINDNNIVYGPYESRPAFSVEPLVLHFEYYAPFVTVTEMTRLIEVSHWGNIAVEETLEIVNTGAKLRGPFSRLDFDYGIGQPVAANSLKTALPASAKDIYYRDEIGNISTSTVRNLLDSIEVTLVPRFPLMGGWKTRYTLGYNIPAYEFLYRSGSNFALVMRFVDHIYKNQFIRNLTLKIVLPEVVSDIQFEPPFPVYEQHLENMKTYLDTSGRTVIVCKAGNLIDEHMQDFKVKYHFNLLMILREPLMLVAAFLCIFGAMIIYVRLDFSIYKVIGFAFVFIIVTF | Pathway: Protein modification; protein glycosylation.
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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 449
Sequence Mass (Da): 51192
Location Topology: Single-pass type I membrane protein
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A0A6I9ZD37 | MSVSNISDDSLPGTLILTGIPGLEWAHIWIAIPFCTMYLVALTGNAALILVIVTDSALHAPMYIFLCLLSLTDLALISTTVPKTLAILWLYAGEISFGGCLAQMFCVHSIYALESSVLLAMAFDRYVAICNPLRYTTILNHTVIGKIGLASIFRSIVFVSPFIFLLRRLPYCGHHIMAHTYYAGFI | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 186
Sequence Mass (Da): 20433
Location Topology: Multi-pass membrane protein
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Q5BY57 | MYLMSVYFSFCFLLLFSICVSSSLADDATVLSEEDSSLLPTVTNEHDVYKGSPAVSVLVAFSKPAYGLYSARREMNFPAGEVSSLVASLANTNPPDKEQFRLDFIEGALHYPSYYDYRMQNFTRQRLQGTLEPGQEVCLIVFS | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 143
Sequence Mass (Da): 16024
Location Topology: Single-pass type I membrane protein
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A0A7S0SFB5 | APHRAIKARQGDSCTPPSLHRIMRLTSLAAVALLAALCSGGASLASAEEPYVVELDVVLSKKKGKKPAGGVVKIEVHPDWAPVGAARFKEIVGAGIWDWNRFFRVVPDFIVQWGIPGDKALTGVWQSKRIPDDPVLETNARGTITFATSGANSRTSQVFINFKDNAMLDKQGFAPFGKVIEGMDIVDAIYDGHGGDPDQGQIQAKGNQYLRKEFPKLSYIRRARLPGQMPSAVDSSEETTEESPEDKDEM | 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: 250
Sequence Mass (Da): 27189
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Q4RFQ1 | MLEALKALSVFFTENSLRTRRNLRGDIERRSLAINEEFAQIFKEVKEELESVNEDVQAMSECCEEMTNRLKAAKEQTQDLIVKTNKLQGEK | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 91
Sequence Mass (Da): 10565
Location Topology: Peripheral membrane protein
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A0A1Y5TKW8 | MIRMLNWLVAGGIATISCMLIAQVFFRYVLNSSLSWTEEVGTFLLIWVGVLGVASGLRSEDFIAFTLFRRSRIAAVRLLCTIISWPSTIAFSGLIAFYGWNLSFDRAYGPVSAAASIPLAWIYAIFPIGGVLIAALSIARFVRELSGKAQQTSGVDSGKDI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 161
Sequence Mass (Da): 17518
Location Topology: Multi-pass membrane protein
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A0A6V7VG66 | MLIYMENDIKKMFELFEEYSRCIYKVKLIKEYLPENYNKEIIHVSEENIPQQELLSKTNTKLFISHCGTNSLNEAMYAGVPLICIPYAIEQFYNSSLVEHLGIGKYVSLIKIVEEKEVKNEKFIVDFENAFREMMKENNVYQKAANKLRKNIHKDYKGEDKYPIKQHFLEIISKLIDEDE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 180
Sequence Mass (Da): 21389
Location Topology: Single-pass membrane protein
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Q4RUB5 | LQPLARWWRLLPKDAAKMPESAWKLVFYTMSWSYSTYLLFFTSYSFFHDPPSVFYNWKSGMSVPTDIAIAYLIQGSFYGHSIYATIYMDAWRKDSAVMVVHHIITLALICFSYAFRCVVPSGLSGGEDPRLTPLLLRYHNVGILVLFLHDINDIQLEFSKLNIYLKSRGGGYYLLNDVLSNMGSVSFSITWSVSVQGVRRSGPSRQLLSCVSVFACFHLPQVLVPSLLVPSQSAVCHLCVQHPVRPHHPLLLLLQRSALCAAAHEYLLVPVHRDFRSQGAEGEGGERRQGVRGGGGQQGSSGSALQISGRKQGRWCWTPHGCTGVSCTAAICQEKRTKHRKQLILSEKDDSCARSSPPR | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Membrane
Sequence Length: 359
Sequence Mass (Da): 40094
Location Topology: Multi-pass membrane protein
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A0A6V7UBE1 | MRYCTENQNDPECKPEWIITEGEIPEAPYGPGKGKGKGKKFPKFKKNAKKPPKKHKIKDPTEGLPNKYKKKLPPGKVKKMKKEHIDALRKNCPGNSCKEDKDEHRNSRATLADYDVALLKLAYPDKSLEEIDEYVETKMQRVYELKEIIYEKLGVHDFSKPADNGLYGHNLLTLEQAEAYIAQLNSSLEYSYAIPDESNGRRKRAGNLIYFKTSPTRKWPIGKPIPYGFDKSLNTRQRDVIRTCINEITSKTCVRFTETNLDATSERPPNISSIYFVRYPTTAYCGLSYIGVYTPSNPIYLSFLCNDMAGVACHEVMHALGVEHEHIRPDRDDSITVLWDNIDAQFLDYYVPADGSTYSSYGIPYKCDSIMHYSYKIGARDFGLHTMTCKVDPDINDPLMGQRKGLTQADVDAINKLYCFPEECTDNSNFCGAWATQGLCYCPSSGKPNCYMVQNCPNSCNFCNCTQYGD | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 470
Sequence Mass (Da): 53376
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A0A1F7UME9 | MKLTVSNYAELLDEVTPDAKGKVIPERIAKFLALVRKNRAWSQLPRIISAYETRVFKRQGIVRVTVRTPKPLTVSEEKKIAEQLGRDLKSIIWNTEVDPTLVGGLQLQIDDRVVRGSIRDHLQSLSKQLSS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 14861
Location Topology: Peripheral membrane protein
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A0A4Z2CTW3 | MIGSNAADDDDNINNGNADDDAVNSLTNKLNHSSFNYDIQTSYPPSDPEDILQLLKLLYQLPGLKEFYFNDINNDSDHTLLGDKSMKKIDENVFIDKNELFDVKMEYFTSTRLTNKLLRQIHDPLALASGALPNWCISLSQRFNVLFSYAVRSQLFSACAFGPARAVVWLQNRPLQKRTYVSHPDAYSRSGSAGSTSGRSSYRIILPSVNASLISALLNNTSATTSASANNTNGNHPLDDGASTSPNEDVVLLRPSILTHLLNIPSANSRAVNQNMNNVQQVEMNTVNNDFDTSFDQIPSFESILSNLGIPLPSTTTSSSLNCDTYLSGNIGGMRSTTTSNDLINCEEGTGLGPTLEFYSLLAAELRRRDGLMWVTDDFSLAEQSNQSHSILPTVSSSTTIKEHVISSTGNHNYSPDSETDDIDEENIYVNTPHGLFPAPWPGDQVPESVLYRFFILGITVAKCLQDNRRIDLPLSPPLLKLLTAYGSVVIPSVEDADNVELKSSEPNQNHSTNCSIDKVDTIIDDNSVDFSVLSDVESAFQNLLYSCSYSTNQPVSHFCQFTEKEFSQHDETFNLASFLISPQYKRLYQCCRKRSDNNTLKTSSHWISGLLNLNDFCIIYPERAQFMRQIAEFHRRKFILLTRNANEKEISDLAVEIFGCDLDDLCISMEFLPPSKLFGFSSYPLKDVYHWESNSTNATISMKCLYENTINNSQSVVVPITIHNIEKYLELTLAFCLDKGVRKQLDAFKDGFQRVLPLRWLALFTGTELGQLISGDSVAQWTREDLLAYTVPSLGFTKQSPTYQMLINVLSSFNSNERRAFLQFTTGCSSLPPGGLKNLHPRLRIVRKEITNSGPYPSVNTCVHYLKLPEYQSEKELRTRLLQATKEIGFYLN | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 894
Sequence Mass (Da): 100048
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A0A532U3K9 | MRVTMLQAICQKKERLIVGLMSGSSADGIDVALVRVSGFGKSTTIHTIAYDTLCFSSKIRELILKCSHPDTGRVNDICRLNSLLGELFAQAVVHIAKKARSELSQIDLIGSHGQTIHHLPSTEKISGVEVTSTLQIGEPSIIAERTGITTIADFRPRDMAAGGQGAPLVSYVDYLLFSHPEKSRVALNMGGIANITVLPAGSSENEVFAMDTGPGNILLDQLIYTITGGKNRYDLDGQRASQGKVNQRILERLLEHPFLRKPPPKSTGREDFGEVYLHWVIEMGKGTEWDDLITTLAEFTVRTIVNSLEMFVFPYHQIDELIVSGGGLRNFYIWHRLEESLPQQRMLTSDDFSIPSDAKEAIAFAILANETLMGQKGNLPRATGARHSVILGKIIPGRSV | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
EC: 2.7.1.170
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Length: 400
Sequence Mass (Da): 43905
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A0A533YMQ9 | MGRVFDTSSDREGGRGRANAAGVHITGSARDQMFTRMWAALVEFFNDVRSELRKISYPSRSETIGSTTVVIILVFIVSLFLRLADIVISLLIVKIL | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 96
Sequence Mass (Da): 10660
Location Topology: Single-pass membrane protein
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A0A934B719 | MSIQDLCRRIQPVDVNLQKKAQARLDRLTKPLGSLGRLEELAASYVAITGELKPNVPHAVVFTFAADHGVTLEGVSAYPREVTPQMVLNFLRGGAGVNVLAKHAGVDVRVVDIGVDYEFGTVPGLLDRKVMKGTNNLAVTSAMTRSQTEQAVMIGVELA | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Length: 159
Sequence Mass (Da): 17081
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A0A0D0PMH5 | MLSATSAAHPLSGLGWDEDRAADFHPLAEAGLLAGRITRIDRGRCDVLLVDPETGEPTTLRADTRPVTGADTVHNPCTGDWVAVDPAARPLPALTAVLSRTTAIIRKGAHKRSEGQVLAANIDTVLIAVSLAAEPDLGRIERLLALAWESGADPLIVLTKSDVVHDGEFVRADVEAVAPGVTVLTVSAETGAGMDALRALTTGSCALIGQSGAGKSTLTNALAGTDTMTVQQVRSVDEKGRHTTTTRELVPLPGGGAIIDTPGLRGVGLFGGEGIDLAFADIDALATGCRYDDCSHRTEPACAVRKALTDGTLPERRWESYLKLQRENAFIASRTDARLRAERARHHKSRTKAARTSHRP | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 360
Sequence Mass (Da): 38000
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F4LXQ2 | METDEYFMQRALELAEKGRKTTGENPMVGAVIVKDGKIVGEGYHKKAGGPHAEIEALKEAGLNAKGATIYVNLEPCCHYGKTPPCTEALIKAQIARVVAAIEDPNSKVAGKGFSQLQNAGIEVSVGVLKNKASKLNEVFIKNISEQTPFVIAKIAQSVDGKIALSSGKSKWITCDAARKKGHEIRSMYDAILVGIGTVLADDPILDCRLANNAANPVKIVLDSSAVIPIESKLLQGKGKVILATTAQADKGRLQKLEEMGADIIMTSQNKVNLNELLKALYNSGIYSILVEGGAKVFTSFLIEGLLDKLIVFLSPKIIGGDGKDYVENLFLREMKDVYDFYIDDAEKVGEDIMLTMYSKKG | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 361
Sequence Mass (Da): 38995
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A0A533YUU2 | MDMMVRDTLPVVFLVGPTAIGKSRVAISVAKALGTEILTADSTQVYRGMDIGTDKPTPAERERVPHRLIDLVEPDEPFNVGLYRRLALQEIARLHAEGRMPLVVGGTGLYVRALAYGLWEGPPADWGLRRQLLEEEEAHGSGHLWRRLAQADPALAATLHARDRNKIVRALEVAIRTGVPLSEWHDRHQFRERPFPSVMIGLTMDRSALYRRIDARVLREIDDGLVEE | 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)-dimethylallyladenosine(37) in tRNA
Sequence Length: 228
Sequence Mass (Da): 25621
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A0A1Z9VQ51 | MLNPIENSILQSIQPHCAIRVAFSGGIDSTALLLACLSLKQQKYIHYFDVIHINHQQPHSQMMAKHCQKLCDHYHLDLTIHNIDTKDTSNEGVFRTLRYQCFQKQTPLFTQILLGHHMDDQAETFLLKALRGGHNESMASMRNQTQLYHRIYIRPFLKIRKHDLTQYIQSKSAHWFEDPTNQSIDPCRNYLRHTILPALVKKWPDAIHSLSQSAAHAHQQFESQKKEAALFQMNQWLKKHSIYLTLKQLETVLHQFSSASPDTSPLFQYKDRQIVRFKNKMFIIQPQALLWEPIQLSPSQNEYRLFENIKIKLIPSNQGIPKEHLEYISLRPKRLLGNNQLSLGISHQKIKKYFQQLQIPTWVRSHYPLIFHDLTFIGLIDHNKQAKRHGDHCFTLTMEPSYHSWLYSIPQMDLSYLVDSITP | 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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 423
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 49683
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A0A953BUW1 | MIVTIDGPAGTGKSTAARALAERLGFEYLDTGAMYRAVAILCVEDGIDLESDAAAARAQARPITFVDGRTLVGDRDVTDLLRTPEASRAASLAARHPGVRAALVEQQRVIAAGRNIVCEGRDQGTVAFPRAGCKFFLTASPEERARRRQQQLERAGQAVPFEELLRQQRERDERDASRSVAPLRPADDAITLDTTRLTSGDVLDQLEAHVRRRMD | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 23479
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A0A7W0FDA3 | MGIFEFLYYLGCSAKKHYSLKYQKRLPHKVISIGNITAGGTGKTPAAIAIADEAKKRGFYPVILTRGYKGKAKGPCFVKGRNPLSVMRNGLKNEVNASRITLHASRLYGDEPVLMSETLKDVPIVKCADRYEGGMFALQTLNSQLLTLNSQLLFILDDGFQHWQLFRNKNILLIDAENPFDNRRLLPVGLLREPLKEIERADIIALTKTDNIRQAVIEDIAGEIKSYNSKAPVFLSMHKPAGFMRLSGEAMPIEW | 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 tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Sequence Length: 255
Sequence Mass (Da): 28596
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T0Y015 | MTGMPAQERGARLALFLDFDGTLAPIAPRPDLVRLEARELALLESLGRLLPVFVISGRAFPDILLRLPVSTLSGLSGDHGAVRRFRDEIAIHPEALRARESLARWGPVLREVTDRVPGAVTEAKEFSLSIHYRGVEPERVPRLFSEVEGLFGVWDDRDRFRISHGKMVWEVRPAGGVTKEETMDFFLELLARESGGVPGEYRPVMVGDDTTDLGAVNRALVLGGRGYWVGDPPPGLAAGAARLGNPAEVWSLLARLRDALAQGKDPLRELA | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 271
Sequence Mass (Da): 29699
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A0A7C8E993 | MMSKHFKCLSTDSRTIQKGEIFLALKGDNFDGHDFVHKAINIGDGAIINQNVLYAQHNVPITDLDFKGTLITVDDTLKALYQIGSLKRQNFKGPVFAVIGSNGKTTTKELTSSVLSQRFKTLKTIGNNNNHIGLPRSLTYMDSDTECLVLEMGTNKPGDIKQLCEIAPPDYAIITNIGFEHLEGFKSIEGVRDAELEVLSFASVVIANKDDKFLMEALNKSEYHKKITYSINDDTADVIAKNIKTSPEGNIFHVYYEGKHIELKTKLFGLVNIYNCLSAITAGLFLGLPFDLIKRGIESYNGMPMRYEFLKIKDRTIINDCYNANPSSMKEAIKELKRISNKNGRTIAVLGDMFEMGDETLNKHIELGRFVNNEEIDILVGTGEMMLYAINEFKGQKFYFKNSLETANFIPTITKPQDIILVKGSRGMKMEKVTEAIKNAL | 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-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 441
Sequence Mass (Da): 49430
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A0A2N1V8T3 | MTDQMVTEIAGKAFYYIMIVSGPILLVSLVVGLIISIFQAATSISEQTLTFVPKVITVFLVTILIFPFMISSMKTFTIEMFSMIEKMGP | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 89
Sequence Mass (Da): 9876
Location Topology: Multi-pass membrane protein
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A0A3M1QVB8 | IRPMGRILEPLRRMGAAIEAEGEGERAPLAVRPARLTGIEYRSPVASAQVKSCLLLAGLSAEGRTAVHEPAASRDHTERILPAFGIPVERLPDGAAVTGGGRPRAAELTVPGDLSSAAFFLVAAALAEGSRLTVEGVGVNPTRTGVLDCLEAMGAEIERLGEREQGGEPVADLVVRGRGLAGIEIGGELMVRAIDEFPVLAVAACFAEGETLFRDAAELRVKESDRIAAMAEAIRAIGGEVEERPDGLVVHGRRHLPGGRVRSHGDHRVAMAMAVAAARCTGPVVVRDTACVDTSFPGFYRLLRAAAEA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 309
Sequence Mass (Da): 32368
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A0A7X8HWA3 | MDGSIFIKKLLDKVLSGDDVTVNEANMLIKPDLTDLNELIQASATISRHYLKEIEMCAIYPAKIGNCSGDCAFCAQSAHHNSKVIPLSLQELDDNKVLEKAKELNRLGVKRFSLVTSGEQLTNEEFDRILDVFQRLNNETKIGLCASLGSLTLKRAIKLKESGVSRYHHNIETSRSFFPRICSTHSYDDKLETIKIARQAGLEICCGGIISMGESPKQRIEMAFALKELDVDCIPINILIPIPGTPLEKQQPLSIEEILRSIAIFRFILKDKPLRLAGGREQALGEYEYLAYTAGINALLVGDCLTTAGKSIEKEKCMLFNKNQKHHSCSSSEK | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 334
Sequence Mass (Da): 37174
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A0A7X8L9F8 | MQVIYVLIGIALIWVVLLQESKASGIGAIGGAAESYWGKNKARSLEGTFEKYTKIGALIFILLSLLLNILM | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 71
Sequence Mass (Da): 7712
Location Topology: Multi-pass membrane protein
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A0A3M1SND0 | MEIMIEYQLLMRHLRIHIAYDGTGFSGWQIQPGEKTIQGTIEEALRKITGKQTRLTGSGRTDAGVHALHQVASFSTTSTHPPEVFVRALNALLPPEIRVLCADEPPPGFHPRYSVKAKRYFYLLDLSAVQSPFISRYAWHLHRGLDIQSIHTATSYLTGRQDFAAFSGAGSSVATTIREITAVDLVEKRQMDIFFSTIEGRFLKIVFEGTGFLRHMVRNMVGTLVEIGLGRMEPAQIKTIINSRDRRLAGPTAPARGLFLERVIYDEDEGD | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 271
Sequence Mass (Da): 30371
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A0A496U5Y5 | MEKSKLKRNIESIIWTIVIVFLLRAFVVQGYVIPSGSMEDTLLPGDFVLAAKFVYGLEIPYTGVKFFQFYKPKRQKIVIFLFPVDKHRDFVKRCIGLPGDTIQIINKVVYVNGKPLDEPYAEHKDPRVFPPLVEVDTPFKQKMYQEAWMEGKFINEDRVRDNFGPVVVPENHIFVMGDNRDYSFDSRFWGPVPMKLLKGAPLIIYFSIDPEQPVWKLWKKIRFGRLFKIVLTA | 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: 233
Sequence Mass (Da): 27236
Location Topology: Single-pass type II membrane protein
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A0A931Q5G3 | MSPPKPVKTIAVIGAGSWGTALAAILSEKKIKTRLWAYEKEVLDSIQKFKENKIYLPGVPLSPDLRVTCSILEAVDGSDLILFVVPSHAARPVLKKISLHLKKEIPIISATKGIENETLLLPTQMMQEIFPKRFHRHLGVLSGPTFAKEILLKQPTAAVLAMKNFDLAASLQKKLTTSSFIIYLSRDVMGAQLGGALKNVIAIATGCSDGLGFGDNSRAALITRGLSEIIRLGTAMGAKKETFSGLSGIGDLILTATSRQSRNYSLGYQIGKGIPVARILSETKSVAEGVKTTLSAYHLSKRYRVATPIIEQLYYILYKNKDPKKAVAELIYRAAHSKGKKFEF | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 344
Sequence Mass (Da): 37495
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A0A7X8ESY1 | MIVLCFVGILFFNSVEEGKHQQVLLERYGEEQLLLIKQVVAFSENMSQKGETVEEVLQQLTDYFEENVTSGSRYWILCQGRQIVFYKNNAVTKQYIKLPITNYFPQEENINFYKEIGKRGFFSKVVSDQYQQKFIISSGSIQLSGQIYHLMLCTSKDFITNQSQTRVHHTYITLGILLLGAVSLCSVLLFHKELVRAKREIFSLKQEVLKKNCQVSALSSEKYLTDEDSAQRMEAEERKMPKEQIEEPKVILEKRALYRQYRLKFYLNAYHSIMIDGKEGDIHPHTWQVMIQMVKQKDEFVLFNEIEDKIDALFAKYQDQTINTIAPFDTLNPSLENISEYFKNEITVILQESGWILTQFECSETPTRSYLIEIPFEIQ | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 379
Sequence Mass (Da): 44403
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E4NBQ2 | MAIDESSVIWFDGALVPWREARVHVLTHALHYGTGVLEGTRVFETADGPAVFRLDEHLARLERSARMLRIELPYKQQDLAAATVELVAANGHRSCYLRHLAFLGYGSMGLDMRHSPTSVSIASWDWPAYLAAERGLRLMTSSWRRTDPNSVPPAAKATGPYLNSALARREASDAGFDEALLLAPDGSVSECSSENVFAVRDGVLRTPPGSAGALEGITQDTLLTLARDLGVEVRVENLLRSDLYAADEVFVSGTAAGVVPVASLDNRELPSAEGELTKRLAQAYRAATSGADARYRHWLTPVRSA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 305
Sequence Mass (Da): 33069
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F4LWV0 | MKNGNSKTILYLDCFSGISGDMFLGAMLDLGLDKEEFLSELTKLPLHDYEVEIKKALKGGITGTDVMVKTHEHHPHRGLKQIYEIIDNSKLKSDVKQKSKEAFYKLAEAEGKVHGKPPEEIHFHEVGAVDSIVDIVGSCILMDMLNPAAVYASPVNVGSGTVNCAHGILPVPAPATIELLKGVPVYAAEESGEFTTPTGALLLTIFVDEFGSMPLGIPEKSGYGLGKAERKSPNVLRAVLLKEYCNTGDIHTNDLEKDKIAILEANIDDMNPELYEEAIESLFQKGALDVFLTPIIMKKTRPGIKITCLCPPDKKQHLAEAMLRETATLGVRELVSDRIKLFREIEEINTPLGNLRVKIAKIGDEIIRTTPEYEDMKCLAKNNKMPLLKAYEIVNQFLAR | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent enzymes.
EC: 4.99.1.12
Catalytic Activity: Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide
Sequence Length: 400
Sequence Mass (Da): 44154
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A0A7L4PGZ6 | VSPRGEKVLFDLAKKARVSSRIIDFHNQEESLTHLLRLASGLESMIIGEDQILGQMKDLYLMAKKAGRTGWMLDTAFKKAISVGKRVRKETRINERSVSVGSAAVDLAEEILGGLENKCVLVIGAGETGELISRALISKGIGSLMVTNRTFGTALSVAACLGGVAVPYEEMKDRIHRADLVISATSAPHYILLKSDLEKIMEGRENKLLLIDIANPRDVEESAGEVPGVDLLNIDSLRDISDENMRLRMAEVDRVAAIIEEELRLLDAKYKRRQAEELLARLYSQAREIKEQEVKRAMSKLSAYHTLGEIEQKVLMDMSHSIVNKIFAEPTKVLKRASEENDLAILKSAELLFRLGDDEFEKDETA | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 366
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence Mass (Da): 40687
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A0A2H0QWZ6 | MQILEILGKIGFDWKLALANLINIGIIFLVLYKFAFKPIKQKIVEREAAIKKGLNEAHKAEIARQEAEDEKDEVLAQAKRDAVLMLEEAEKQRKNILKDAETKALKERENILHKAQLEIEGKQAEMERVLSEKSAELISRGVSAMLQEEMTPEINDRIIKKMTSHGK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 19074
Location Topology: Single-pass membrane protein
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A0A2H0QWI0 | MDAILPYIQIFLSILLIVLILLQRSEAGLGSAFGGGDSMSSINYTRRGFERVLFSATIVIAILFVLSVFTALVL | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 74
Sequence Mass (Da): 8037
Location Topology: Multi-pass membrane protein
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A0A533XXE4 | MIRAFIAIQLSDEMKRQIGSVQAELKREVSGSGRGGKAVKIGKVGWTQPEGIHLTLKFLGDIQETQVEALREILHKAAAPARPFTLEARGLGAFPNPRAPRVIWLGLHGSHDDMAELQRLQAAVEDGVAGLGFAKEARAFTPHLTLARIRDRVEAGALEPVLTAQQNRVVGEFAASSVELIKSELRPSGAVYTTLVEVPFGAGV | 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: 204
Sequence Mass (Da): 21946
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A0A953BTH9 | MSDPAALPADPPRRLAGFRLVSLWTLVSRIVGFARDSAMAAAFGLGEILDAFTLAFRIPNLARSLFGEGALATAFLPAFIAERDQRGAEAAQRLTTAVCVRLLVILSALVAAAELILAAARWLRPAPPAAYADRLLTLLAIMLPYLVLICLAALLSAVLQAQRRFGWPAALPALLNLWWLAATGLAAWWTTDGEQRIRWIAASLVIGGGLQLAAPALVLRRLGWGIDPRWRESRREANAVFRAMLPTVLATTVAQFNTVLDTLLAWWLAAPRESGGEPWIESGTAAALYFAQRLYQFPLGLIGVAVATVLYPVLSARAGRNDHDGLRDDLTHGLRVALSLAIPASAGLVLLAGPINRFLFLHGRFDADDALLTSRITAIYGSVVWAAVALLLVQRGFFAVGDRQTPLKTGLASVLVNVALTAVGVWLGRGVGLAMATAGSLVFHLGLSLHVMRRHRVGLAWGPFGSSLARTLGATAAMSAACLLLRQVPGVEESRTWGLVLPLAGGLATFAGTAWLVGLHEPWELLRGRRAVAVRVDGDPSGK | 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: 543
Sequence Mass (Da): 57870
Location Topology: Multi-pass membrane protein
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A0A953BX45 | MAAPAAKPGADEQAPAKKGPGLVVWILVAAVSAGAGFAVPMAMNSGHAAGDGESGHGKSDAHAPKTPVPSKPAFVEFGQLVVNLNDGRLSRYLRLKINLQVDSKHQKDVQDLIAENRLLLQDWLLSHLADKTMEEIRGAAGQNMMRREILEQFNSVLFPDGYDRIYAVRFEEFNVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 19132
Location Topology: Single-pass membrane protein
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A0A660ZG32 | MDTTCHKIQALHPMKGKLFVVGSPIGNLEDITFRAVRILREVDVIACEDTRRTKILLEKYDISTPMLSYNEHNERRRIPELLSMLSDGKDVALVSDAGMPTISDPGYRLVRAARENGFEVVAVPGPSAVTAALAISGLPTDRFVFEGFLPKKKGKRLKKLEEIREEERTVVVFESVHRIERTLAEMLEVLGGDRKVAVCRELTKSFEEVIFGRLDEVVQKLSTIKGEFVIVIGGKSID | 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: 238
Sequence Mass (Da): 26622
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A0A485HY45 | MSTIAENIAKVAARIREAAQAAGRDPATVGLLAVSKTKPAAAVREAHAAGLRDFGENYLQEALGKQAELADLPLNWHFIGPIQSNKTRPIAEHFQWVHSVDRLKIAQRLSEQRPAGLPPLNVCLQVNVSGEASKSGCAPEDLPALAEAVKQLPNLRLRGLMAIPEPTAERTAQHAAFARLRELLLDLEPWPGHPVHGHERRPRGSHRRRCDLGPHRYRPVRRPRLRRAGFLKESPMSTPRIAFIGAGNMAASLIGGLRAQGVPAAQIRASDPGAEQRAKIAGEFAIDVVESNAEAVADADVVVLSVKPQAMKAVCQALAPALKPEQLIVSIAAGIPCASLEAWLGQPRPVVRCMPNTPALLRQGASGLYANAQVSAAQREQAGQLLSAVGIALWLDDEAQIDAVTAVSGSGPAYFFLLMQAMTDAGEKLGLSRETASRLTLQTALGAAQMALSSEVEPAELRRRVTSPNGTTEAAIKSFQANGFEALVEQALNAASQRSAELAEQLGQ | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
Subcellular Location: Cytoplasm
Sequence Length: 508
Sequence Mass (Da): 54102
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A0A485ECW1 | MRLCVIGAGYVGLVTAACFAEMGNQVRCVERDRERVARLRRGEMPIYEPGLESILRDQLDAARLTFTASLAEGLADAEVVFIAVGTPCGEDGSADLSHVLAVAEQLGAQLRQACIVVNKSTVPVGTAERVEEIIRLGLARRRKRFRVAVASNPEFLKEGSAVDDFRRPDRVIIGSAETQAGETLRQLYAPFLRNHERVLLMGRREAEFSKYAANAFLATKISFMNEMAGLCALTGVDIEDVRRGMGSDKRIGTHFIYAGCGYGGSCFPKDVRALIRSAEQQGYDSQILRAVEARNARQKELLFETLGELFQGTLARAHGGALGAGLQAGYRRPARGAEPGPAGGAAAPRGAGQGP | 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: 355
Sequence Mass (Da): 38211
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A0A496U2R9 | MRISFHKLQSQGNDFVFIDEKDVKNVDLSRVATRILDRHFGVGGDILVIYNMEHNFLRFFNPDGSEAEICGNALLAYGEFLRISQRQSGSVEVATKGKKAKIIFKEKIIVRFEIKDFKFEKITIFLGKRKIQGYYTKGFGNPHFVLINPDVDFKKASEIEKRNFFPEGTNVDFITINSRSEVIHRIWERGAGETLSCASGALSSFMIIYALGLVDEKVSFISRGGILIIRKEGNSIFFTGKPEYVFKGELNLS | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
EC: 5.1.1.7
Subcellular Location: Cytoplasm
Sequence Length: 253
Sequence Mass (Da): 28756
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A0A7V8DJ58 | RERINDVETVIERVFKSMSGEKTEQFPIHESRSIVAAHDITPADMLQIDRNNVLAVITEIGGRTSHTAILARALEIPAVAGVEGVCDVLLDGSPVIVDGTAGTVIVNPDRETFQTFLSRKQHYEYVESELLKTAHLPAVTLDGHAISLRGNVEIPEEGASVLKHGGIGVGLYRTEILFMNRSEMPDEDEQYFLYHSMQQAIKPHPLTVRTLDAGGDKLLEGLDHTAEQNPALGVRAIRLSLGMPYEFKKQLRAILRISAEGPVRIMFPMISGIDEVRAATALLEEAKLELADAGIPFDSGIKVGIMIEIPAAVTMADLLAKEVDFFSVGTNDLIQYTLAIDRT | Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 343
Sequence Mass (Da): 37546
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A0A933S2Q6 | MRRNAFGFMARAAWLGVALAVLAGAAPAWAVSYTAKTVVTMDALSGQVVESQSGDAPVGPASLAKMMTLYLVYAAVAEGHANWDDPVLAGSNAFHKEGSTMFLREGERVTLRELAYGIGVASGNDACIAVAEFLSGSEDAFVTRMNETAARIGMKHTHFGSATGLPAEGQVTTGEDMARLAYHLIADFPPVIEVLSTQYYTHGGVRQPNRNRLLWKNIGVDGVKTGHTEEDGFHLVASAQKGEQRFIVAVMGADGETSREEIAERYLLAAFRRFATVRAIKPGEPVAQVVVWKGAADSVGAVPDGPVFVSVPREREAEVTVAATVAELEAPVAKGQVVGTAQVYVGTEVVREVSLVADREVPEGGFFTRIWDALVLMFRALLDKLF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Length: 386
Sequence Mass (Da): 41242
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A0A533XVS5 | MRQTRKRRSKLILVLGGAASGKSQAALGLAGQVGPKAFMATGQALDREMKARIERHQATRPSDWVTVEIPMDIVSWVSEKGHDYRAIVIDCLTLWLSNMRGQRIRDLAISEATADLLHAIRATRARVVIVSNELGLGLVPATKSVRAFRDLAGRVNQQVAAEADEVYVTISGLPLRLK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 178
Sequence Mass (Da): 19508
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A0A931VK64 | MDGSKTLVLGGTRSGKSRFAFEQGEKFPGKKVFVATCQPFDSEMKGRIALHQQSRNASWKTVEEFFNLADRIKEISEPYKVILVDCLTLWLSNWVLKEDQDTKVREEIFRLLEAVQQTVTPIILVTNEIGMGIVPPTPLGRRFRDLQGELNQAAARMVDEVYLVTAGIPLKIK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 173
Sequence Mass (Da): 19569
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A0A933VYP1 | MNILSVASEAVPFAKTGGLADVAGALPGALARLGHRMVTVMPLHRKVDKARHGLKSTGRIVSAQVGGHTHIGAIWMTEQGGAETYFIEHDLFFDRDGLYGEGGDSYGDNAARFAFFSQAALDLCGAIGFAPDVIHCHDWQTALVPVYLRERPGAYPDAERAGTVLTIHNLAYQGVFGFRDWPALELPDHAFSIDGLEYHGAINLLKGGMKYAHAITTVSRTYAREIQTPAFGYGLDGVARFRAADLHGIVNGIDTALWDPAHDPALSQPFSADAIDGRAANRELLRHSLGLSDGAGPIIGMVGRLAEQKGLNLLLDALDGLMRRDVRLVILGEGDPAIMRALERAAAHHGGRLRLHAGFDEGTARRIYGGCDLFLMPSAFEPCGLAQLIAMRYGALPVVHRVGGLADTVIPYGSEPLHATGFAFDHFTPEALLACLDTALEVFRHGDVFRRLQRNAMGRDVSWAASAKGYVDVYRTVAQRAGAVPSGAARG | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 491
Sequence Mass (Da): 52645
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A0A931MB47 | MGKKLSSAEIREAFCKFFEQKGHTRVISSPLIPAGDPTLLFTNAGMVQFKQIFLGDEKRAYQRAVSVQKCMRAGGKHNDLENVGKTARHHTFFEMLGNFSFGDYFKPDAIEYGWEFVTQIMGLSPEHLWITVFKDDEESAFLWAKKVRADRIVKMGEKDNFWQMGDTGPCGPCSEIYFDQGPEISCGKSTCGLGCDCDRYLEIWNLVFMQFNRNTRGELLPLPKPSIDTGMGLERISAVCQGVKSNYNSDLFKPIIGEIEKITGTRYGQNPSKDVSVRVIADHIRAITFLIADSVHPSNEGRGYVLRRIMRRAARHGRFLGMSDPFLFQLTDTVIIQMKPFYPELDSNQSRIRQMTQGEEERFIHTLNIGMKLIEELFLKMKRDGEKTVPPEALFKLYDTYGFPLDLLEDIAVEEGFNLDIKGFELEMENQKKRARAASRFGTEDSALVSFSKEILKEYGKTKFLGYDSLEGQSTLIAMLNGTERVKRAREGNEVFCVFKETPFYGEGGGQVGDQGTVSGETVLAEIQDALKPAPELIVHKVKVVQGELIENSTYVLEVDEKRRKDSARNHTATHLLHAVLREVLGDHVKQAGSYVDPARLRFDFNHFFPLTRKELDKIERLMNERVRKNVPVHPKIMGLEEALKEGALAFFGDKYGDEVRVIQIENLSQELCGGTHCRATGDIGVFKIVSESSIAAGIRRIEAVTGEGAYELIKTQESQFLQMAENLKVKPAEAPQKLLKLISSLKEKEKEITSLKSKSISPKNDRETEIKKVNGTSVLIKKMGAMSPKDLRSAMDEYKNLPGIDVIILGSSAEGKVYLTVSVSPSKTNRFHAGEIVRELSVVVEGTGGGKPEMAQGGGKNPEKLEEALLQAEKIIQKHSQTAFNG | 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: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Cytoplasm
Sequence Length: 887
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 99409
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A0A974RXQ4 | MSLTQVWLGLGSNINQQQHISAALLALSKVLQNMQCSPVFESESVGITSSNFYNLVVTGSTSLPLLELSAILKKIEADNGRYDKNKKSLPLDVDLLLYGEQVGEFDRITLPHTGILKNAYVLLPLSMLSPFHKHPILGMTFAEIWQHSQSEINQKLWIIDTPWLSC | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 166
Sequence Mass (Da): 18535
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A0A933TCA9 | MSDLSRRLGVHTSIAGGVHLSLERAGELGCNTVQIFSHNPRQWFVDKVPKEQTAQFKEMREAYDIDPVFIHASYLINLAAFDADILDKSICLLIHELDLADALDADYVVLHTGSASQDSEDNARRKAIDALKIISKEKTWNARLLLDNTAGERGDISSHMKDLAEITDRTNSALIGGVCIDTCHAFAAGYDLRNKQGLSDLVKEIEAYLGSESVKLIHLNDSKKGHGSHVDRHEHIGEGGIGRLGLKRFVNHHAFRNIPFILETPKKSEEDDPRNLKIVRSFF | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Length: 283
Sequence Mass (Da): 31532
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F4LX84 | MNKSDIGLIGLAVMGQNLALNIERNGYQISVYNRTAEKTKEFLETSAKGRSRIKGVFSLEELVASLKKPRKIMLMVKAGTAVDAVIHQLVPLMEKGDILIDGGNSYFKDTVRRARELEQKGIHYMGVGVSGGEEGALKGPSIMPGGSKEAWEQISDIFIKISAKTPGGAACCDYVGPDGAGHFVKMTHNGIEYSDMQLISEAYFLMKELLGMTALEMKEIFAEWNQGELNSYLIEITADILGKVDDKTGKPLVDVILDKAGQKGTGKWTSQEALDIGVCIPTITEAVFARYMSSAKEERVEASKILKGPSTSFKGDRKQFLEDIRKALYASKICSYAQGFDLMAKASDIYNWDLNLGNIALLWRGGCIIRAQFLEKIKQTYDENLQLKNLMLAPYFNQSIENCQAAWRSVVSTAALNGIPVPSFSSALAYYDSYRRHTLPANLIQAQRDYFGAHTYERIDEEGIFHTIWM | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
EC: 1.1.1.44
Catalytic Activity: 6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH
Sequence Length: 470
Sequence Mass (Da): 52132
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A0A7J2MEU4 | MYKVLRTVRSIDIEHCADTPPKSSSGSEPYKMDKRDIEDMPPITEHGTTVELREAFYNPHTTPDRDLTIAVLAAFDRMVDPIESYLDTFAATGIRGLRAASELKLAVTLNDRDPDATYLIRQNIALNSLESSCVVTNEDANVLLHQRRFDVVDIDPFGSPAPFLAAASRSAIRLLCITATDTAPLCGAHLNAGIRKYASVPMNNEYHAEIGVRVLMGAIARALAVQEKAMVPLLAYARRHYVRVYAKVLKSVSSADMSMQELGFIAHCRHCSFRTWAAGLAPVIHESCPVCGSRVVATGPLWLGRLHDPAFLGSVLSELIDRESDKKSIKLVEMCRDEIDAPTFYDQHKICRALKIPPVRIDAVVDKLRDFGFAASRTHFSGTSFKTDADIRVIAEILSKGR | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length: 402
Sequence Mass (Da): 44424
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C5LUH1 | MVSVYLFVPNLIGYTRVALMLISFYVAFDNWKAFVFCYFWSQMLDAFDGAAARRFNECSMFGAVLDMVTDRISSNILALILSHFYPALYLPLVMFAVVDYASHWTQMYSSVLAKNGSHKYIAPNRPWLLQKYYGSRVMLFSLCFAQEAVLVLMYLYHFATMPTAAAPVWMQQAVFYAAVAFFPIALLKQVINVIQLFDAGHEIVKIDEANRGEKVE | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
EC: 2.7.8.11
Subcellular Location: Membrane
Sequence Length: 216
Sequence Mass (Da): 24706
Location Topology: Multi-pass membrane protein
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A0A1Z4GXP8 | MIDCFGDPCSSHCPQNSDSQLSILENSELSVCSYNFEFRSYQHHKGDLPGELLVNGNCIEQCVTAHNNVTEVANFIQNVLQYQPTNGSTAQYICSINCVENYDQIEWQYAAWLDPYEQAIFGQCMVNGKLRSLAVAQDIVAHEFFHGLTYQIVGLDYYGQSGALDESYADIFGILVANFQNSDIETWNWELGSGFGDNGRAIRSLSNPAIYGQPEHMNNYRILPDFDDYGGVHYNSGIHNKAAYYLLSSQDAEGNYLFDATSGATLFYLALSQLSKQSVFSDSRRAIQQVARTLFRQDSSKLEKLRAIATAFDNVGIGDNIGIFE | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 325
Sequence Mass (Da): 36311
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A0A3M1SGR8 | MDRLRKRHQFQRVFSEGKKVVTPSLLLFISPAETDSLRLGLSVSKKVGKAVVRNRVKRIIREAFRMAEKELKKEGITLDGLDVVVVPRRGAVEAKSTQLLMEIIDKFRELRCDNS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 115
Sequence Mass (Da): 13178
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A0A2W6BF74 | MGLLAVALPAAIGAPLRHLVHRWIHRRYGGTQAWGTFVINVSGSFALGVVIGLALFHGLPQTPKLALGTGFCGAYTTFSTFTFETLQVGRDTSIRAAAANIVGSLTASLLAAAAGLAVAAIGS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 12534
Location Topology: Multi-pass membrane protein
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E4ND38 | MSTTREPWVVGVSGASGTPYAASVIRALLAAGEPVDLIVSRAARLTILDETGLSFRDAHWRADLAAWLGTGEEELADVRHWSAGDFAAGPSSGSYPAKGMLVVPATTGAAAGIALGLSKDLLQRTASVTLKERRPLVLCLRETPLTGSTLRHLVALDEQGAVVLPASPGFYAGGSTARELVDFVAGRVLDAVGVPHGLYRRWSGTLGESAGTPENHPRNGPRRGE | 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.
EC: 2.5.1.129
Catalytic Activity: dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2
Sequence Length: 225
Sequence Mass (Da): 23501
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A0A3M2D9R5 | MADHWLIACLWAYLLGSIPFGVLAAKIFRCADPRAAGSGNIGFTNALRVCGKKIGFLTLAGDFGKGLVVGFAVTSAAIPEPHAFLVLLSAVLGHVFSLFLKFHGGKGVATGLGVLIGYDGIIGALLICIWGIAVSVWRYSSGGALAAFVALPILAAALGRTFDYIVFCIMLSGLILWKHRDNIQRLLGGTENKLGTRKAAS | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 21089
Location Topology: Multi-pass membrane protein
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A0A3M1R6D9 | MAQLPNALTLLRVCLVPLFVLFHYPIVVDDRTYWAAGWTFALAAITDFFDGYLARRYGLVTRLGKLLDPIADKVLITAALVMLVEIERASAWVVIVILGREFAVTGLRALAASEGVVLAAESLGKWKVGAQITAILMLLVDHFWFLPGLRLRPLGTFFLWVAMVLAVVSGLQYGWNYWRSSGEAAAG | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 187
Sequence Mass (Da): 20612
Location Topology: Multi-pass membrane protein
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A0A9D6LNG1 | MKSTRRKTNAPLGVHVSIAGKISGAVERAHELGCTAMQIFSRSPRMWAAKGLDPAEVTRFRELRERFGISPLVVHASYLINLATPEGALKRRSVEALIDELDRADRLGANYLVVHVGSCSDGGSVEGVERVREALADVLASGQWSTRLLLEDTAGERGDVGANLEEIGMIVKGLPGGARVGVCLDTCHLFAAGYDISKPDGVERVARLVKETIGLDRVKVIHGNDSKKGLNCRVDRHQHIGHGGIGLKGFRAWLNHPAFRDIPMILETPKDSPEADPRNLKIVRDLVGSSTVSKEGRA | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Length: 298
Sequence Mass (Da): 32242
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A0A7V3SV48 | MKMYKSLPEIIYLIGYLIKKNYKIKNQKRIPYNVISIGNITLGGTGKTPTTILLVEEAKRRGYLPVILTRGYKGKENRPILINTNGNKEINKLDVESLGDEVVLLAEKLKGAYIVKFKDRYEAGMYAIKYLKNSQIEDNKKIIFLLDDGFQHWGVYRDKDVVLIDSINPFGNKRLFPVGVLREPLTALRRADIVLITKSNMLDNTSKEKIVTEIQRYNENCPVFFSEHRPVSFVDKNGERFHLGLLEGKEVFAFCGIGNPESFKKML | 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 tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Sequence Length: 267
Sequence Mass (Da): 30625
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A0A521QTT7 | MLGAVLLLLLAACRASASFAAPQTMVAAAHPLAVDAGLEVLRRGGSAVDAAIAVQMVLGVVEPHASGIGGGGFLLHYDASTQAITVYDGRETAPAGANPSMFLDADGKPLGFREAIASGMSVGVPGLLAMLELAHKERGKLAWSDLFVPAIAVARDGFAIPPRLAAWLARIPSLREEPAIRAIYFNADGSPKKLGERIANPELAKTMRLVAEQGPRAFYQGAMAAEMVERVQSHRRPGTLSTTDLADYRPIKREAVCGPYRVWTICSMPPPSSGGIAILQILGLLEPFEIWHDKPTDLRALHLIAEASRLAFADRDRYVGDPAFVDVPVAGMLSSAYLAERRKLMSPDRSMGKVAAGVPPGYVERGTSHISIVDRWGNAASFTTTIEAPFGAQIMVRGVLLNNELTDFSPRPELNGKPVANRVQPGKRPRSSMSPTFVLDRDGKLVAALGSAGGSRIIGDTLQAAVGLLDWNLSPQAALALPRVLNLNGATELEEGTAAATQADALRALGHEVQVRPHEGGLSAIRRTAEGWEGAADPRRDGVAKGE | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 547
Sequence Mass (Da): 57853
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A0A7C0ZSV5 | MVMRLLPSLRERRRYLAFEMLSENAITRRDFNRELERGALSLLGDSGASECRMSLLLFDGAQGKGRGWGIIRCVHTHTLETRAAIATICEVGGSRVAVRVIGTSGTVKGAKRFFD | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 115
Sequence Mass (Da): 12743
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V5RJQ6 | MVIKDLLSSEQLSNIDFKVIKEILMVLNKWSANDFSINNTIENKKLDLFFEYINQFKQGIPLEYITKKKYFYESEFYVDDRVLIPRVETEMLVEEALNFTKSGNLVIDVCCGSGCIGLSLKKKFRNIELWLSDISSSALEVAKYNSEILNIEANLINSDFLDFIFELQLTPDIILMNPPYIKKGDVNVAHSVSKFEPHLALFAVNDGLYFYQKLFDLLDNLYKINKNLIIISEFGFQQKNGIEKLFKHKVVKYKIDFKKDYFNNWRYFVISK | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 272
Sequence Mass (Da): 31882
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A0A520JUY6 | MKRTKIICTIGPASSSKTTIREMIISGMDVARVNFSHGTHAEHKKTIQLIRKTANELETQVAILQDIAGPKIRIGRIENEKISLQTGSNIDITTKPVISTVKQLSINYTKLPLEVHTGDAILFADGTIEVVVNSVEKETIHCTVIDGGILTSNKGVNVPSTTIRTPTITEKDEADMLFGIANDVDYIAISFVRMPEDILQAKSIITGANADTAVIAKIEKQEAIKKINKIIAVSDGIMVARGDLGVEVPLEDVALIQKKIIKLCNNYGKPVITATQMLRSMVENNRPTRAEITDVSNAILDGTDAIMLSEETANGSHPIQSVKIMSRIAQATEISDEFKEQMFRRNLAPLNNIPDAISQAACNIAKHLDASAILTPTSTGSTARLVARYRPAQSIIAMCTISKVYRKLRLIWGVQSVMTEVTDNTDQLVQSAKQIARLKGIKPGELIVITAGTPTGTAGSTNLIRVSRIKPVD | 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: 473
Sequence Mass (Da): 51290
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A0A934CS67 | MSIKKIENKILSGKRLTAEDAAALFQSDDIFTIGRLANIVAEKKNGKNAYFIRNHHINPTNICVNRCKFCAFSRSKGEKGAYELSIKEIIKKLSSQSSKVKSQKSEAGKKYRPPIPNPQPPFTEVHIVGGLHPDWKFDFYLEMLKAIKKNFPYIHIKAFTAVEIDYFSKINGQPLAETLNELKNAGLDSMPGGGAEIFDSRVRSKICPEKISGKKWLQVMEAAHTVGIRTNATMLYGHLETSKHRVEHMLKLRDLQDRTGGFQAFIPLAFHPMNTELGIRGRGLGVSKKPTPNPYRYTSGIDDLKTIAVSRLFLDNFLHIKAYWIMLGEKIAQLALMFGADDLDGTIIEEKITHSAGALSGNSLTREQMINLIEKAGKTPFERDSFYNSVG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
EC: 2.5.1.120
Catalytic Activity: 3-[(1-carboxyvinyl)-oxy]benzoate + H2O + S-adenosyl-L-methionine = 6-amino-6-deoxyfutalosine + H(+) + hydrogencarbonate + L-methionine
Sequence Length: 391
Sequence Mass (Da): 43804
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B0Y9I8 | MRALSVFVALFSFLALSSASPGQDVAKRVTSGSLQQVTNFGSNPSGTLMYIYVPNNLATKPGIVVAIHYCTGTAQAYYTGSPYAQLAEKYGFIVIYPQSPYSGTCWDVSSQSALTHNGGGDSNSIANMVTWTISQYNADTSKVFVTGSSSGAMMTNVMAATYPELFAAATSTPASPPAVSTPPPTKSTAGTAAAPRATSSAPQRSGAVSPKQCTRGIPGHGPACRSTTAAWIPLSTRRITTKPASSGRVSSGTTITRRSRPRATPRRRTTRLPSGARICRASLQRASDIRFLFMGSRTWSGLGLPGVRRRRRLLLQRLRRRARRHRRGGRRPALVLQSTGVNVAVMGGRGRRRVRAGIPAP | Function: Esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides.
EC: 3.1.1.-
Subcellular Location: Secreted
Sequence Length: 361
Sequence Mass (Da): 38419
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A0A849PIR1 | DGVFLAGSAQAPKLVDESISQASAAASRACSILAKEQLETSGVISVVDAEVCIGCGRCVEVCPYGAPELKEVEVVTEEITYMTRKSEIDPAICKGCGSCAAECPTSAITSRHFTTKQISAVIDAFAFTDGIIEEVA | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.-.-
Sequence Length: 136
Sequence Mass (Da): 14138
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A0A533XU81 | MFRTLRDDLAVVFQRDPAATSRLEVILTYAGFHALAAYRLAHRLEAWGVPFLPRVISQVARFFTGVEIHPAAKIGRGFLIDHGMGVVIGETAEIGDYVTLFQGVTLGGTGKDRGKRHPTLGNHVVVGAGAKILGGIRIGDNVKIGANSVVLKSVPE | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
EC: 2.3.1.30
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Length: 156
Sequence Mass (Da): 16696
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A0A520KPX2 | MDNKEHNIGNPGDRALEILEDKYLCDHCLGRQHGLLLSGTDNKNRGQAIRNYLMMYGDIKLLEENDPTTLKLVGRNTELGKKSLERRGVEIEKQDRECWLCGDIFSQLDKYVQHIVRETQDIEFNTFLVGTKLTSRLIQKEEEIWAEYGAEYSESLKSEFNREIGKRFEEKTDAEVEFENPEVVAIINLESDEVEIKNNPIFFYGRYIKHARGIPQTEWHCPACRGEGCMRCEGEGTLHQTSIEEIIGKPILRDTEGKEAVFHGAGREDLDVKMLGDGRPFVIEIKEPKKRKINKDEVIEEINSEYNDKIEINGLKPVDRDKIKEIKEARAPKTYRAKIKRKPDNNEISREEIKKALKKLEGKTIKQKTPRRISRRPEKTRKRKVHKTELLDTTDEHHIIKIKTEAGAYVKELISGDKGNTKPSLAELLKKDIKCIELDVLEVHYPK | Function: Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(54) in tRNA = pseudouridine(54) in tRNA
Sequence Length: 447
Sequence Mass (Da): 51746
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A0A1V5C0A3 | MNRKSFDKESFIRFILILFALSSLLFLFTIFIFILSEGLPLFYKAGVTAIALGMKWAPTKNFFGIFPMIISSFMVTFGALFVGAPLALACATYLSEYAGKKTKIVLKPSLELLAGIPSVVYGFLGVIYIVPIIREHLGGAGFSILSTSLVLGIMILPTITSISFDALMSVPPAFREGSLAMGATKWQTVYRVVLPAARSGILASFILGMGRAIGETMAVIMVAGNALKIPTSLLDPLRTLTSNIALELAYATGDHRRALFSTGVVLLIIIMSLNLVANFWVKRRVVK | 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 membrane
Sequence Length: 287
Sequence Mass (Da): 31098
Location Topology: Multi-pass membrane protein
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D2QLM6 | MSIGMLSTEQLYHKFQECTGVSTDTRRITPDCLFIALKGGNFDGNQFAEQALASGARYALVDDAAVAERDRASGTDRCLLVADGLTALQDLARHHRQTFTFPVIGLTGSNGKTTTKELIAGVLSKKYNLYATAGNLNNHIGVPLTLLSLNEQHELAIIEMGANHQKEIAFLCSIALPTHGLITNIGKAHLEGFGGIEGVRIGKGELYDYLAQNAKTVFINSRDKTLMAMYRERLKSIRSETTFAEAIFYPAANPDEETTTLISESPVVVYKNASGHEITTHLPGRYNFNNMLAALAIGDYFGVSPEEANRAIADYNPTNNRSQQVIKGTNTVLLDAYNANPSSMAAAIQQFAATPAKRKAVILGDMYELGDESEAEHAALGKLIAESNFDLVILAGKDMRFALEYLPKAYYFPDKFSLHNWVMDNPMADTHILIKGSRGMSLESVVPFI | 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-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 449
Sequence Mass (Da): 49068
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A0A931VT81 | MAEGTEPGFFDYVLPDERIADRPASPRDAARLLVVSRAAGTLSHRRVRDLPGLLDPGDLVVLNDTKVVRARAAARKVPTGGRVELLFLLRGGAGRGDRTCEALARGAGRPGTRLRLEPDGPEVEVLSAAAGTISVRLPDRFDLRAWLEKSGDIPLPPYILRRRGEKTARADDFQAYQTVYARTDGSVAAPTAGLHFTPGLLDELKRRGIETASVTLHVGPATFRPVSKAGCPEVAPDPEWYSVPPETAFAWERARERGGRVVAVGTTAARVLETVFREGAGVSAGEGWTSLVIRPGRRFGAIDGLLTNFHLPRTSLLLLVSAFAGEETTRAAYGAAIREGYRFYSYGDAMLII | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
EC: 2.4.99.17
Subcellular Location: Cytoplasm
Sequence Length: 353
Sequence Mass (Da): 38095
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A0A933S5P2 | MSPTPRGAEADATPRRAAFAVLQRLDREPVDLQAALDQAFRQGAWDPRDRRLATELTFGVARRRFAIDPLIRHLTGRRLKDLDRATRTLLRLGLYQLLYMDRTPARVALAETVRLAGDARRRGFVNGVLRAADGGAQAPPAADETERFARDHALPGWLAQRWLADFGPEGAAARAAQANGPAPLTLRVNGAVTRREALAERLCAAGCEVTGTAVAAHGLTVRGGGPVPELPGFAEGAFYVQDEASQLVGELVGARPGERILDACAAPGGKASQLAEAVGPSGQVVALEQDARRMERLRANLDRLRLGNVTVARGDAATIDGAALGAPFDRVLLDAPCSGLGVLNRHPEGKWWKSAEAVAACAASQGAILAHVAAMVRPGGSLVYAVCTGERSETVRVVADFLATRPDFAVVRADLLLGEQARPLTTAAGFLDSNGNALGMDGFFAAHLTKKSC | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 453
Sequence Mass (Da): 47870
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A0A1Z9VP97 | MSEGHSAQAAEFRLTSGSIFSKVNGVIQASILFFSFALIGLDQIAKYYALYSLIDGGIALVPHFIELNLAFNQGIAFSMLANESSIVHHLVTLFNMATIIGLMVFLFYKKHHPLTKFGLILIIAGGCGNLLDRIKLHMVIDFIQVKFFNFPLFICNLADIYVTMGALLFIYSRIFKQNERHLFSKN | 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-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 186
Sequence Mass (Da): 20888
Location Topology: Multi-pass membrane protein
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A0A521RN29 | MSSGVKEHGRRKAEGGKGKRKKTVSSLSPSPPRLSTFGSHVQQWEGGAAGTGFRFGIVLSRFNQSITDPLLKGALQLLETQGVRPEDIEVVKVPGAFEIPGAAKKLGSLGRFHALICLGAVIQGETPHFHYICSEVSRGIGQLSLELGMPVIFGVLTTNSMEQAIARSGNEMNKGAEAAMAAIEMAHIYQKLK | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Length: 193
Sequence Mass (Da): 20582
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A0A7C1Y6U0 | MKGLLLALQFLTILPVRVPGRVSSRDVGRSTAFFPLAGLLKGGLLLLAYAALGPVMPIEVVSAILLAVSVLVNGGFHLDGLADTFDALASGKPLKERLDIMKDGTAGPAGITAIVLVLLLKYVLILETLSAGATAYLVLFPTAGAWSTVIGVFHGRSARSDGLGHLLIKESGAAEFAASAFLATAVFVSSGYLSPPPSLTASALLVAGIYLFTLILVRFFSSRFNGITGDNLGAVCELNEVFFLILAVALRGG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 253
Sequence Mass (Da): 26201
Location Topology: Multi-pass membrane protein
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A0A7C6FV29 | MPSPENPKIPSQNEAAFPPPLAKELAPRLLSWYRDNARALPWRESTDPYRVWVSEIMLQQTTVEVVRPYYARFLKAFPTVESLAAAEESAVLKLWEGLGYYTRARNMLRAAQVISEKHSGRFPETYEEIRALPGIGDYTAGAIASICFNLPRAAVDGNVLRVFSRLLAQNYLSAAEKRRLAAQISAIYPQDACGDFTQSLMELGALVCTPSSPKCGLCPVRWLCRAFLEGCVNEYPARKGAAAKREEALTVLILTREEDIALRRRAPQGLLGGLWELPNRAGHLIEPEAVAFTESLGARPAELLKSGRASHVFSHVRWDILWYHIACADTEDAPLEGGALWVSPKARREGHSLPSAFTKLLKQAGIPS | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 368
Sequence Mass (Da): 40765
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A0A3M2D6R4 | MKKAWAKTVEFLAEVRGELKKVSYPTVSETIGSTAVVLLFCFFMSVYLSVIDSVLVWIISKIL | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 63
Sequence Mass (Da): 7087
Location Topology: Single-pass membrane protein
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A0A3S1BL49 | CLYSATNEWIKVEGNIARVGIDDYSQKEFGEIVYVDLPKVGNGYSKDEEACVIESVKTASDVCMPLSGKVIRVNTDLESNPSLINQSCYEAGWLFDMELSNESELKELIKPEDYKSYV | 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: 118
Sequence Mass (Da): 13257
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A0A9E0NEU1 | MSCWALLALKTAASAKGRLAEILPPAQRVRLVHRMLAQVVCTLQTARHIAGIAVVTGEALAQPGLWRIEDPGNGLNAALEHGAAQLAARGIDEVLLLHADLPLVRPEEIDTLIEAGRQHGLALATDKLGQGSNALYAPLPLPIPLRFGPGSCRQHQDEAARRQHPLEVLRLPGLAFDIDEPRDLQYLCTVLPQHYGDFSALLAAPPLP | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
EC: 2.7.7.106
Catalytic Activity: (2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-diphospho-5'-guanosine + diphosphate
Sequence Length: 208
Sequence Mass (Da): 22363
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A0A3M2AR60 | MKARAAIRPKKALGQHFLVDPNIIKKILAVAAVQKDQTVLEIGPGQGALTRALCEAARQVIAVEIDQTFTPILEALQQQYPHLEVKWEDALTVDYQALPPGTVVVANLPYYLSTPLLCRLLESGLRLARMVLTLQVEVAQRLVAGPGNRDYGSLSVIVQSCAAVERAFSIAPSCFFPRPAVESAVVVISPNPSSMKPQRRQALVHTVKTAFAHRRKTLLNSFREEGWPVEKVVEALQTARIDPMRRAETLSIQEFLALADALFP | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 264
Sequence Mass (Da): 29064
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A0A0S7XDT4 | MDVSQKIRDERIAKLGLLRRRGINPYSAKFAVTHSSSDVLSCFETLESEERPVSVAGRLVSKRKHGKASFGHVQDRTGKLQLYFREDNLGKEAYELLAMVDVGDIIGVSGPVFKTKTGEITVKVEAFQLLSKSLRPLPEKWHGLRDVETRYRQRYVDLIVNAEVRELVTTRSRIIKTMRNFLDERGFIEVETPVLQPLYGGAFARPFVTRHEALDMDLYLRIADELYLKRLIVGGLERVYEIGKDFRNEGIDRTHNPEFTQLELYQAYADYMDMMELFEEMVCEVVTELFGELKCVYGEHQLDFSRRWKRFGYFEALKQHLGVDLQGATAQEVRSLCTELGMDVDAVLAREKPGMKAGRRDKEEARGAGKTLGPGGSRPPSRSGIDQPAAREILLEELFSEKVQPHLIQPTFVYDYPKEISPLAREKAGSPGIAERFEPIIAGLELGNAFSEQNDPLEQARQFDLQAGRGEKGDAEAQPKDLDFLRALEYGMPPTGGLGVGIDRLTMVLTNSRNIREVILFPHLRPEASLGESDTDEL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 538
Sequence Mass (Da): 60844
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A0A9D6Z8V4 | MRKQVSLQRSISLSVLSIGLLSGSVGLGYAYWQSTYSLRETIGLGFQELARQSADKVGLILDREIEWVERFSSLPEVRGAVQEGTRLTFDQAVLQRWKESQRPYFRSLIILDRLARSVGGVATDNTGTDHTGQPWWPVVFEQRRSWVGELRIDETGQGHLEVAVPIVDETGVVVGVLHAMIEKEELLTSVLRSRIGNTGHVMLIGPKGKVLACPFLPPAQHTTITASMNESHNSAPSMPELAWMEAQDDGHGQGGGIIGLASVALRPGIVQEAMWSILVSQDPNETYAPLRLLTWKLSAFGMLTIAVVGLLRWRLGRRIVQPINALVERVHLLGEPDGEKPTMATQPSGIVEIDTLAVSFDELAERLERASRERRQYVAELERANQELVISEEHYRLLWDHSTDIRLLVNKEGIIQDVNRRGEIKLRTSADRLIGMKIGNLFQEADRSRLHRLLDEVIDTKKEEPAGEMRMPSPAEGTLIMDVDLVPVENAGSPVVVMVQLSDLTEKKRLEEQLIRSERLASLSQFASMFAHDIRNPLVGIKKTLELLAQDEGSQPSARRQWWGDMQLTIDLLLGMINDMLDVYQESYSGLPLLTSSVSVNSLVADVVQLFRSEATARRIAFQIEMPEDDVGMTADRRRLLRVLINLVHNAIKFSPHGGTITVTVHAEARGSTGRESCGTSSSQATIQVADEGPGIAPEDLPHLFEMFFRRKDPGDIRIGRGLGLHFCRLVVAAHRGRIRAENRPSGGAVFSVELPLNQEAYAGHIADCRGSTAF | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 775
Sequence Mass (Da): 85995
Location Topology: Multi-pass membrane protein
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A0A1Z9VP39 | MNDCIQKITESYYKHKDNSDIEIEARLGFFNIGKFDTNVTEEFFLKIKNKFDNTSTWNNVEKINKTDYYYDKVRISIEDDGTTECIQKKNLEKLDFEIENSPFDFRISFSSEKNVPNKNYTSKEGLFTRVKERTRYTLKDVYFDLTVVTTENNAVVNKTYEIEIEIKPNDKSCLYNSINLVLKTIDVINMCENIGKTPCITSI | Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
EC: 3.6.1.74
Subcellular Location: Nucleus
Sequence Length: 203
Sequence Mass (Da): 23828
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A0A7M5URV9 | MAPRLLHPGPIFALSIIGFCFLTSIITILSWLPPNNTKNILNGVIFHFWVLNILKNFFKASFMGPGHIEFKWKPKRKSDEKLLQYCECCEGYKAPRAHHCKTCKRCVMKMDHHCPWINNCVGHYNHKSFTYFLFFVVVGCSHAAVMMILCIIDHITSKNGYILLRVYEEAMIRMNHYLIIMLFFGIGLSVGCTLAVSFLLYYQVKSIVKNRTGIEDWIVEKAISRNKHIGRTFVYPYDLGKKENIKQVVLWSADYTGDGITWPVVKGCDQYTLTIEQLEQKDLKRDRMVPYHVTKSYSGTWCPLMLGCRVLYDCPWSDEARLKVNEGDTFFGSRHKKHWIYGERVLDEDSKEVQEHKLGELRRKKGWVPRVHLQPIDDKDEETSSDDDRRIEQLKKDKERTKKQGKESKKKR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 412
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 48196
Location Topology: Multi-pass membrane protein
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A0A7Y8LPP7 | MENPKAKILCVDDDADLLQLNSTILQSAGYEVIEACSGNECLQRIKEIRPDLVLLDVMLPDADGFELCKKIKEDPEMFGTYVILISGMEISSGSQVKGLEIGADGYITRPITAPELIARIQAILRIKITEMALRKSMERYQMLIETMNEGLGIVNENMIVTFINDKLCELTGYAKNEIIGNPLLAFFNLENQEILRNEFNKVRNNICKPFEIKGKKKNGRDFYVIFSPRAIFDSSGEFKGAFAVLTDITRNKEIEEANTKNFIRLKTIMDSVGDGIYGVDRNGKTIFVNPALLRMTGYSEKELIGRNLHYILRHTKSDGSAYEREDCPILMTLLKGETFFNITDEVVWRKDGSRFPVEYTSAPIVEQDRITGAVVVIRDITERMQAEEEIKRLNKDLEHRVVQRTRQLEAVIRELEDEIFERKRTEEKISKYADRLKTLSNRLIEIQEAERKYIARELHEGIGQTLNGLKNVLDMMVNTRPNANEALFDIQNTVKDLLVRVRNMSLDLRPFMLDDMGILPALLWHFDRFQTQTKIRVRFSHDGLNIRFRPEVETAAYRVVQEALMNVARHSCADEVIVFIKADSNNLTINIEDKGIGFDYSAVKALGNSAGLKWMQERISLLGGKLFIESSKGKGTRLTVTLPLTDMF | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 648
Sequence Mass (Da): 73948
|
A0A7X8JQC3 | MFEDTRVTGTEVNYYFVCTKKLWFFTHGIQMEQTSDRVYMGKLMHEDSFAREDKEILIDGTIKLDFIKKSLEVHESKLTNSMQEATLYQILYYIYYLKGKGVENIKGFVHFPKSKRKEEVQLTEEYEQELQEVIQRILEIKQSSKPPSVEEKKICKKCSYYNLCFC | 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 complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
EC: 3.1.12.1
Sequence Length: 166
Sequence Mass (Da): 19806
|
A0A9E5YNN8 | HETLIVAKERAEDMIDGEYEVLEELKGSDLVGLEYNPLFPYFVDSEKAFRVVSAEFVNTEDGTGIVHIAPGFGDDDFRLGQDEGLDIIRHVNIDGTFTDDVVDFAGDQAKPSDKKIVEWLASRGLVYTTKQIRHSYPHCWRCDTPLLNYATESWFVKVSEMNNDLLNTNAETRWVPESIKDGRFGNWLEGARDWSVSRSRYWGTPLPVWKSETSGDIIVVGSVAELEELTGKKVDNLHKHIVDDYVFEKDGQTYRRIPEVLDCWFESGSMPYAQQHYPFENKEKFEAGFPADFIAEGQDQTRGWFYTLHVLATTLFNKPAFKNVIVNGIVLAENGKKMSKKLKNYPDPMEVIHAYGADAVRFYLASSPVMRAENLRFKEHGVKEVSNKLIGTLNNVLSFYKLFVTGVPEEVEKEDLHALDRWVLSKLALTRNNVTKYIEEYELSSAAREIQEFVTELSQWYVRRSRDRFKGDDKDSAVAARVLYRTLSTLSQLIAPFVPFMAEHIYRGLHDRDEADSVHLTMWPTVKDLDFFDQEALDNMSTVRDLVRKALEARESAKIPVRQVLGSLVVNSPTELDSAYLEIVADEVNVQNVTWKKGSQLGVDLDVELTPELVQLGLVREVTRTVNSMRKELKLTIEDEIVLQWETEDGNAITMFEKFGKDISDKARAFKVLQGLDGAEQTGQVETEDGVIELGITKA | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
EC: 6.1.1.5
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Sequence Length: 699
Sequence Mass (Da): 79519
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A0A7V2MED1 | MASTPASWIELQASAFRHNVLALKKKAGSAKLMPIVKANAYGHGLSQVAVLAKKWPIWGLGVAHGSEALQLRKAGYRGRVLVLSAWDSKELLTLAKMGIEVVVNDFTTLNQVISFGRRAGSRLIRIHIKLDSGTSRLGFLPSDLRRVKKLLNDLPRTIIVESLWSHLSSSEDQASHVTEDQLVQFLTMTKALPPTRYRHIACTAALIRFPDTRLSLSRAGIGIYGIWPSPPTRQAAKGVTLKPVLRWYTTVRQVKNLPKGAYIGYSRTARLKRAGRIAILPIGYADGYDRRLSNRGQVWIAGHQYPVIGRVSMNLTMVDISGSRIAVGEPVELIGPHVTADRMATIIGTIPYEVLARLSPAIPRYTV | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 367
Sequence Mass (Da): 40434
|
A0A847WDZ3 | REKRWERVERAYNAIVFGEGKQEPDAVKAVAESYAAGVTDEFIEPVIVNPEGIVKDGDTVFFMNFRADRARELTRAFVDADFKEFKRRANPSVNFICLTQYDEDMPNVSVAYPPEFPHNTLGEFLSGLGRTQLRIAETTKYAHVTLFFNGGKEQKFIGEDRVLIQTSKDFATFDLIPQMKAFEVAEEACKRIASGKYDLVVVNFANCDMVGHTGNFDAVVKAVEAVDKCVGQTVEATEDAGGIAIITADHGNAEQMLEEDGSPHTAHTLNLVPFIIRGADVRLKDGRLCDIAPTILELMGLEQPAEMTGVSLIK | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 314
Sequence Mass (Da): 34730
|
A0A933S6P1 | MSYQVSARKYRPQSFAEVVGQPHIVRTLSNAISANRVAHAYLFSGVRGVGKTTVARVFAKALNCENGPTPTPCNRCEPCRQVTQGTAADVLEIDGASNNGVDAVRDLTDNIRYRPLACRYKIYIIDEVHMLSTAAFNALLKTLEEPPDHAVFIFATTETHKIPRTILSRCQHHAFRRIGREEIGGHLAQVARQDGIEASRTAIGMLARAADGSMRDGLSLFDQAVSFGDGRITQDDLTLMLGVVGQDTLTALAAELLAGDAGAALARLRNLIGAGHDLQILAAELVEHFRNLLMCRVSDAPEDLIDLAADDVADLGAQAQGAPQEVIEQVLALLTDAQERCRRALNPRFVLEAALVRCCQAPRLMDLGELLARLEGSTADTPRPAAPAPRAPQRPAPAAAAPRPEPARPAPPQPAVAAPPPP | 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: 422
Sequence Mass (Da): 45224
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A0A2N2DY37 | MKFWIRAIRPHTLSATIIPVTMGAVLVIKEGVFHWGYLLLSLITMILIQSAVNLINDHDDYINKVDTKESLGSSRVVAEEKLTAKELYIVGSILVAVAFVLGVIISAQRGWFIFVIGLCGIALVYSYTGKPLRLKYRGLGFIIIFIVFGPLALMGSYYVQALTLSREALILSIPIGMLTTAILQANDLRDMQHDKLAGIKTLSIIIGKERGETVYRGLILLPYAFLIAMIFFDTLPNWSVMVFLTLPSANSNIKTFSNPGKMTSNIIELDKKTAQLQAQFGVLLIASVLL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell membrane
Sequence Length: 290
Sequence Mass (Da): 32038
Location Topology: Multi-pass membrane protein
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A0A7J4EJP1 | MKKTFAVLVENKPGVLARISGLFSRRGFNIDSLVVGTTEKPDISRMTIVVEG | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 52
Sequence Mass (Da): 5679
|
A0A7M5VDK8 | FRKVELNRKSLQQKMRHSCLLLLLFVVSTNCRYYLDDSNRDYLANLINQERFRDSRQDSYDYDYQRYNNDYTQKRNDFSSTRNKFMNILSDILEARKEENGLHHAASVVEQQHIPSAQEKSNIKKPDVEKHKLLMPGVSPQKPDTYLCYAQKMSDDDQYITKFEPLADMKVAHHMLLFSCDEPFQKDKVWGCREMAPVCKSGMQMIKYAWGKNAPSLEMPKDVAFHVGGKSPVKYLVLQVHYLNVDSFKDGKTKDHSGLIYTTTTQKPSYFAGIYLLAAGWPPIPPHKDKFHMDMECGYKSSKQMKIYPFRFRVHAHKLGAVITAYRVRNGKYTLIGRGDPQRPQAFYKVDNDLDIKDGDDVIGRCTFNSTSRDTVTNIGATHKDEMCNFYIMMFYKADYGDQNPGCMQTTDSFSYPDDSDVTLAEMERKGSMYLHEHSFKEVDGWPKGLKAGQVGQIAGVEVNKDHVIIFHRGGRKWDQNSFDAQNKLASALQEPISDDTLVWLDRHTGEFVKSMGAHLFYMPHGITLDQSGNIWLTDVGAHQVFKLSPEGKVLLVVGERFVPGDDGKHFCKPTDVVVVQETGEFFVSDGYCNQRVVKFDKTGSKMLMEISPKSISHLNPPSMRIVHSLAFDEENNRLYVADRENNRVLVFNSQDGDYVWQIAFKEAVYAVAVNKKDNVLHAVTTNYVDPKKTSGYTYHLKSKSFITTWKPPAGFGRPHDLAVSKDDNEIYVSEIGPNRVIKFASKQAQKTRP | Cofactor: Binds 2 Cu(2+) ions per subunit.
Catalytic Activity: a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 754
Sequence Mass (Da): 86303
Location Topology: Single-pass membrane protein
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A0A1M6IVN7 | MSKSVRVIEVKGRRIGGDRLQICVPLVAKTEAELLKEASSIAALKPDLVEWRVDFLEVVESIPDVLDILLQLRNRLLEYPIIFTCRTHLEGGYRSIDENIRLQLIKKAIKSGRIDMVDIELISGEKVIQDIIDTARLNHVYVILSNHDFQKTPPINTMVERLKKAQDLGADIAKIAVMPNSMEDVLNLLYATNSMKEQYAHIPIITMAMSGKGLITRIGGGIFGSAVTFGAGKAASAPGQIAKEELETAIEILYKNL | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 257
Sequence Mass (Da): 28462
|
A0A2N1V4C7 | MDNRPIGVFDSGVGGVSVLRTLIELMPNEEFIYLGDTEKVPYGTKSREEIVQYSLDCAEFLKSKNVKMTVVACNTASNNARVELKERFENIRLVDLVKPILAIEFEEDEICHIGIIATEATINNAHFRKSLEEPEDSGKVKLFKKAGPKFVELVENNEIHTDKADHIIEEYMAPLLLENIDVLVLGCTHYQFLKKKIQTFAPDLHIVDPSEWAAHDTYKELKHREMLTDKTNDKNVKFYISKESPEFRDLASSLLEFECSEPQIVSIH | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 268
Sequence Mass (Da): 30616
|
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