ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7V5F1K6 | SRLADSRASASDVPPGTVIGPLTMACGNGAAEITRAQRPGKRAMEAEDFLRGFEMPDRVD | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A7J5XDV9 | MEYFPSTFFVLSPHRPTMSGDTGDSGPGEVEPMPGYLYLINRASTVMFGAWRDCSSCGLELSKRTLLDNAYITFTEIALFFFCAFLWTQVRRGLTESLFQPLARWCRLLPKDAAKMPESAWKLVFYTMSWSYSTYLLFFTSYSFFHDPPSVFYTGVEAGVEAGVEAGVEAGWKLGWKLGWKLGWKLGWKLGWSWGGSWGGSWGGAGVEAGVEAGVEAGVEAGVDAPQLGWKLGWKLGRKLGWKLGWKLGRKLGWRLGWRLGWKLGGSWGRSWGGSGVEAGVEAGVEAGVEAGVEAGVEAGVEAGVELGWKLGWKLGWSWG... | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Membrane
Sequence Length: 751
Sequence Mass (Da): 80249
Location Topology: Multi-pass membrane protein
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A0A7J5YR52 | MHIAQLKEFLSQKTPSPSKSPGNKGPADTPSSRTPGPSSTLSKDPEVEACPICMEAIENTEKKTLQCKHSFCRDCLKRAFDYKPVCPTCGALYGTLTGTQPDGGRMDVTKSSSSLPGYEKYGTITINYYIPSGIQKPYEGASRTAYLPDSSEGRGVLKLLTRAFSQKLIFTVGRSTTSGRNNI | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A7J5XZB6 | MHVELSFKAPSKHGSGLQPCPVEDTDRLSPALSKVLTRGDGAPWEERRWTENSGFVLLSVSVRRGEERREGDLECWNHQPPFFCRGCGKSRSRCRILEPVAQQISHLVIMHEEGEVDGKAIPDLTVPVAAVQAAVSNLVRVGKETVQTTEDQVMKRDMPPAFIKVENSSSKLVQAAQMLKADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLITYTKNLGPGMTKMSKMIEERQQELTHQEHRQMLVNSMGTVKELLPVLISAIKIFVSTKTSRGAVLKRQDEPEIYL | Function: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular Location: Cell junction
Sequence... |
R7FA11 | MVKLNVLHMYPDLLNLYGDGGNMEILKYRCAMRNIECQVDKCDIDQDMQDFSGYDMIYLGGGADLEQNIVSSALMKSKDGIRRAYENGAFLLMICGGYQLMGQFYRDSNGTETPGVGLFSYYTTASTNKSARCIGNIIIDANLGGRQTRIIGFENHGGMTEHVETPLGRVLYGNGNVSGGTYEGYFEKNVIATYLHGPLLSKNPAVADYIIQYCMERKLGYPVTLPQLDDTIEEEGREVMFQRLLKENAE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is chan... |
F4NUN2 | MPSTNNQRSSNSSRSQGSSLLKRRQRWWRWGLSSTRLILLLLVIALGLLLLERSGVGTANNADSTVLKNSNTKEKSFDSSTDDGRRVILKDFHIQNTTPPKPKLTYEQRRFLQTIPQRTPPDLERGQAYFTSGMSSKITTALKLSKIKITGFNYCKMLDGSIFNAMVYLHPLKGSIATLNPLVKTVISLLDDTAEKITEFIKIKFETVDVLEAHRYACYAVAEGNNPSANLTDVRFVVSFDPNEFFHTALPSIRPTAPLVTPSKKRYLVAFLIMVHEDAGLHQLKMLIDLLDDGNAIILIHVDKSAQDLYIRISEYLADR... | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Membrane
Sequence Length: 973
Sequence Mass (Da): 110813
Location Topology: Single-pass type II membrane prote... |
K1X4Y4 | MACHDATLLAKSQGPRFWESWDDMTVYQASVHGDLDQDGGDRNGQRANYYQLQGPFVPKAFGFLAVLLGDRSFFASPGALILKHFILYLTTPPQAHPSTWPRNTLFENSAKFGPATTTAHFTAPNSWRCGVIRAQVDAPLARHLSIIMTIHSFKMPSTLSTSVLALASAAAVSAHGFVKGITVDGVYTTGWLVDYAYNPNPPKSIGWSEAALDHGFVPSDKAGHPDIICHLNGTNAELSATVAAGTTIDLHWSGWPDSHRGPICNYMANCHGDCATVDKTTLEWFKVDEKGYENGVWASDELIAKDAIWPFPVPASIAPG... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
A0A0C3B2U7 | MPHNATLQGFFDTNGKWAEAVSQHDSSFFQKSAEGQKPKVLWIGCADSRVPESVVMACKPGEVFVHRNIANQFHPNDDSAISVLTYAVENLGIKHIVVVGHTQCGGVNGAFELACNPSAAASTGNSPLGRWLTPLINLAKSHNLPSQGKEAGVPKLLDASIKTQVDNIAATSVVQNAWANGNPVTIHGWLYNLESGKLQDLDYDIQAPWDQ | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 211
Sequence Mass (Da): 22696
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A0A0C3BQA8 | MNTLITACFAILFLVILRVIFVIRHPPTPRFSPGQTCHLTVFLGSGGHTSEMLQMLRGLDVERYEPRTYVVSEGDQFSAVKAAELESSFPFSPKFEVFTIPRARKVLQPLKTVPMTAIVSLYACMWLVTFKPLLKRQSFGDLLLLNGPGTCVPLFIAIFINRALVGRFLVQWPALASKKADYAGWLI | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 187
Sequence Mass (Da): 20949
Location Topology: Single-pass membrane protein
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A0A6N0HW54 | MDQLRLILLIAGVVLIAGIYFVGKQRRRRQADRQPDPLDESVSFEEEFDLPPMSSVEAARDKSIDELGDLDSFSASGEKFEIDEQEPPVLDNPVQAELPSIDTEQRTPEEEEVDADKVVAIYIAAPRGTPFTGTALRPAFEAVGLEYGAMQIFHHRVEGGGVFSLASLVEPGYFEPEKMGDDYATPGLSIFMPLPGRGDAIKTLDTMLESAHTLADRLGGDLLDETKSVLSRQTASHMREEVQDYLLHRKLEQQAANK | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
F4P4X1 | MSAVDTTESAAAEVNAAKFGHDTASNMSIHSIANTPDMSATNCNESCTSSTPSDNNPNHDSAAHVTTWSRLSGGLSLLMTRALHSIQSLDMASELSRFTKYHRPYLSSAASSGIPTLDPNSPIVFLAQTYSSLAHPHFLDDFHSRLWMTYRKGFAAIKPTGYTCDSGWGCMLRSGQMLVANALLFHELGRDWRLGDSNDRDTWLTYCSILTKFLDVNTSPYSIQRIATLGIRFDKQIGEWFGPSTISQVLKVLVNDDQRISLKVHVSNDGVVYKNEINTILSATRDDGKTPAVLIMIPLRLGVETMNPVYYPGVKHCFAM... | Function: Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Catalytic Activity... |
A0A659SD78 | KPTCTLCPLQNGCIAAAHESWSRYPGKKPKQTLPERTGYFLLLQHNQEIFLAQRPPSGLWGGLYCFPQFASEDELREWLAQRHVNADNLTQLNAFRHTFSHFHLDIVPMWLPVSSLDACMDEGSALWYNLAQPPSVGLAAPVERLLQQLRTGAPV | 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: 155
Sequence Mass (Da): 17481
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F2JKT9 | MQNEKKLFTTQNMMRMALLSVIAVLLMQFGALKLPMIFPSFLELDFSEVPAIIGVLTIHPLAGFVIVILKNILKVVLFQTNTAYAGELANMVVSLGYILPLSLMVMKKRDFKTITIGICVGIIGLTLAGAIVNYFITVPMYAKLFMPMDAIIGMGNAIYSGIVDKGTLILYSFIPFNLLKGSVVSVVSIIIVKGLQPVIKHFGYHIRG | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 208
Sequence Mass (Da): 22801
Location Topology: Multi-pass membrane protein
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A0A3D5Z247 | MKVFITSAFILCVLFQINPVFGNATKSIQKILNAKPDTNKVKSLSDLCWDYRFKSADSALFFGEQALQLATQLSYPRGIAQAYNDMAVIHINRSNFRSATNFLNEAMKIRQQMNDSSGVAALYNKLGIIAQKQGRLKDALQNQIDALKIYQQLKHDKWIGYSLNNIAIIHQNLENHEKALEYHRKALEYRISLKDQEGEATSYGNMANLFARMHDTIQAINYYEKALALSRELKKDELVSANLSNIGNIYMARKEFNKALGLFNESLLIKEKIGDPKGISSTLSRIGTVYTETGRFKEAAVTLNRSLKMAQNTVVLEEEL... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A914BWB1 | MKKLEDRLLSIFKLDKTGTIFYFDASTTTTKSLLRVLCRWRGSIWKATLKQLCVWTILYMAISILYRYVMSESWQRYFEALSAYLNNDINTMIPLTFMLGFFVASVVKRWSLMLNSFGWIDDSAIAIATFIRDNDEDTLMLKRNLIRYMVLNQALVLRDISIQVRYRFPTLETLVAAGLLTTEELKKLISIPDVYSQYWLPIQWVCDHLVKAHQDGKIKGEKLLDTIIMKVQKFREGLSELLRYDWVPIPLVYPQVILFSVRLYFGICLISRQFLLPNHAKNKDSVDLWIPFTTMLQFIVYMGWMKVAEALMNPLGEDDD... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 471
Sequence Mass (Da): 54424
Location Topology: Multi-pass membrane protein
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A0A5M6A8F1 | MFGAMLSDLKRMLSNHKIFFQEGVSLAEKTWIRRGGIVKYWIVPTSVEKLVVLVKYLYVNKLFFELVGHTSNIYFLNNYNPDIVISTRKINCFFDNDDVLICDCGVSMKILSKYCIEHGYRGFEGLIDLPGTVAAAVYNNSGCFKCSVSDLLIKVDFLDKNGDLIELNSRQMKFTHRSSCFKTKEMEGVILRVYLKKIKSDSVKLARIAADNRQYRKMYQESPKQNLGSTFATIPFKKNPLLFVSVLTKICVVFKVDKKRKWVLIKYILLFIYGKLELSRYISDYSLNRFVWIDEQADEKFWLYKLFIERISNSPQLEIE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 325
Sequence Mass (Da): 37912
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A0A5C6C6H3 | MACWKKRSVYENHIKTWRRSLVRRILITGAGGFLGKNLVAHLSQREDVSLQLFGSENSNDELHDWVSTADVIFHLAGVNRPENVEEFDTGNAGFTQTLVDAIKASGRKPHVIVSSSIQAALDNPYGNSKRRGEQILQRFSEQTGAPVSIFRLKNLFGKWCRPNYNSVTATFCHNLANDLPIEISNPEHQLDLAYVDDVVAAFIEEMETRPERIDGMVDPDPVPSYQISLGDLASRIQFFRDMQQTQLLPDYSVLFNKQLYATYLSYLPRDRWEYGPQKIHADDRGNLAELIKSPQFGQIFISRTKPGITRGMHYHHTKTE... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 396
Sequence Mass (Da): 45213
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A0A7K3H1Q5 | FRFVSNVDGADLHEAVRDLDPAETLFIVASKTFTTIETITNATSARSWLLDAFDGDEKAVAKHFVALSTNAEKVSGFGIDTANMFEFWDWVGGRYSYDSAIGLSLMIAIGPDRFREMLDGFRIVDEHFQNAEAPANAPLLLGLLGVWYGNFLDAQSHAVLPYSHYLSKFTAYLQQLDMESNGKSVDREGREVEWQTGPVVWGTPGTNGQHAYYQLIHQGTKLIPADFIGFAEPVGELSDGLKAQHDLLMANFFAQTQALAFGKTADEVRAEGVP | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 274
Sequence Mass (Da): 30192
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A0A263DNV4 | MEIAELVRRLARLQVSSLSDADKTLPVCDPAIGPLLPDVTLVGTAFTVRSDGDLLGMIDAIGQAGPGTVLVAATDGSPLAASGELFATEGRRRGLAGIAVDGWCRDLRGLRRVGLPVFARGTTPAAGPAAGPAVVQVPVRFGGVEVQPGDLVFGDDDGLLIAPPERVAAALERAEEIERVEAEVAAAVGSGRSLHEVTNAAEHLRAVAAGEPSTFRFQP | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A7J5YHM0 | MCEHVTVKLLRGRAECGAEGEGRRDGWRKGGTGALFFVFFHHPSVFEMCFLPSYSSACPSTPSPSPSPSPSPSPSPLSPPPRLPPAVMAERLIDQQQQQPDQKHTVTHGHAQRGASECVFVSTRQPHTTACLELFEQERPLHQRCSQIKHSYANIISLSSMCVGGGDEVIENLDISISTTSFPPICKKNIRLQDFTIMYFTAIAALMVILVASYQGPTNAVEVSDLKINPSGPLPPLPMPFRMSLDPRGDVQLSWNISYANQEIYIQLTVADIKHGVVFGMSDRGELTNADLVDAWSDSEGHVSLDSQQDYELLDAKHKP... | Pathway: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
Function: Conversion of dopamine to noradrenaline.
Catalytic Activity: dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radical
EC: 1.14.17.1
Subcellular Location: Cytoplasm... |
A0A7K1JQV7 | MPGSGLWRTKSVEQSIADTDEPETKLRRDLTWWDLTVFGVSVVIGAGIFTVTASTAANITGPAISLSFVMAAIGCGLAAMCYAEFASTIPVAGSAYTFSYATFGEFAAWILGWDLILEFSVGAATVAKGWSKYLVEVFNLPSATVHLGPVRLDWGALLIVAVLTLLLAIGTKLSARVSAIITAVKVAVVLLVIVVGAFFIKASNYSPYIPPPETGDSSGGSWLNQTLFSFLAGGPGGHYGLFGVLAGASIVFFAFIGFDVVATTAEETRNPQKDVPRGILGSLVIVTVLYVAVTVVLSGMVKYTELRAADEHPTLSTAFR... | Function: Probable amino-acid or metabolite transport protein.
Subcellular Location: Membrane
Sequence Length: 492
Sequence Mass (Da): 52076
Location Topology: Multi-pass membrane protein
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A0A7J5Z9F9 | MNGTDMEEIPFQKVKTRRKRSHCPTGVPLTTIACEDEFDCKELESLFQNYNLKLEQTSALKALAVLIFMSSTLALVELLSGPSLTISKGSHPVHCVIFVSLFIVTNVKYLQVTQLQQIVNLALLFSFTFSFLCCPFSLGAMGMEPPTSPEQGVWQLILVTFVAYALLPVRTLLAVVFGIMVSVSHLIVTATSVTAKTQKLWRTLVANTVLFTSVNLSGLFVRILTERAQRKAFLQARGCIEERLRMEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTSLASQCTAQELVKLLNE... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 350
Sequence Mass (Da): 39371
Location Topology: Multi-pass membrane protein
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A0A4Y7NKR5 | MAEDREVLREIWEGKLPVCFTLATEEVSIPVTPDPFYLMVPRLTYFPIVTEKVRRHFVRCVAADKSDNEMWLEFENQPLKWHYPIGLLYDMYVTDSALPWQITVHFEKYPDNKIMRCPSKDFVESHLMHSLKEADALKHKSHLMALMQERDHKQLWLGLLHDRFDQFWSANRKLMESAGDEGFRYIPFRLYAPELTSKPYIQFLIRPEDNEKKSTIEDLLRKASLFLSNK | Function: Involved in autophagic vesicle formation.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 230
Sequence Mass (Da): 27383
Location Topology: Peripheral membrane protein
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W6MI62 | MQYWGWLDSAFIVLISTYLVLAPYSKVEESFSLQAVYDMLNHGYADLELYDHKTFEGAVPRSFFGPLLISVIVKPIKPLLDKYYPDPTELNLQLLVRGVIGLTNGLSLIRLRRSLAASCALNSKYISVWFAVLQYSQFHIVYYASRSLPNFLALPFVNHALAYIVKGEFVPGVTWMCFTGVVMRLEVGLYGCCFALMSVLLGQSSLITTLGGMVAGSLVGLGTTLFVDSYFWGHLEFPELTAFIYNVVEGNSQNWGVEPFSAYFFKYSRALFFPPIVPIMLVKGLTKDPSQNGKGNTIRTICISSLLFVFVMSFQAHKEW... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 557
Sequence Mass (Da): 62149
Location Topology: Multi-pass membrane protein
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A0A1Q2SJS0 | MSYWLASVRSLAEAKWLLESSNIPDILDLKDSEKEALSPLPTSLIRQIVNLTQNRCQVSATIGGLPMNPMLISNTIKEVAATGVNYIKISLFLDDRISNYLAVLQPMTAQGISLVGVVFADQYPLPLFSGIPLIRQAGFKGIMIDTAIKNGYNLLTYFSIKELDNFIKLAHNNGLASGLAGSLQIRDIPILLSLKPDYLGFRSALCYRGQRDSNLSLKAISLLKRMLEDNYT | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
EC: 4.2.3.153
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Length: 232
Sequence Mass ... |
A0A7X3MLX0 | MKIAFWRNLTVFEGEITMTIRDIAKAAGVSAATVSRIINHKDENISEETRRRVLQIIEEHEYVPYAKVRDRLLQSNRTIGVILPSLGSPFFASFIEHIQTLAASDNYTLSLYLTQNRPKLEEQAILHFLDIHALGILYFPESDNGIAALKHSQDQLRSAVLMDCETPEFPFPQVYRDFFNIAKTGTTALLKQNNRRLVLLLSGEGSFRVHEQLADGYREAMLSYGITPDDSTILKADDSFHTAFEQLTDAGIDGVICQNAYLTSEVYCIASRKHFLIPSDLSVLCLEDSISLEQLLPPVTAIRTDISQMAKTAYHTLLSQ... | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A2E9GBF8 | MYLRLIKIIWFTFFAGLIALVLYVASVYGNWNNLYGGLPDFKELENPKNELASLLYTADGKIMGKYFIENRDPVKYRQLSPNLVDALKAVEDVRFEMHSGIDFRSLTRVFYGLVTFDRKGGGSTLTQQLAKILFSTRGELSNGQLNDIPYLNILISKTKEWILAIELERAYTKEEIMTMYLNTASFSGNIFGIKAASKTFFNTIPDSLDILQAATLSGMLQAPSRFNPYRNPENAKVRRNTVLAQMEKYGFLNETQLDTLSKKPVTVEYKMESHNTGYATYFRNEIAKDLKKWCATHYKPNGEPYNLYTDGLKIYTTIDS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A2S6QCJ9 | MRSLVAANGVMVSPPSDQKNGELIPRLLSTLVLVPPTLIAIYLGSPWFEIIVGIVALLMAWEWARICSNGQFHLSGWLVIAGVIGTIGTMVLGVPSAALIWIFVSTVVVFFLQYLGSSKSLAIGIVLIGAFTLSVLWIRGLPETGRVLTIWLAFTVWCTDIGGYFVGRGIGGAKLAPRLSPNKTWAGLVGGLVLASIWSGLWLSGAGYTDYVTGMAVGIGVAVFAQLGDLLVSAVKRKYQVKDSSSIIPGHGGVLDRLDSMLLTTPMVAIVLLMFGGGGA | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 280
Sequence Mass (... |
A0A368NQX7 | MANVERGINRLLSLRLALLGWESKLGVDVTEQSALLVANVTLRANELSLLLNFANTRIGELAAELPKATSYEKEDIEYALRRLRIKREICTESIEAAVTVLESLDVNSDYFKQVLITSTGAVSEDIFEVKVLSRLLENWTEAATNWFGENSISFIVKLIVFCAILFGFHLLADVARTVATKAVSNSKLKLSKLLQEFFISMAGKVVFFIGLMIGLSQLGVQLAPLLAGFGVAGIVIGFALQGTLSNFASGMMILIYRPFDVGDMVIAGGVQGNVKKLSLVSATIQTIDNQRIVVPNNMIWNDVITNITAEKVRRVDMVFG... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A7J5YSK9 | MMILPRRGSDRVPDSVVLVIFVVAASLGTVFAKDTAFVEVVLFESSPNGDYTTYTTGLQGRFSKAGATISAEGEIVQMHPLGLCNNNDEEDLYEYGWVGVVKLEQPELDPSCLTVLGKAKRAVQRGATAVIFDVSENPDAIDQLNQVAEDPLKRPVVYVKGNDAVKLMNIVNKQKVARARIQHRPPRQPTEYFDMGIFLAFFVVVSLVCLILLIKIKLKQRRSQSSMNRMAIQALEKMETRKFKAKGKGQRESSCGASDSLSSSSTSDCAICLEKYIDGEELRVIPCAHRFHKKCVDPWLLQHHTCPHCRHNIIGKTIFS... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cell membrane
Sequence Len... |
A0A7J5YQL4 | MYCCVFFQDFAKTIPGHGGIMDRFDCQYLMATFLSYVMSGWRYFVCPVEFNNDSNRFQVDCEPSELFQLQDYALPSILESFIGWTTVRLYPFQIHSIALSSFASIMGPFGGFFASSRDF | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 119
Sequence Mass (Da): 13720
Location Topology: Multi-pass membrane protein
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A0A4R6QTX2 | MKSLSLLLQRLVATALIGLTMTAAASAQSLDLWRVLPGERGIPVMPGDATPVGATCADNDTAAALAAPLALADAIRIALCSNPRARQAWLDAAAQAATVGLSKAAYLPTVNASLSKSYDAVRTPGSFNSQRSGNQVHGANLTLSWLLLDSGGRAANVRQAEQNLAAAMAGHDGLLQSLFVGTAQAYYEAAAASASVRAAQQAEDTARESAQATETKLQLGAATVVDMLQARTALSQATLARVRVEGQARTSLGALAHVMGIDVRSPLQLAADADLDPLASTERPVAEDYLQQLDSLINEALAAHPTLLAARAQLASAEAR... | Function: CyaE is necessary for transport of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin).
Subcellular Location: Cell outer membrane
Sequence Length: 488
Sequence Mass (Da): 51489
Location Topology: Peripheral membrane protein
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A0A1F7L7I5 | MRRLLVVCVGVVLSGCAGMMAEKEPPMLPSAGATLKDKDGKQVGSATLIETAEGLRIAVTGYRMPPGEHGIHIHAVGRCEPPGFESAGGHFNPAGKQHGLQNPAGPHAGDLPNLKVAPFGEGGIDVPMKAATLGAGPTSLLGGTGTSIVVHAAADDGKTDPAGNSGARIACGVIAK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 176
Sequence Mass (Da): 17540
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A0A8T3VMZ0 | MESLKEDIIRQMDEMEENRAEKIHEMFKKSKKNQMSENINEENIDEEIQKLEKANRIISTYQRFMDAFEKDLDIDPGRLMGLTDGIFSIVMTLLIFGMALPENEIANYTGFMNFIGSISPIAGVVIVSFILLASFWIYHHEFLKIKRLNIPYLWMNMFYLASLCFIPFTTSLIGNYSHFFLANVIFGVNILLVVGFFLLNFYYAQKRGFLEEYTSEEDKKHVFNTLCIIMGLTVIVNLLDFNVNPNFIYLFLLVPIISTIRHIQYIMK | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 268
Sequence Mass (Da): 31392
Location Topology: Multi-pass membrane protein
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A0A961K3M8 | MGLAPLTLHLFVVVFAMMSTVTPPVALAAFAAAPIANANPIRTGFEAARIALAGFLIPFVFVYHPAVLYKLQVLFQWFGEEAVSSRAMIDITTVSWGDLGWIVVAFTLAMWLVASALAGFDRARLGTAERVARGIVGLVALTPQMGLAVPAAAIGILLIFREWAAHRLTARATP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 174
Sequence Mass (Da): 18559
Location Topology: Multi-pass membrane protein
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A0A191ZIA7 | MIQVQDRLPEATLHCRGPQGLDGCSIGELTADQRIVLFAVPGAFTPTCSDKHVPGFLALNEEIRARGIDEIVCVSVNDPFVMKFWAEHLGVGGAIRFLSDGNGMFTRSIGMERDMSGGAMGMRSKRYAMIVSDGQVEWLGVDESGLQNASAESVLAALS | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
EC: 1.11.1.27
Catalytic Activity: a hydroperoxide + 2 glutathione = an alcohol + glutat... |
A0A6J0V4F4 | MRQNLQARAGGLIATEMMAGPKDSSPEDSLKIKPLKWPSGMGSPASLAEQEGRKSGLTTPEEDSRRTVGISKISANLCSSHSADSLDLSQDGSPKTLFNPPTSTNNELATSPACGRGEPLAKRVPQKGQAGEKKPESSCSSEMNRKSSHLHISQWKMSAGSEKRMELSQKRELPFAACRKALASPSCKDRLPRDALELEDVEDEGLVEEAYKMPDHSALNMLQVASKPIDFSLARELKTLFFGSSLGCFSKEWKIQSFAFNDNPQLKYGIVQKKGGPCGVLAAVQASVLGHLIFGDGVKNSDTRCLQPSEAHRTKCLTLA... | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting... |
A0A518K654 | MSDAKRYSFPKELRLRTGAEFDAVFKAKVSAGDGVLVIHARPNGLGHARLGLAVSRKVGGAVRRNRWKRCLREAFRLSQHDLPALDFVCLPRLRDKPTLAVVDAALRGLARRLEKKAAKQAQPSEGRS | 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... |
A0A058ZSB3 | MVIRMIIRMLSAATSPFTLLAAPLSFRLKTHLAFRPIRPPPPPSRPVSAAAPCGGFGSPGRSRRSFRGGVVATAAPGSVQKSEEWQAVLSPEQFRILRQKGTEYPGTGEYDKFFEEGLYNCAACGTPLYRSTTKFNSSCGWPAFYEGLPGAITCTVNLSLYQLNVWSQSDPDGMRTEITCTACGGHLGHVFKGEGFPTPTDDRHCVNSISLKFVLANSYPSQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantio... |
A0A928KXD6 | MSIFNQSQKAYLLLADGTVFEGRSFGAEGTSFGEVVFTTSVIGYQETVTDPTNFGKIVTQTFPLIGNYGVNDEDYESPKAQVSGYVVREWCNTPSNFRCKGNINDFLKEKNVIGIHSIDTRCLTRIIRDKGAMNAVITTENVNDKKDELLKQLAEFRPANAVKSVTCSENKVYTCENAEYKVAMIDLGCKNSLINEFTGRNCEVTLVPATVTADEIRALGVNGVVLSNGAGNPEENPEIIENVKEIAKLGIPMLGVCLGHQILAVSQGAKTEKMKYGHRGSNQPVVDKKLGKTFVTTQNHGYVVLSDSVTPEVGEISHVN... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 368
Sequence Mass (Da): 40285
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A0A2R4MF80 | MLNSSPLRAALIVIVALAGILFTLPNFVAPATLNSLPDWMPKKQIVLGLDLQGGSHLLLEVNREEIVSERVKELRREARSILANDNGIGHLIKTDEAKLTIELTDKENLETALNALQELDVPLSQSLGGVGGIDEMIINQTPDQLITIELTEEGISERLSSVVAQSIEVVRRRVDELGTTEPTIQRQGNDRILVQVPGFDDSERLKDVISKTARLTFHMVHPTMSAAQAKIQGLPDGTMILPSQDGGEELVFEEVAIGGESLVDSQPGFDAQNSSPIVTFRFDTRGGVKFAEITANNIGKRFAVVLDNQVITAPVINSAI... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 847
Sequence Mass (Da): 90785
Location... |
D4YNI8 | MSLRRVQAWIRILFRGIVRTFTHSLQVRVVAVTVVFTIVAIYGVGAYLSQQIARGLFESKQSDVSATTNGYVAELEALSGLSDSQEAADALNAQLRSMLSRSSLQLQAIALEPAGNSTVPPLVAITTGYEPMSVSDISPELRESIRESPAGNQKFQSAELAGTEAPGLIVAQRLTVNGQGDFILYTVADLTEEQGTLDFVQRALGVSGVVLSILVGGVAWLVTRFVVVPVKAGSEVARKIADGDLNQRMPVSGRDEIATLAQSFNDMADNLQDQIERMERLTVLQRQFVSDVSHELRTPLTTIHIASDMIFESRDEFDES... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 558
Sequence Mass (Da): 60467
Location Topology: Multi-pass membrane protein
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A0A922L6E8 | MTRLGKTLVLGVCLIGLWLRLLMMKEAETYLSRIHIQLMPIYTIILFGIISALIVLYRTFTFNGCPEAYEELKAEIKDAKNDLKQKGFEFK | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 91
Sequence Mass (Da): 10529
Location Topology: Multi-pass membrane prot... |
A0A1I8FU18 | IRNSSRRTIRTGVQTPLTGDWVLVSPHRAKRPWQGQTERREAGPAESSPVCMLIRCARVPLVPVAPLIQLHTGTYLFDNDFPALMPDTPAPPPPLLPSADGADADSDCGGVTSPWPGLPKADTEQVIRAWMAALTELAADYDWVQILENRGAVMGCSNPHAPLPDLVNCLSANRGQLKRTQITRNGNRPMLVDYVQQELRRKNESYSKTSTGSAWCLFGLFGRLRLCCYRNGTWLRLTDLNDGECLAEALKCLLTKYDNLFECSFPYSHGFHGAPTGSRLSGESGHWQLHAVFYPPLLRSATVKKFMVGYEMLAEAQRDL... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 341
Sequence Mass (Da): 37693
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A0A922IBN4 | MRNATPNPLRSFVEFNRTTTTTTTPSLSRDESQTLLNFSLEDAFDYIESYIFFALIILISFVHSDESPVLAKLYSINEQTRGSDIVLTCNVAKGSKPLRFQWFKNGVELSNTGRSTIENKDIFSFFTLRNIDSNDVGNYSSKPILNKFPASEINLSINSSYILPCSISSGSTSIFFEWYKDDHKKLSSTEYKIVIYDTMSSIVFKRLNSNDDTGTYTCNARNVHGTDSITTKLVIQDAPRISKLFSTELNQSEGSVLNIPCSVISGSTPLSFKWFKNEQELLRHRNPELSYQIKTDNFLSFLTISKLKAADSGNYSCIKN... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 805
Sequence Mass (Da): 92823
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A0A0S8DDU3 | MRVLEDFSLSNFSTIGIGGKSRYFTKVKNEDDMRRAFDFSNKKKIPFFVLGKGSNIVFDDKGFFGLIIKNEIDFLRIDKNRVEVGSGFSLQKLSRMVSKKNLSGLEFAGGIPATVGGAVYMNASSNNMEISSYLEEIRFLTIDGKIEIFKKKDLFFGYRYCSIKKKRGAIISLVFLFKNSFKVEKRLNKFLEKKKKMQPIYEKSAGCVFKNPKNNIAAKLIEGCGLKGKIIGDAKISNVHANFIVNSNNASSKDVLDLISLIVEEVKKKYEVELEKEIIYVPYV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 284
Sequence Mass (Da): 32167
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A0A517YZG6 | MKEQDIIKIMSGEDQSFVGKGMRCVMRSIEPIYSMAMTCRNKMFDHGIRQQHDLGRPTISIGNITTGGTGKTPFVTMLAEHLIKLGHRPAILMRGYHSDDSGSDEAMVYRNILGNKVVVEANPSRIKGAKTVLLNHPETSVFILDDGFQHRTASRQLDIVLIDATQPFGHKHVIPRGLLRESISSLKRADLIVLTRSDQVQNQEIKYINQTLTQITDQQSFIKTKHAWTHFLNNDDQIVPLNQVSTLNVLAITGIGNPNAFRSTLERHVKSIIHFKAMPDHHQYTNDDVSTILAQAKSNSSDALIMTEKDYVKFKPLIAD... | 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... |
A0A7X0VIC3 | MLQNLLLNVIIIIIPVVFFAIMLQYSGYHDQRGLAKYRYAIALVCGLSSVLCMLIPVVNADGFRWDLGAIPIGVAVLYGGRLPGAAAALIYAAANFATADGRFAAEMLSLAAALLYPYIGSGRYARSNLSVKLIGGLGASIAFYFVTLNLVLYLSDSFDASLRLDRLTFIVFQFLVIVALPIVLFLVEKQFVWAMFQERLRQAERLNMIGEMAASIAHEVRNPLTVVKGFLQLLSSSNDEKTRLYMTTSIAELDRAEFIISDYLNMAKNQPEERHPLDVCELVETAVQTMTPFAVMQSIELRHLCERDHYVQGDTVKFKQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 421
Sequence Mass (Da): 46437
Location Topology: Multi-pass membrane protein
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A0A655Q4W3 | MIDVPKDVMSPLNKLPYEYPETIKMRSYNPTTAGHKGQIKKGLRALLDAKKPVLYVGGGAIIANADQQIRQLAEALNLPVVSTLMGLGVFPGTHKNSLGMLGMHGVYEANMAMHNADLIFGVGVRFDDRTTNNLEKYCPNAKIMHIDIDPSSISKNVKVDLPIVGSADQVLDGMLKLLEESAERNDAAALDSWWNEIQVWRDRQCLAYETSAERIKPQQVIETLYKITEGKAILASDVGQHQMFAALYYPFDKPRQWINSGGLGTMGFGLPAGMGVKFAMPEEEVLVVTGDGSIQMNIQELSTALQYDIPVKIINLNNRF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 415
Sequence Mass (Da): 46129
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A0A951SX91 | MNWQQAFDENYWNISNLLSIVRVLLLPFFIYLTLLYVENATGALLSYIISIAILATATDFLDGFLARLLHQETIIGRYLDPICDKIVILSAMTLLLLYFELPVWVYSFYIGREIVGVWGGTFLYFKRNLQARPNIFGKIAVAMAALLTLWYYSVPYLKTVLSADDFFLDASPAAYLFVLIHVLGMIGYLQSYGKIIVAKN | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 200
Sequence Mass (Da): 22807
Location Topology: Multi-pass membrane protein
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A0A8J7X558 | MFVGIDDTDSIKGMCTTYLAAKLCHELDIIGSPKLVRLNPNIPYKTRGNAAIAFETNDLSAKKKVISLVKKYSMVSDSKTNPGVVFLESKKVPKKVKDFYSRVVSELVSIEDAEKVISAIKADTFKLKNGRGIIGALAAIGFNGEKTYEIIAYRKSKKEVKERKISRDSVVRMNDLFFPGVFDNLDVSGKRILITPKGRDPIFCGIRGRSKNIVCKAWDMIEPLEPIEFTQLFETNQATDAHLRIKKISEIKPYDCVIVSGTVSSNPKRVPGGHVIFGLTDKTGSIECAAYKPSRDFRDIASFLAVGDEIKVYGGISKYV... | Function: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Catalytic Activity: agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H... |
A0A267GGR8 | CRVACALSGGVDSAVSAYLLRQRGFQVTCVHMANWDELDETGHCSGERDLRDAQLVSKQLGLPFLRLNFTKEYWTRVFQHTLGEYESGRTPNPDVLCNRHIKFDCLYKYCIDELKFDALATGHYARTSFGDFLEHRQPGESVRLLCSADPVKDQTFWLCQVPQEALRRAAFPIGSLMKPDVKRLCSNIGLSSIATRRESAGICFIGKRNFSDFIDQYVERRPGRFVHLETGKELGQHDGVHHYTLGQRPRLAIDHRRYFVAKLCPNSRTVYLVDGVSHPSLYHRDMRCEPAHWIHSEPPELAATDQLHCQLRWQNKWRPI... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of t... |
A0A267ERF3 | MSDCGEKSEFNCDQLGLAAEDYEFGSHLGDGGFGRVYQATCKRTGKPVAIKVLDKRKVHQRNMTSRVISEISIHQRLRHQFVLQLYSYFEDTANVYIVLELCQGGNLHDYVRRNGCLSEDKVRYFLKQIVAGLCYLHRSGIIHRDLTLANLLLTEDCKVKISDFGLAAELSEDRTNKTMCGTPNYISPEVSSQGVQGPEVDVWSLGVMLYTMLVGKAPFDTKDPKSTIDNARRLKYDIPGSLHPEAIDLIAKLLRERPKERLTLAQVLQHPFMRDKAHERSTSNDSGNDSVQSGSHCLAASTPIPAAASSVATPSTPASV... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.21
Subcellular Location: Cytoplasm
Sequence Length: 757
Sequence Mass (Da): 82891
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A0A840I0W1 | MDRLLITGAHGQVGTYLTRLADAHGFVAIPLGSKDLDISDREAVARVIGAEKPDAVVNAAAYTAVDKAEGDEARTHAVNADGPANLAAACAGVPLLHFSTDYVFDGTGERPYREGDPTRPLGAYGRTKLAGEAAVRSAPLGTVMRTAWVYSDVGSNFLKTMIRVGRQRGALSVVSDQHGTPTHAGDIAEAALRIVRQQLEGREATAGLYHYTASGQTSWHGFAAAIFEALAAQTGERVALTAIPSSDYPTPAARPAYSVLDCALIEETFGVTRPDWHVPVAGTVEAVLKDDQ | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Seque... |
A0A2I0LUV9 | MTHQFPALSPEQKKALSDIAQRIVASGKGILAADESVGTMGNRLQRINVENTEENRRAFREILFSSDASINQSIGGVILFHETLYQKDSSGKPFPALIKEKGIVVGIKLDKGTAPLAGTNGETTIQGLDGLAERCAQYKKDGADFGKWRAVLKITSTTPSQLAIQENANALARYASICQQNGLVPIVEPEILPDGDHDLQRCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAXRRMWP | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 242
Sequence Mass (Da): 26495
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A0A1I8H6J0 | YSKPLHHIARPQASPAAVRLGRDFYARDCVELAKRLLGQRLVCEASDPSGCRSAGRIVEAEAYLGEADPAAHSYRGRTERNAAMFMQPGTCYVYSIYGQYCCINVSSNGDGCAVLIRALEPCEGESAMQSRRGKFSKTTNSSNDTVGAKLLKPHELCNGPSKLCQALAVDKLTHNKTDMCDPAARVYIESAPGPPANQIVTSRRIGIDGCGPAAAAMPLRFYWLGCSCVSRRDKAAEALTAPAEAATSKASTNANLPTSKQISQATSKAPPPTSKAPPPTSKAPPPTSKAPPPPTSKTSARPKAQIRNADSDSSPPKRKR... | Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
EC: 3.2.2.21
Catalytic Activity: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Sequence Leng... |
A0A1B6GSM0 | ADTLFLVDSWLTDMGSSTLAVLSLLALFLHQGEAIRCYVCSSQRDSSCKDPFNSKQHEHLLTHCSQETMRNIGDNIFPGVFSNFGYHTSQPEEFACVKAVTKNYDREEVVRSCSIPRADTFDVCSQLKARGDVTFCQTCNSDSCNGARGLAPLALLAAAPVLALLFNKY | 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... |
A0A7D5LEQ3 | MAKTKGPMSGFRDFLASELIPRQRMIETIKKVYESYGFLPLDTPAIERFETLTGKYGEEGEKLIYQFEDHGGRKVALRYDLTVPLARVVAQYKDDLVLPYKRYQVGNVWRGESPQTGRYREFLQFDADIVGAKSALSDSEIVMMMADAMQALGVGALISVNNRRILDALSEKLGLDSDASRKLFLIIDKTSKLGKDKVLEEIKIEFGDKVSELVLQFLSISGSSEEKIDKIREVLGSSVALLEGISNLGEVFSILKKSGYGENLVVFDPTIVRGLDYYTGIIYETYLLDLPEIGSVCSGGRFDKLISLLSDGKVDLPAVG... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 435
Sequence Mass (Da): 48310
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A0A401XNF5 | MYDLSEAETLIRYVLEDFAGVKRWQQWSDETVQLSQDQIFKLQEVLDRLCKGEPYQYILGKQLFAGQWFEVNGNVLIPRPETEELFQLVVEWCKKRSFAPDTIIDHCTGSGCLAVSLKKAFPNARVMGTDVSEKALDVAKKNAKALNAPVEFIQVDLLKPDVAQHLPESVDVIVSNPPYVLLSEAKAMHVNVLKYEPHIALFVPYEDPLIFYRRILEISVNTLNQKGLMAFEINPLYYSELKELFSKFFLVELLKDLSGKNRFLFATKQTK | 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... |
V6DIP7 | MEKEIKNQILWDNFAKRNLLSSEQIDQFKKYYNLLIEHNKLYNITAITDLESIINDHFEDSLALSKAVDLNNKVIVDVGSGGGFPGIPLKIRDNSLKVILIEVILKKVNFLETVIEELNLDNIETCNLDWRTFLRTPQEPLENKVDYFCARASLHTDELLRVFKPSSFYKNSSIVYWASKNWIPTKEEKELIYKTYSYQNDNKQRQLIFFKSKI | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 214
Sequence Mass (Da): 25146
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A0A3C0QSE8 | MELYEIICGAVVLLIAILVIILCLMQDNKSQDNMTSALGGGFNESFYGQNEGNTREAALAKLTKILGIVAFVLIICMNVVIPYIMTFFQSGS | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 92
Sequence Mass (Da): 10010
Location Topology: Multi-pass membrane protein
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A0A0L1J5P1 | MQQPLIFSESAPAYFSMTDNLTDWHTVMDWVPEYGELARHSDDIIVYGGEGSAWDSIMTNYRFNTLVARYQRPGYYNDPDFLISDHPGLSLDEKRSQFAVWASFSAPLFISAHIPDLSSEDLKYLTNQALIEVDQDPLAQQATLASRDSSLDILTRSLADGSRLATILNHGSDPVETDISLDILGLSTDCTYKSQDLWDGSTQNIKDAIHIKLNTHATAVYKIDIDQKCSAVTPTGIIFNTASGKCLTGTTSSVGFESCDGSKSQIWKVDASGLIRTLSDPSKCLTAEDKAISLKECKEDGAQKWSYATTGNLKNLDTGN... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
EC: 3.2.1.22
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and ... |
A0A0G1W5F5 | MEKIVSLCKRRGFVYPGSEIYGGLAGFWDYGPLGVELRHNIKQHFWDKFISEREEVYPLSTSIISNPRVLEASGHVSNFGNELLQTKIGTGEEAAVSQLRPETAQGMFVNFKNIVDSFHPTLPFGIAQIGKAFRNEISPRDFLFRQREFEQMEVEYFSKEENWEAAFELWRGLMNEYAREIGITAHEYEVPADDRAHYSKRTIDFQFDYPFGRGELWGLAYRTDFDLKNHNLDYFDEETQKRFVPHVVEPSLGVDRTVLAVLTEAYTEDELGGEPRTYLIPTVIEKSQFGERAYDIYSRLLKERIIFLGGSIDDAVASTV... | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A0A833QQK8 | MEGIREEEALGGLEAGSLPSKPSNSNSNSNGHIGIGNTSTDTSGPHHHHKPLSRHGRTAHSLSAASLRKKSDVTLLTKIPCLGLRNLLINLQEIFFNTKLFFLFPFVVVAFVFFFLNLNQGWIFAVSLVGLVPLAERLSFLTEQLALYTGPTIGGLLNATCGNATELIIALFALHKGQIEVVKWSLLGSVLSNLLLVLGTSLFAGGIKHLRRPQIFDKKQSDIGIGLLFVAGLCHLLILVYGYGYASTETDFFPSNQLEMSRVCSIFMLVVYGMHLFFQLKTHSQLFDLEEGDDGNDAVDEEEQPVLTWWSAFAWLVFMT... | Function: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
Subcellular Location: Membrane
Sequence Length: 482
Sequence Mass (Da): 52517
Location Topology: Multi-pass membrane protein
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A0A937NV04 | MRGNVISVGGLILSAVLLATAFPPVGEAQAAWLALVPLVLVVRTLSPGRAFYWGWGCGTLFWMISLSWLWRLGFTGCPIVVALLAWGGLSLTLGLFRGAFAATTAWAFSVLEAGPREEGHASFYRTLPLVVIVPVLWVGFEYLRGIVGTGFPWNGLGISQYRNLPVLQLAEWGGVSLVSAVVVAVNTGIALMLVRVGGVYMGGRRVRFQIELMVVLLLLASVWTSGVRRVRALRAMGGEETRPLRVVAIQPNIAQLKKWPEEFAQEIYAALEERMDLVVALQAQIDLVVWPETAVPGYLPHDGEVDTFVRQLARETATPL... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A518N0U8 | MKVRRFVAADMRGAMQLVREAHGPDAVILSNRRIDEGVEIVAASNYDEAFVQRAIEAQRMAVEPVPVKAALVPSPVSAPARPAHAPFEPVRPAFAGPVARDPAPAATPRDGTPAPAPVPGPVPAPPVPASDGELARMRDELAQMRQMIEREMARLTDERLRGSPVRAQAMHLMEDYGFDAGITRDVVLQIPPDTPEHRARGLMLGLISKRLPICPVDPLHEAGVIALVGPTGAGKTTTIAKLAALYASQHQARDVALVTTDTTRIGGREQLHGYGRQLGIAVHEADSEAGLFHLLQRLEDYRLVLIDTAGLSHRDHALAS... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 431
Sequence Mass (Da): 46828
Location Topology: Peripheral membrane protein
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A0A1E4LK03 | MMTLVIGASSSGKSALAEGIAMRQTGESLIYLATMRHGGTETEQRIARHRAMRHGRGFVTVERALDVGETPLPQRAVCLLECLSNLVANEMYDRTPPPDLAGKLVRDVLALRDSAAALVVVSNEVFSDGAQYDPFCTAYIETLGALNAMLAREADTVIESIAGLPFYLKGERL | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A2T3KMV7 | MDVQDKLNKIKDSFESLSFNKKALASAILMSGIAVSGLSIYKLNQPDYVSVISGLDRGSLQKIIPALETAKITFKISADDTTLFVDSDEADQASIVLAKNGLPGKPTSGYDHLRNTDSPYLTKSAEDQLSRQVLEENVASAIKKLTPIADVQVRLALSKNSQFLQDVDPASASIVLTVKQGQHLNKSQIQGIANLVANAVPNLSTDNVIILDQTGRVLSSSDDLVGAASSQLDHKLQIEKELTNKVTEVIAPIVGLDSVRVNVNATVDYNRTELTSETPADKTVILSQQKEISYDKSLTGGQGVPGSLSNEPPKHSKFDK... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 556
Sequence Mass (Da): 60655
Location Topology: Multi-pass membrane protein
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A0A1I8F2T6 | RPSVGLASGRGFESFLAWPRHAMLVSCACLCSSATALLWWVFADQKSQLDAKEAVNFPLLDLETQNEDAFLVLSIVSTVLLLVLLFCLCVVCSRARYVGPLFVQAATCLAMDRPSWVSWLWIYHVPVCLDWRVCSGLSAVCSVAVVSAGRLRLVLSDERHSAKWPVAGALADLVWRRLGTVAIGSLVIAVTRLPRWALSWFHKRLRNQKACGGSDACCVRCRRLNKSALAAAALTGEPFWSAAGAASDLLGNKHASLRLAALNSAGDFVLLTAKLALKWSDKSIRFFPLPIVLVATFAFLVAHCFLSVFEFVIDAIFICF... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 437
Sequence Mass (Da): 47755
Location Topology: Multi-pass membrane protein
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A0A1I8I538 | MDSKEPSTSAKSNATTASSLLPSHAELVRAYRMDELWISRIAEHLDRLALAVLGLERYTACRSGLSAFGQVASKALYYGASTAQCLQTLGEEYVNLVQCLFPDLLLWLLRRAEHRCRSDLTLSEPIQRRRLALLSRLSALATSAYELNSALFYINGSYYQLSKRVLGINYLRSRPGLGHVTETLYRLIGWLSLARLAGRAVNQMRSLASALAAAGAAAPTAEPSDNPTDSMSLQEKQTFEAEANNNNGRLNRICPLCCDRVLEASAIALCGHVFCWACIVRCLQLTGRCPLCRLECQPNRVVHLANYSDAPICVYEPKSL... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 576
Sequence Mass (Da): 63840
Location Topology: Multi-pass membrane protein
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A0A5P2BC39 | MRRPPPETADHRSHPLHLEGHTLATATHLHTLLTQPPCALGVFIPGGVHEPDIQRRQLDHLAQAGADLFEIGLPCANPVLDGRLIRSAYQRALAKGSVLDRTARAVAHAASLRPTVVMTYWDAVRRHGPERLARLMADAGAAGIMVVDLPREEALRWHRTAHHAGLSTPHLVPRTTADTDLRAAVEGASGWLYAPASGGVTGFQGPLDLAALEAFTERLRAASALPVVSGVGISSPDLAARVAPLVDAVVIGTPIVRALRPDPGPAAAVTAAFAQALKSRIGTAHGA | 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: 287
Sequence Mass (Da): 30161
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A0A8J3PGH7 | MTVVAVLLGGGLGATLRYLLGLALAPPTPPDFPWVTFAINVVGAFALGAVMTMLTLKRLRAPWAKPFLSTGLIGGFTTWSHFIVEADQLIGARQVGLAVTYLVVSIVVGVAAAAAGAALVERLTRLHSAGA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 13481
Location Topology: Multi-pass membrane protein
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A0A3R7T2D4 | MNVPQSSLDYSHFPVMLKEVIEICAPKNGGYFVDCTFGGGNYSKELLKFSNTKVVALDRDKNVIEKAQKIKSLYKDRFIFFNEKFSSLEKVLINSNNKPDTIIFDLGVSSLQLLDMSRGFSFKSKAKLDMSMGLSNLSAEEVINNYDEHDLKLIIKIFGDEKEASKIAKNIIKARKEKKISTVTELVKIIEKSKKKNYNKKINICTKTFQALRIFVNKETTELIEGIIQATKLIKAGGKIIIISFHSIEDKIVKFYFSNFSKDKSKSSRYFPENTDNEFIFFENYGNQFLKPSNEEIKINPPSRSAKLRFVTRNKQKFNY... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 339
Seque... |
A0A0A7LFZ0 | MAVIDIRIDLKKGVADPEGSNTKKTLESLGFKGVIDVKAVKVFEVTLDMPAEEAKKCGEEMCRRLLANPVIQSFSVTVR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A1I8HFS9 | MPTELLLVFKRTWFRFVNPASLNRFSAKCYILACACIWSFGVFLIGPINIQRQGWGWWATAFNAAFPTVCLAQMMLNWLLIRTQQRRFVGEPLQMQGDFVLNPNDPEKVHFRKTKDNQQASKKAGSSIVPELYNAYNASQPIPMPQNNPKFKRTIAEDHKYSYLSYKPCFSCRHWRPPRTHHCPLCDICVFKRDHHCFFSGTCIGEGNERFFLVFLFYAVLAATYASVHCILYMVTNFVPRLGLAATLLPVTIAQAFTGSASWQDCILVFTGYCLGFFEPLLLGFLMEHAELISRGGLLSLEVKEKLPIKSSLKPAEALC... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 377
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 43365
Location Topology: Multi-pass membrane protein
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A0A1I8JQY4 | LMRSAVRRLCSQAAAAAAASSSASTSATSAAEAQKFASLADSWWDRAGPLQALHSLNRLRVPLVRTAASFARGPAGLADAELVDLGCGGGLLAEPLARLGVRCSASTRSPTSSRRQQSAAAESGIADGRLTFRCQTVSELAADRPAEFDLAVASEVLEHVDNWPEFLRSAADLLRPGGCLVVTTINRTAASYWLGVVAAERLLRLVPPGTHDWRLFIPPDQLRRRLADCGLETRLTVGMRLNPLTGRWAWSRDLSLSYGLVAQKLPAAGTH | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) +... |
A0A059B243 | MKVVQWLLPVAVAWWLRQGGAPTVAGECATKCGDVDVPYPFGLELKCARSQEFFLNCTTEGNHTQLLLASGGNCPIRNISVEDATMVISVPEVYICYDPDGQVTEMSGTINLTRYPPYRFSDTRNKLTVLGCNTYALMSDPDGTFGTGCLSYCGYPIDFANETTCSGLGCCQTSIPKGLKMLDIFIEPLHDRIEPLYDRIEPLDEHACGLAFVVDDRSFNISNRKFPTLEEVGKSSDLVLDWMVEWDVTCGKASSNKSGYACGNNTDCNDFTNGPGYRCLCKPGYNGNPYNRSHGCQDINECKEPEVYPCHGKCRNKLGN... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 731
Sequence Mass (Da): 81082
Location Topology: Single-pass type I membrane protein
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A0A410Q2F7 | MNQITKDAAEVLSEVRRKSPLVHNITNYVTVNDCANALLAFGASPIMADDIGEAADIASISSALVLNIGTLNRRTVESMLAAGAKANELGIPVVLDPVGAGASALRNRAVRELLKRIRMTVLRGNLSELSFLAGIRSATKGVDASEADSGNDAVSVAVSVAEQYGCAAAVTGAVDVLSDGERTVKIRNGHPMLSSVTGTGCMTSALAGACAAVSHDPLAAAAAAVAAMGIAGELAYEAAGSAGTGGFHIAVIDALSRLDPALFEKRAKLDEA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-m... |
A0A8J6NFX9 | MKAEKRKIRISLPSKGFLGEKSKELLANVGFRVYSPNPRQYQASILRFPEMEVIFQRPGDIVHSVRDGSVDFGITGRDIYLERKDENGNILELHKRLGFSHCSLNVILPQSWGEVNSLADLSIMEASLKRPLKVASKFPNLTRKFFEQNSGVQFKVIQSEGALEIAPTVGYADLIVDIVSTGTTLRDNHLKILEGGELLQSQACLIANKVCLQKNPATRKIAIQLLEVIGAYLRGNEKLSIFANIRGESPQKIAEKIFEKKVIGGLQGPTISQVITREGRGWYAAHLVVTKSKLHQAVREIREVGGSGVVVSQVDYIFEE... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosyn... |
A0A059D294 | MFGSRKGGNALGRFKLKWQRESSLTTGLLGDVPPEIELSEYGRVPSPGSESPSALLNGESLNLEPITDLDLFFERLYSYYCEKGLWCIIIKWIVELLSLGFTICFSGFFLLYVDWNGLRNAKCGMDAVESGIKPCDLSKEALDEHPLTPLTVSKAVIVGYLGIFSIYWIFCFLRFFAQLKDILAIRHFYYDSLHVTDNELQTIPWATILEKVVQLQNSQQLCIVKYLSAHDIVMRLMRKENYLIGMLNKGVLAFPISIWVPGAGPVVKVGRGLIQHRLILTKTLEWTLNWCILQSMFDRNFCVKRDFVSTPKTLKRRLML... | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A9D9L842 | MRSPFIWIAKLPIMFYRKFISPLLPPSCKYYPSCSSYALDAYEKHGLIKGTVLTVWRLLRCNPWSLGGVDYVPERVTVDYFRIKKVRKK | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 89
Sequence Mass (Da): 10504
Location Topology: Peripheral membrane protein
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A0A955HLL1 | MSKKAGMLLVDKPSGISSHTVVNWARKAFGVKKIGHTGTLDPLASGLLVLLVSREYTKLQDTYLKQDKEYFVVAELGVVSDTFDRMGRVEQTATYDELALVTQSQIDSALHAFVGESLQTVPAFSAVKIAGEKLYDLARKGNIDTFDLPTRSITLTNIVLHSVMRDGQQKKVFVTFSVGCSSGTYVRSLVQDFGVTLGCGALVSELRRERIGTFCIQDEQTICPVVPKRFHITKKSL | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 237
Sequence Mass (Da): 26065
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A0A833VNS0 | MENKRFKAHMGTFTIIVRNRSVEQFSLIPYLTSLLSCMVSVMYALPIVHPNNILVLAMNGVGIIIEGTWITIYIFFLPTPPPCKILGTVAVELLLVGAFLAGVLRGAHTHDKRTKIASILNIVFNLVMYSSPLSIMTITGKIFKVDTIDGTVKEVLSRDSSMPLALSGHAIALQSKRSIAVATNQSVLLIESDNSWAQGVAIHKKMKMEEGKMVVAVAIRDGENVTVLVNSQKGYMIEEAVWGGSIKEYVYVLWCFILGSINFSCFTFPLVSVGTQ | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 276
Sequence Mass (Da): 30285
Location Topology: Multi-pass membrane protein
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A0A951Y0D3 | MRVALVQMNASVGALAANARGIVERAHGAAKGGADLIVFPEMALSGYPPEGLLRKPDFLSDCAKELRALAASLPPEPVVVLGTPIQEGKAVFNAVAVFQGGRLRGIHRKTCLSRSDVFDERDFFVAGSRASVVDIAGLRLGLLISDEVCCAHAPQNVFRGAGVAAVVTTAALAFRRGALAVRRKVLGTLARQMGVPVLSANLVGGQDESVFDGASLALDARGRLRARADQFVETILHVEVPLEGKRPPRISKGWKGATIRVPRLGSVQKSPRAEGYDGVATSAVPRNSIAPELSDLEQVYGALVLGLRDYVGKNGFGKVV... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
EC: 6.3.5.1
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) ... |
A0A1I3BIA6 | MNNTSYVRTPNEKEYNNMRAARLPGLIWIVIAYTISLILKIKTAPAIEQYVIFTILIILFTTIYWYSNLFLPGKFWLYFILQSFIVYISAFFTQDIPLIIITLYPLLVGQAIGTAGRKKNYLFLMILVLFTINTLVMVPGEILDTFLIITLPIMVVIVAYAVIFFNQVNARIRTQYMLEEIELAHQQVERLTLHNERQRMARDLHDTLAQGLAGLKMQLEATNVHLTKGNDKKAQEIVVQSMKRVSELLTDARLTIDNLRLHTKEEYDFQQSIIEEVQYFTDATGLECHFEFRVMQQLSSTISEHCVRVISECLSNIARH... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
U5D7W9 | MDASPPMAEPPTLSVEVCVQVTDAIAALADIPRDSEHWTQWIATWLAVAPKIPPSGTGYELALRLCDDAEIQYLNANYRDRDRPTDVLAFASLETDMPDPTALELPEASAEPLYLGDIIISVETARRQAAERHHALSLELVWLATHGLLHLLGWDHPSADALAAMLACQEIMLRNSNHWQKERALTLGHSELADYT | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 196
Sequence Mass (Da): 21668
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A0A3D2N464 | MNNKKMLAFLLSLTLCGTMMSGCGSTSADNNAADNSKAETTTTTSAPAESQAETAPSADTPAETEAVTTEEAETTEAPQADPANDTEEPTSADSRETVYQVALLQSLVQGYYDGIISVDELKEKGDTGLGTFDGVDGEMIVLDGEVYRADENGDITKADGDAMVPFSNVTFFDNDTTLELKDIEDFDALKAELDKITQQNKNMFYVVKVNGTFSHIQARSESKQTRPYKMLNEALAETQKEFEFDDMNGTLVALYCPDYMGGLNTTGWHFHFISEDRTKGGHVLQVSVKEATAEIDMTQGFKMHISDEENFQKMDLAKNV... | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 330
Sequence Mass (Da): 36097
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A0A3D2MCH1 | VLRGLHYQIQQPQGKLVRVVAGEVFDVAVDLRRSSPSFGRWVGTRLSAQNQRQLWIPEGFAHGFVVLSESAEFLYKTTDYYAPAHERSLLWNDPQIGIEWPFQELPQLSQKDAAGKILSEAELFA | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A7R9HY13 | MDLKGIRCNVVDWMELVRERDRGYSKSGSYFANFGYFRGTDKAKTTVILVLKDSICQKERNHFNLEVECLVLNGLKSKTISLEGFSQHELHPQVSDSAAVDWIFVVDTLNFSFWSPDDSSCKWEVSHNGRKYTGYFALCAAINRAIQEGVQITDPNYYCNVSVEQLTHILRSDTSTPAPMIKERVSNLHEVGKILVNKYKGSFVNCLEQADNSAQKLLELVITDFPCYRDEADYQGHKVAFYKRAQILIGDLWASFRGKGLGFFTDIDSITMFADYRIPQSLVHFGALKYSDELMAILKSGVELPSGSPEEVEIRACCIH... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-pho... |
A0A267DVR1 | MEQLMKILVIGDPTVGKTSFVHRYVNNMFQTDYKQTIGVDFALKVIRWSDTQTIKLQMWDIAGQERFTSMTRVYYRDAHAAVIVFDLTKRSTFDGALKWKRDLDSKCALPDGSPLPAILLANKCDLLSGERQLQLSEIETFCRENGFIGWTEVSAKEGVMIEEAMRFLIESVLAKTANSESAAQTVSLTDDPAIVRLGAVSGAKNKPRRGNADEDDEIGGGRCAC | Function: The small GTPases Rab are key regulators in vesicle trafficking.
Subcellular Location: Membrane
Sequence Length: 225
Sequence Mass (Da): 25020
Location Topology: Lipid-anchor
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A0A6V8PHC7 | MAIGYYPINLNITHKSCLVIGGGKVAQRKVEGLVESQASVTVISPSTTRVLDALAVQGLIRIIRREYRQGDLEGTFLVISATDDEEINQAVFAEASEKGILVNVVDQPELCNFIVPSVVRRGDLVISISTSGKCPALAKRVRKQIEKQYGPEYQEYLLLLSQAREKIKASYKTEQERGKALERVMDSGILELIRVGKKDLAEETIERCI | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 209
Sequence Mass (Da): 23177
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A0A0S9M413 | MVLVMPGVQAAGIDPVYFGVMFIINNSIGLVTPPVGTVLNVMAGVARMRMDDVTRGVLPFMAAEFAIMFVMVLFPALVTVPARWLAG | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 87
Sequence Mass (Da): 9283
Location Topology: Multi-pass membrane protein
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A0A8T0SEP2 | MLTKFETKSNRVKGLAFHPRRPWILASLHSGVIQMWDYRMGTLLDRFDEHDGPVRGVHFHATQPLFVSGGDDYKIKVWNYKTHRCLFTLHGHLDYIRTVQFHAEYPWIVSASDDQTIRIWNWQSRTCVAVLTGHNHYVMCASFHPEEDLVVSASLDQTVRVWDIGALRKKRFNLALESGNIQIAVASAKELDDKDHWYRLGIEALRQGNVGIVEYAYQRTKNFDRLAFLYLITGYLDKVGFMCKIAGQNNNFMGQFHNALYLGDVRKRVEILENTGQLALAYVTAATHGLTEIADRLAAELGENIPSLPDGKASSLLIPP... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
A0A923PPW0 | MRHLFLPLLLLFAQGCQPEPVESTASYTFVAPPHFPPPTYDFARNPITEEGFRLGKRLFEDLRLSRDGSVSCASCHQQAVAFADPQHRLSVGVEERVGLRNAPGLFNLAFTTEFMWDGGIAHLDFVTINAITAPFEMDESLENVVHKLRADASYRTAFARAFGEDTITSGLMLQALSQYQALLVSDRSKYDDVVLGRNGAAFTAEELRGEAIFKLRCASCHAGPLFTDGTYRNNGLDGAGEQDLGRSLITETEEDRGKFRVPTLRNVGRTAPYMHDGRFSTLVEVLEHYRTGVITSPTLDPALENGITLSAQEVADVLAF... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 335
Sequence Mass (Da): 37154
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A0A1B6GWY7 | TLKCVGLLYLQFSGNMFANYLWFMAVCGLVLLFTAPHIRAELELRPGTVHVLTKENFTEFINSRYVMVDFYAPWCGHCKSLEKPYASAAATLHLKNISEPAYFTKVDVTAETEIGTEYEIKGFPTLKWYDYGTNEWSDYTGDRTEEALVEFVLQMINSKAVLISSSTEWAQAYDKDKTNVIAYFKDPNDTEEFKIYSKMAKNFHKFKFFVINSEDVRKELGITTDVYLAVQKNGETVVFDEPWSQKAVKQFVAIHIMDKVTDFDHDTAPMIFGNAIENHVLIFLSKSADQYKEIEKLTATVDKYRGKFMFVTVDVDVENH... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 521
Sequence Mass (Da): 59624
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A0A0G1CNZ3 | MKILENVPLSGYTTLGVGGPARWLVEVENRNEILEIRDWVEEKGVEWMVIAGGSNLLVSDEGYGGLVIVNKLPGSGMMLNDLVDQMNDLGLAGMECLAGIPGTVGGAVYGNAGAYGQTISDHLVGVTTLSGYWPKEKCEFSYRESVFKKNKEIILEVKFELPRGDKDVLIAKSNEIRELRKKKYPPEMKCPGSFFMNLWFDQLPEEVQKQIPKEKVKGGKVAAGYLLEQIGAKGRKLGGAAVAEYHGNLIYNAGGAKAGEVWELAKQLQREVKEKFGVSLVPEVQLVGYGKINTCLPSFH | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32879
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A0A0R1LVW4 | MYQINAIDDFDVTEFTDTFQLKETTAPDAVLVRSSVVPDSLITNHLLLVARSGIGTNTINIDACTKNGTAVFNTPGANANAVKELVLQSLFASVRPLQAAIDATAELSGDQLQAKAEATRHQFVGGELYGKTVGIIGLGAIGQRLANSCYHLGMQVIGYNRSPKNLQHVQQLETIEEVLQLADFVVLLLPLSDGTRHIMAAKQFREMRENATLLNFGRGELVDQDALLTALKQGQFHHYVTDFPHRDLQHNSAVTILPHLGGNTIEALSNSANITLQNTRDFLEAGTIRSSVNFPTADLPFTSPQRLTFFYEDRPTFWAD... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydrox... |
U5DMF7 | MRQGLSAIALRLQQFTRSRPERVTTTGAEDTPDEQFLCALRCLPVGSRAATDLHVPLAPRDGAAMFIVPNVRLKSARSRLLLSLAGGILMGLTVAPVSAWWLAWIALVPLWLAATGSNSVRAAFLCGGAWGFGFYATMLSWLLGMHPMTWLGVSWQTSLAIALACWPAAALCLAVLPAVWAGGLCWVARSMTGSATVVVGAALWCALETLWSWGPVYAGPLAFTQSPHNAIGLHAMQLSGPVTVSAAIVAVNGLLAIAIGKRSRGAMAASLAVLVGVHALGGVLYARSPADDPAAALNVGIVQGNIPNEIKLTSVGLRKA... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A6M6E1R9 | MTSKEKKKQIRKQRKKRFLTDVRDIFIFMGILFLLKVFVLDFGFVYGHSMEPNMKDGQLIVIKKWNVFLDEPNKGLSFYDKVALENVRIEGQAHPLSLAKRVIGLPGDKIEIIDGYIHRNGKKVNEPLIKERANQPDQTFQLEDNEIFVMGDNRNHSTDSRHFGPIPIEDVSGKIITNVNAQWLSSLFQKIRVSLHLEENMRI | 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: 203
Sequence Mass (Da): 23590
Location Topology: Single-pass type II membrane protein
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A0A3C1H2T5 | MVLAVDIGNTNIVVSSFEDDRIIFMERMSTERLSTDLEYIVLIRTVLELNGMDFRDFDGCIISSVVPPVTQTVRSSILRTTGKEPLILGAGVKTGLKIHVDNPAALGSDRVADAAAASYYYPCPVITVDMGTATTISVVDADKTFIGGLIIPGVRVSLDSLTGRAAQLPEISLEPPKKLIAANTVDCLKSGIIYSTACAIDGVTARIEEELGQPCTVVATGGNAPRIIPFCRRKIIHDEHLLLQGLMLIYQRNTAENSKKASGSEA | 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... |
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