ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A545TYN8 | MISLTVIVVVAVIFRKFDASLSWYDEVASINLAWITYYGAALAALRRQHIGFDSVILAVPPAFRVAAVLIAEVLVIGFFIVMAWAGLEVLDVLEGETLVSLTWVPIQVTQSVIPIGAILFIVAELLSAPAYFKAVMSGHSTEHPDIDFDSSEGDARS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 157
Sequence Mass (Da): 17008
Location Topology: Multi-pass membrane protein
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A0A5C2SB50 | MRSIGSPLTGYVCRSCAANFRNARKPAHIRLASNLVDRKPTNFSSFFFDNHRWAASPRNVSISSRTTSQPVRGHSAGAAYSPSAEPSAASFRQAEVLTPRRLAKIYWQLSKSNLTVLIALTAMSGVAMSPLPTSVPVLLSTALGTALCSASANAFNQIQEVPYDAQMARTRNRPLVRRAISPLHATGFAVTTGIAGPALLWTMVNPTTAILGAANIVLYAGAYTYLKRKSILNTWVGSVVGGIPPLMGWTACGGSLLPSQSFELVLPPFLSTLSALPADALAAAENPLAPLALFLLLYSWQFPHFNGLSHLVRESYAQAG... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
EC: 2.5.1.-
Subcellular Location: Membrane
Sequence Length: 440
Sequence Mass (Da): 47693
Location Topology: Multi-pass membrane protein
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A0A1B8C180 | MPTWRDTSTTATLKGQPQRRHPDIEMNGPMFGGFGGQQMNGGDADAMAAVKNVGPTPYMILERVRPDMEMRNMQMIMESCPAKTVLSGTMGFALGGAFGLFMASMSYDTPLTPEGRAMGNLPLKEQLRKGFKDMGQRSLSSAKNFGKVGAIFAGTECCIEGYRAKNVLSNGIIAGCITGGVLAAPAGPQAAALGCGGFALFSAAIDSYMRQPKED | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane ... |
D4G4W3 | MWEQLYDPFGNEYVSALVALTPILFFLLALTVLKMKGILAAFLTLAVSFFVSVLAFHMPVEKAISSVLLGIGSGLWPIGYIVLMAVWLYKIAVKTGKFTIIRSSIAGISPDQRLQLLLIGFCFNAFLEGAAGFGVPIGGAARRTWF | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 15906
Location Topology: Multi-pass membrane protein
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A0A0G0QPF6 | MEGKGFAEDDEANPPSFYSWTKYWADSILKNFPVLILRLRMPIDTESNPRNLINKLVKYTTVWNPENSVTVIPDLLETVKKLTDKKKIGIYHVANPGTISPSAIVELYQKIVDSSHKFEKISVEDLYTRGLAKAVRSNCVLNTNKLESEGIHLKPINEKIIEVMEEYKRHLEQNTL | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 176
Sequence Mass (Da): 20201
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Q08056 | MKVKKEHASVAFDDQCSILEKEAVNVSLENLKTYPFVKEGLANGTLKLIGAHYDFVSGEFLTWKK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 65
Sequence Mass (Da): 7317
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A0A520ZIK4 | AKAAVVSSAMTGLISGSSIANVVTTGTFTIPLMKKVGFSSEKAGAVEVASSVNGQIMPPVMGAAAFLMVEYVGIPYFDVVKHAFLPAGISYIALVYIVHLEALKAGMEGLPRSYTPKPIVQRLIGIAFTVALICALSYAVYYGMGWIRPAFPETAGYIIFAFLTAVYVGLLYVASKEPPLKLEDPDAPVTHLPLPGPTVRSGLHFILPVVVLVWALMVDRLSPGLSAFWAASYMIFILLTQRPLMAIFRGESRLVADIVAGFVDLIDGLVTGARNMIGIGIATATAGIIVGAVSQTGVGSALADVVEVLSGGNIMAILLL... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 338
Sequence Mass (Da): 35346
Location Topology: Multi-pass membrane protein
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A0A558DTT4 | MLSYRHAFHAGNFADVLKHLVLAKTIEYMTQKPTPILYIDTHAGTGRYPLNNAMSLKTGEYALGAGAIKADLLDPAFSPYGEVLNRHLAKGIYPGSPQIAADLLSPLDQIRLFELHSTDFPLLEKWASADRRIKAVQSDGHQALRSLLPAVKGRALVLMDPSFEVKQEYQQVISSLEEGYKRMPNATYLLWYPVVQRAQIDKMIQQIQRRPFRDVWQFELCLSPDTADRGMTGSGILAINPPWTLPKELEALLPRLQQRLSPKGGHYRITNLIPE | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 275
Sequence Mass (Da): 30999
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A0A2N6CVH8 | MRRTRFHFSTLKSLLSSWLCVLLIASAPPAVQAGEQLALPDIGNPSGNVLTPADEQRLGRAFMRSIRNTMPVIQDPLLSAYIQSLGEQLASANEDAIGRFEFFLINSAQVNAFAGPGGHIGVYSGLITTTESESELASVIAHEIAHVSQKHLVRTYDAVSSMSLPAAAVAIAAVVIGAATNNPDIGVAAATGVQAGMMQREINFTRSHEEEADSIGIRTLAAAGFDPTAMPVFFSRMGKASRLYDNGTLPEFLRTHPVTSNRIADAYGRADAFPYKQRRDSLVYHLARERLRVMAFNEPSEGIEFYSKALDDGRYRNEEA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
EC: 3.4.-.-
Subcellular Location: Periplasm
Sequence Leng... |
A0A973E074 | MRRGNIPEFSCEIPRPTGELIWLNIADGAHARAVLDLAARLIQARPDSSALITMPQGDAIKISPEACTNPDIHLQPVPSEHPEHIAAFLDHWAPDLLIWVWGGLRPNLILDAQKRGMPMMLVDAGKDGFDSRRDRWLSEVPRQVVAAFDSVLARSQAAHARLAQLGRPLKSIELTAPLLPTGQALPVNDTELDELFELIHGRPVWLSVNLDRSELRAVLNAHRQA | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A5A4DPC6 | LSSNLAHSGASVDYAIFSLHLAGISSLLGAVNFISTLGNLRVLGMLLDRMPLFPWSVMITAVLLLLSLPVLAGAITMLLTDRNLNTSFYDPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A023UGS9 | HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLGFIFLFTVGGLTGVVLSNSSIDLMLHDTYYVVAHFHYVLSMGAVFAIMAGLIHWFPLFTGVSMNPKLLKMQFLTMFVGVNLTFFPQHFLGLSGMPRRYSDYPNFYLTWNIVSSVGSLISTISILFFIFILWDSFTSIKKSIYSMNLPSSIEWLQ | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A164BAI9 | MTIETTTDPRFSGLPGRPGKIIAVHLSYPSRAAQRGRTPEAPSYFFKASSSVAASGSTVARPAGTELLAFEGEIALVIGSTARHVSLTGAWEHVGWVTAGNDLGLYDLRASDKGSNVRSKSRDGFTPLGPRLLDARLLDPTGLRVRTWVNGVLTQDDTTGALLFPLTQIVADLSQHFTLEPGDVILTGTPAGSSVLQPGDVVEVEVDAPEAGLTTGRLVTSVATDDGPGFDATLGALPAVDDTQRTEAWGNDSPRTETQRTVGAAASPTAGGGATTPPTETDESGSRSTLDADLRAALHRLPVAALSQQLRKRGLDDVTI... | 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:... |
A0A6L8C547 | MSNPTLFNTESRNDDLGQLPKQPKESKFKSLPARVLTALVLAGVALGSYLGGFLTFSLFCLVLFSFLLFELCGLQTPAFSRSRKIVYVVFGCVVITSTMLFALVTAFAIIVDEFYSTLLLYDFALIFLYIIGSGILLRYKIHMVACATGIFLAVLGHLMTYLEESQLFLLIVLLIIGTDAGGYFVGKLIGGPKLFPSISPNKTWSGTIGGWVMAIIILSGFNYFWRDELPTIYLILYALAISVFSQLGDLSISSLKRKAGVKDSSNLLPGHGGFLDRFDGFVGAGVLIFFLTIMNFQPNFG | 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: 301
Sequence Mass (... |
A0A3P9KAQ1 | MHVQTVKGFLISSRKNAAMPTVKSKKKKVKKEISEGEEQREVALEVEVENITNRSNSDNRDPLTPDLQEPAPQKKKKRKKTSTIGQEAERPELPNGNTSDAVMEGEETSVAVTRRTKRKRKAKATEHHSHDLEAEEDDIITESHSPISPNSLFSAPHGHSQPFGKVFVERNREWIFCIKNTQLVVHGNSAALCAGRFHADRVEQLRHSELVDDYMDPRHIWTTRDVALKVHSSFRVIGLFCHGFLAGYAVWNIIVVYVLAGEQMTTLANLLQQYHLLAYPAQSLLYLLLAISTVSAFDRVNLAKTSMALRGFLTLDPVAL... | Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Location: Cell projection
Sequence Length: 397
Sequence Mass (Da): 44429
Location Topology: Multi-pass membrane protein
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A0A7S1VDW1 | SKSAARPPQATNFCRITSEAPCSTFNVCQATRTFSSKVDEGGSPGKKSSATSVGGGSGRSGGRMATTAVGGVAALVCAYVGYELFLVDNQGEPQDDERQVTPGPPQADVTDTVYFDVSIANEPAGRIVLGLHGREVPRTVENFKALCTGDRVHAADTKRPMSYEGVPFHRIIPQFMIQGGDFETHNGFGGRSIYGKTFDD | 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: 200
Sequence Mass (Da): 21198
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A0A7I4YZ82 | MPFRKSFVSQSCSRKRTLFGILLFIAALFTVFGFIADFPTWQTDGFFVFHVITRNFNQTADSGTIRPSTIPYQSSFQPVPRNSSQTASSSGTNLSLSFSTASYQPSLQPVLQNNSQTTHPVTSRSAAISIAPNQTSVQPLNGPSNQTALSSTKPPSTASNHLSSTPAPQNRSQTALPGTNISSTVPLQTSLQLLTGPSNQTAPSNINPPPTTSYHPTLRSLPQHSSQAAPQSRSQTAPPASAPQNSTQPTPLPANISSTNSYQSSFQPLPQNSSHTTRPDLNSSSTASYPSNSSSMPYSNKTDNYPSCSQRLKFVGRFNV... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 587
Sequence Mass (Da): 65652
Location Topology: Single-pass type II membrane protein
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A0A804N0D2 | MEAVARSGDYLWRFVAETEWYNEVVLSAVAPGDWWRGLPHPVQSWMRNCVGGYLLYFISGFLWCFVIYYWKRHAYIPKDAIPTNEAMKKQIVVASKAMPFYCALPTLSEYMIESGWTRSYFDISEIGFSMYLCYMAMYLIFVEFGIYWMHRELHDIKPLYKYLHATHHIYNKENTLSPFAGKTCISSTGWCSASNTTCVRALPLSNALQDTYCTLVPRGCVDNKHPRLHSWQDMASHGCWISHHSPYDIPPQLWPLHHLDGLDVWYAQ | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
EC: 4.1.99.5
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 268
Sequence Mass (Da): 31280
Location Topology: Multi-pass membrane protein
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A0A7S1UXD4 | MTDAPVGFLQNFMAFWNSLGLVFQIVLCVMVFFIFAGFTGGSSPKSSPLKEVKFKDVEGDESNPKVYFDITIGGKPEGRIVMELFSKFVPKTAENFKCLCTGEKGIGKKSGKKLHYKGCAFHRIISNFMCQGGDITRGNGTGGESIFEGGGDFADEFRETLTYLAHSKPGLLSMANAGPNSNSSQFFITTAKTAWLDRKHVVFGQVVEGFDDVVMKKMNNEPSGPTAKKVVIADCGLLAPEKTKKEE | 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: 247
Sequence Mass (Da): 26914
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A0A1D6Q4X5 | MIYAISGEVPDEPVVSKKSGLLFERRLIERYIEDHGKCPITKEELTMDDIVPVKTNKAESATAALNCSGVVLGSLPIRLGIEEALEEAQCAQALDARQAWQSFCK | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
A0A804RPZ1 | MATTAFLSPPKLSLPGRRFASARTAGRVRVPPARAQEQQQQVVVVVEEEEAEVASVPPPPQSAEEQAQARKGDAAAAGGEQEHEPRACQLVFNDFQDLVDHYEGAELSEYTLRLIGSDLEHYIRKLLYDRVIKYNMRSRVLIFSMGKPRIKFNSSQVPDATK | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
A0A0D2BS02 | MTLAEEFRSRNFSIYGQWLGVLCIILGFALGIANIFHFNALIAFSIILLASSFILIFIEIPLLLRICPTSAKFDTFIRRFTTNYMRAAIYGVMSIAQWLSLIVDASSLIAAAVVLALAGLCYALAGLKQQEFVGSKTLGGQGVAQMIV | Function: Golgi membrane protein involved in vesicular trafficking.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 148
Sequence Mass (Da): 16130
Location Topology: Multi-pass membrane protein
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A0A3R9QVK7 | MPIYMRIAAELGLDVEADREATILMDRLMTGKEDKTDELEYLLKNERVIILGNGPSLPKNLEDLHGVVIAADAAASVYKRVVRKEPDIIVTDLDGPPDILEMGSLKVVHAHGDNMDRLRKFVPLMKELVGTTQVEPVGKVHNFGGFTDGDRAVFISMMAGAKSVVLIGMDFDSVTEYDILAGKDLIKKRKKLEIAKWLIEIAGKMGCPLEEVSKWR | Function: Catalyzes the transfer of diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP).
EC: 2.7.6.3
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Length: 216... |
A0A6P6GDD6 | MVSGISQGEMVTVLSIDGGGIRGIIPGTLLAFLESKLQELDGADARIADYFDIIAGTSTGGIVTTILTAPNKDNRPLFWLGGC | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 83
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 8611
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A0A7I4Z3P7 | MGYQPPPSFLSCDRLTVKHILLCSQSLIFLIAFSSLYWQIPGLYGENGLIPVAPKLDFDGPIWECSFPILLSIYRYLNLVPSRALQLLCLIGIVLSFITACKRQSRSPIIYLILTLLYLNAQKVGGIFLWYQWDTLLIETGFHMTFLAALPDSALDSIGIFLVNWLMCRLMFASGVVKLQSNCPAWWSLTAVVIHYESQCVPTPFAWYFHNMPVWFKRLSTSLTFYIEIYQPLAFLLPISCLKKFVFLQQALLMVLIILSGNYNFFNILIIVICIPMLERGRHVEWFSSRTDMFLSLIIGIVLTAHYMYWFDVKLDIFGL... | Function: Involved in the maturation of specific proteins in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 638
Sequence Mass (Da): 74038
Location Topology: Multi-pass membrane protein
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A0A1X7P6N7 | MNPRTASIDGKTNHAARRIAAALSLFAIMAGAAPAAADNYVVIPSPVISGNTPPYGPGFDTGVVVRPQDGCRTVVNCAPGNYQNRPAHRRYYDNYFDVPTPRYSGQRRVGGNPAIGGSSRLGEASSHSEWCSTRYRSYRASDNTFQPFDGPRQPCVSPF | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 159
Sequence Mass (Da): 17153
Location Topology: Single-pass membrane protein
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A0A522BGS6 | MTPDPPAASGYVPVVRPRIGATPERPEPRLLDALRAVSMTDVSDVVGRLYTMDPGIRPLFAPITRTVGVCRTVKAFPGDNLAVHGGLGRVGPNDVLVVDWLGYQDGCGSGARALEAPIARGLAGVVVDGGWRDVAELQARGFPVFGRRETAYSPPKREPGELDVPVCCGGVVVEPGDVVVADEGGVAVVPRRHLIDVVAALATRATAEQAVLSGVQQQHSTAFDARLGLRD | 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:... |
A0A2E8Q6X3 | FGILLWVSDKRKQQKRELSDWTMRHALILGCWQMLALIPGTSRSGITITGARFLNYDRASAIKISMLMSIPTIIAAAALEFYSIGIANISINWAELIVAIVVSALAAFGALSLMMRLLKTVNFTPYVLYRMLLGSFLIIWALV | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 143
Sequence Mass (Da): 15923
Location Topology: Multi-pass membrane protein
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A0A0G0T9R0 | MADKITSVIAKEDNGNIQITFAIPSDVIKSAEDETIKEFAKDTEIAGFRKGMAPLDKVKDKIPQSTLIEHSLSHVLPKALAEAVTENKLQIAIYPKFELISAKEGEAWQIRGTTCELPKFELGDYKKAVTGELAAASIIVPGKDSADKSASGQISRDKKEQIAIKAILENTKIEIPQILIEEEADSRLSNLLGRLEKLGLALENYLASMGKKAEDLRADYAKQAKEAIALDLILTKIAESEGLKIDQKEVDAALNMSQVDIKEKDQNPSETDNRKRLMESILRRRAALDFLINLS | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 295
Sequence Mass (Da): 32528
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A0A804N3S7 | MVRVLGGDARFLAALPHHIYPVRHLQHRPAAPATPRAVRSVRRAAVQAAAPGTAAPGSLPQLLHGRGLHLSARRWPSVRLLSCGRQGLVLCILISCMHACASILSLAKKESMPLMTYDAYIYQILRTRMGLPLPSVRETIAQLVVYSLVEDYLSYWMHRLLHTQWCYEKIHRVHHEFTAPTGFAMSYSHWAENVVLSIPALAGPVLVPCHVTTQWLWFSIRLIEGINTHSGPCRLIPFYGGAAYHDYHHYAGGRSQSNFAPLFTYCDYLYRTDKGYRYHKLKQEKLKSLAENSADKGGNYSFDEGKKNRYFCA | Catalytic Activity: a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+)
EC: 4.1.99.5
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 313
Sequence Mass (Da): 35389
Location Topology: Multi-pass membrane protein
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A0A142BA70 | MRIILPLPPTVNHVWKHRVIRKGRKHIPSVYMTDEGKNYRTLVKAACMEQGIHNRKLTGKLRVSVRLHFPTNRRSDIDNRMKALLDSLTHAGVWLDDSQIDQLAIVRGDKIPPDGVAMVEIQTLSQEVNS | Function: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Co... |
A0A0P7WQJ9 | MDGILDRGRDVAQQGLVLARDWILDPANWSQLALLVGAFLLALILTRKLNPLITKALTPPQDSQTILAKARRFLLMFLPLLLPLLAFGLTAAGEGATRAMFGSGELIAFGKRIFLFLAVRAFVRDMLADPLLTFLGRVVLLPVAAIYALGLLEPVMAWLETTMIPLGNLSFSLLAALRFLVVATVMFWLGRWSNDQSTAMIEKQPMRPATRQLAAKAAEITIFGLAFLLAMNIAGVPLTSLAVLTGALGVGIGFGLQKIASNFVSGVILLLEGQATVGDYVELDGGEAGTIVRMTARAAILETFDGRWIVVPNEDFIVTR... | 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... |
A0A963XF20 | MAEPILMTCYRAATEIARPFLRPWLGWRARHGKENAERLAERFGRASAARPAGRVIWCHAASVGESLSVLPLIDALTDRDFTVVLTTGTVT | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A172QUC2 | MTEPEQHHRSMRMPKPKNNAGRDLKAAVGVGVGLGLLVLLGIVLSPWGWYILVAGFMAAATWEVGSRLKESGYHLPMPIMIIGGQAIIWLSWPFGTMGILASFVATVLVLMYFRIFYNGAEKEARNYLRDTSVGIFVLTWIPLFGSFAAMLSLMENNSVPGTFFILTFMLCVVASDIGGYIAGVFFGSHPMAPLVSPKKSWEGFAGSILLGAITGALCVHFLLHHHWWLGVVLGCALVVCATLGDLVESQFKRDLGIKDMSNLLPGHGGLMDRLDGMLPAAMVTWLILSVVSSSYPA | 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: 297
Sequence Mass (... |
A0A804NSK3 | MKGVEYEYVEEDLRSKSAQLLAYNPVQKKVPVLVYKGRPVAESQVILEFIEDAWSHRGDPILPRDPYQRAMARFWASSVLCMYVLHAIAVMSCMQLSPSIWRWFTTEGEEHLCLPCSAEHHMTVSNIGDNQSTLSEKGYDAARAPALAPLEELPVCLEVTHLDSSPLSSLLHETP | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 175
Sequence Mass (Da): 19699
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F7V195 | MRSVADITVKGAALAAAAAGDFSDLPIHNPAIECASREDIRAIQLAKLIDQVAWTYERVDWYRARMNEQGVTPADIRTLDDVRKLPFTDKSVLRDTFPYGLFAVPLDEVVELHASSGTTGKPIVVGYNRSDMDMWADCIMRLVQMAGVVPGDRAQMAFGYGMFTGGFGLHYGLQKLGCMMIPAGSGNTERHIQMIEDYGTTVLVATPSYALHVCEVGEQMGFDWAASTLRVGLFGGEPCPPGLKAEIEQRMHIVCTDNYGLTEVMGPGVSGECLASRDMQHIAEDHFLWEVVDPETGEAVGEGEEGELVLTPLGKQAIPV... | Pathway: Aromatic compound metabolism; phenylacetate degradation.
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
EC: 6.2.1.30
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Length: 457
Sequence Mass (Da): 50237
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A0A7W0MR58 | FGDARPVWLEIGFGGGEHLTALAAAHPEVGLIGAEPFVNGVAKALARIEAAALRNVRLHAGDARDLIDLLPEAALTRVYLLYPDPWPKTRHRERRFMNPENLAALARVTTPGAELRLATDIADYVRHAVRAAEAAPGFALQGGPEDWATAWPEWRTTRYEAKALCAGRAPRYLIFRRR | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 178
S... |
A0A2D9FXW6 | MSLTYTSYLKIDELTDLQQFKSDPPEHDEMLFIIIHQTYELWFKQILHEFGKLRHDLEKGETWGSIKTMRRILTILKTMVSQIDILETMTPLEFNSFRKFLGQSSGFQSLQFREMEIVCGLRFPLMKEAHKDQPKHIEVLEERMAEATLWESFCAYMRSRGYDLHPQRENEKGLIHEPNDADQEILVEAMKNDPEAAMVAELFVDYDEGLQEWRYRHVKMVERTIGTKKGTGGSDGAKYLHKTLNHPIFPDLWAIRSKF | Cofactor: Binds 1 heme group per subunit.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-... |
A0A3L6ESD0 | MFSDLTEYCILFVYSAKLVDQALASGKIYDGDGFNYIKESFENGTLHLIRLLSDGGVHSRLDQLQLLLKGVSERGAKKFVCTSLPMGVTFLDGSNVGFVETLENDLLELRGKGIDAQIASGGGRMYVTMDRYEVLGEAPYKFKSALEAVKTLRAQPKANDQYLPPFVIVDDIGKAVGPVLDGDAVVTINFWADRMVMLAKALTVCRF | 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: 207
Sequence Mass (Da): 22730
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A0A804QHW8 | LVPRQPQSVKPPRRHRCPPRSRRSQSSSDPRPPARSGIQASRLPDAAIQASRLDGRSRRNRWHVKTSFTSVEDAVSSCVEAVTVHVTQKYFVGEASGQEGYTSASFHPDGLILGTGTTDAVVKIWDVKAQSNVAKFEGHVGPVTAMSFSENGYFLATAAHDGVKLWDLRKLRNFRTFSSYDLDTPTNTGTLYTSRLFYTWCNYQWTLSERTLAKGRMEESRGILREMFQCKEVTELINSVGDKIQAESLVDLLSSACDQGRIDEIDLCLEIGHQPTKALGSVAQIIFVSLDRDEASFRDHFQGMPWLAVPFDAAGLLRQK... | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
A0A1D6Q601 | MLGVGFSCVTNRVGYQTDHPCTINRHPKARIKGKLSNPKPDSLLTHVKSASKQQLHTTTHDCASSAITLLMHISTQFYLWKFFMYQMTTEFLNKAARTKNYSGAELEGVVKSAVSFALNRQITMDDLTKPLDEESIKVTMDDFVNALHEITPAFGASTDDLERCRLRGIVDCGKAHKHIYQRAMLLVEQVKVSKGSPLVTCLLEGPAGSGKTAMAASVGIDSDFAYVKIISAETMIGFSESSKCAQICKVFEDAYKSQFSMIILDDIERLLEYVAIGPRFSNLISQTLLVLLKRVPPKGKNLLVVGTTSEVGFLESVGMC... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
A0A804PR54 | LAVATCYSNFIAYIFAPGVLVTPLGALSIIVSSVLAHFVLKERLEKLGVLGCVSCINLATQPGFLAYVVTALLLVGALVLFFEPRYAIGVSIKLTLDGVNQAAYPYTWLFLNCLWGFSNKLPEQGNCQPRINSSAERTCTQARDHVMPPQAFLRALTRADNSSKSGIFG | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 18286
Location Topology: Multi-pass membrane protein
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I1NV86 | MMNSSEPVKLIGAFGSPFVHRVEVALRLKGVPYELILEDMGNKSELLLAHNPVHKMVPVLLHGDRSAICESLVIVEYVDEAFDGPPLLPADPLRRAMARFWAHFLDENCLKPLRPALFGKARSRRNPWRRHGRAXRWRRRSSGASGSSEAAPSASPTSPAVACWLTGSACSKRSPEXASXATATASTLLCAGGRRITSLMNPXWSACRIEIGSSPTSPGSSRSAFRWPSPRCQSSYXXXTN | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 26302
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A0A961QVE7 | MLLGLLGIAAALTLMFLGLPVGYALAVVGLLGFAAVVGLQPALAVFGQVTFDTVSNGALVVLPLFLLMGNLVGASGMAADLSRSAPWRCRAPTEPPRPPAGPVQRNGLGPARRAICRTVSSSSRDRECAMSWRPLIAGHCPDLPGRCQRAFPANPITADHGKRDGEAGKMRLRVLRRFGCAGAVGSADRSPAGGQG | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 196
Sequence Mass (Da): 20236
Location Topology: Multi-pass membrane protein
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A0A2E6N1X6 | MSEKEPNNLLAPLSTDVQTHQLPKLSILRGKASFEKLFKAPNTFHIGSILFRFCLSHFAKSNSTSEKRLQIAFIAPKHLGNAVTRNKTKRLLRESFRTSNRELHHFLRKNSINLHLALIASYPNPDFELVKYQMHKGLNNLIEILAHDIDTFKCLEE | 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... |
A0A3M8G699 | MNKPLAKLSEVAQKSSRTIIGLMSGTSLDGLDIALCECDSELVKVKQFKTVDYDSRLRSRIAAIQSKSRVDLQEVTALNTELAHLYAEWVLEALNEWGVKREEVDLIGSHGQTIYHHPAEHQTSTLQIVDGDHIAHKTGIITISDFRQKHTAAGGQGAPLVALMDERLFRHQAKHRMLLNIGGIANFTWLPSKESGEEMLTSDTGPGNTLINEVMKKYFNQPFDKGGKTAASGEVHSELLKYLLLEPYFRKAFPKTTGQEDFNLDIVEQLMQSYDIELSPEDLVATLTGLTIKSILRAFDAIAEEKVFELYVSGGGVHNS... | 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... |
A0A804LSL3 | MHSALDGMPYAELAISDEVKEQVELMNAQLMRCKKRTDTQDMELSMDLMVILQNKEEEEQERNADRAILERLARKLELQTLAELRAETMAVKKLINERNESTTQMVGLLNRFKEIAGVDEKDVLGGDVSMPKSLDKCPSLMIPNDFLCPITLGIMTDPVIVASGQTYERRSIQKWLDGGERTCPKSRQPLAHLSLAPNYALKNLILQWCERNMVELQKREPAETESERKGEAADAADSIPSLVEGMSSIHPDVQRKAVKKIRRLSKECPENRALIVDSGGIPALIGLLACPDKKAQENTVTSLLNLSIDDKNKALIARGG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 492
Sequence Mass (Da): 53718
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A0A7U0YFM5 | IFMFLCGLSXAMXXAPLXACXFAXNLVXPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPPALFLLLASSAVEKGAGTGWTVYPPTSFYFSSCWSFRSYSYFLSSPCSCLINLSSYXFHYHNYXYXEQXGMLFXTNTFXLSEQXKSTAILLLXYLSPFXPEXITMLXYSSKFQYXHSLTLPEGETLFCISIXFXIFWSPWK | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
E9NLV0 | FLLLSFIFMMMSSKNSALMMMLAHGYTSTLMFYVIGEFYHTSSTRMIYFMNSFMNSSMIFSIMFAMIFLSNSGMPPSLSFLSEFIIITNSMMLNKILFFFVFVYFMISFYYSLFLIVNSFAGKVYINYNNNNFGIMMFLMVMMYNIFWLSYFT | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A5C2RUM3 | MLGVYNLNEPDFLSSQFQSRKTTTNETLMNVPYLRLGAALTLFRTRAYATEARERVKIVGAGPRDGLENESAVIPPAVKAELVNRLTNARLEIIESGSFVSPKWVAQMAGTPEVLKTMQRVKGLHCPVLSPSEFLYTDEIAVFTAATDAFSKANTNCTVAESLERLDVVLKRATKEGLRVRECIYVSVVDPVKVKDISHALLDMGWYEVSLSDTVGTGDPTTIAKLLRTGHYHHTYGMSIANILASLEYGLHMFDSSVGGLGGCLYSPGATGNVATEDVLYALRGSKYETPGDLNAIAEVGTWISKMLNWTNSSCVGKAH... | Pathway: Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1.
EC: 4.1.3.4
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA
Sequence Length: 347
Sequence Mass (Da): 37895
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A0A3L6E4B8 | MERHRQGSRRQQEDGLDGHDEDGALSAFVCPITMQVMRDPVVIDTGHAFEREAIARWFAECRDLGRGPCCPITMREVRSADLRPVLALRDAIEEWADRQQRDELRRACRWLTKDATEKEAVRALGCVARGWSRGGQASRRTVRAEGIIPMVGGMLRSGSAMVRLKALEAIQEFARETDQDREAVSQGDTIRTIIKFIDCEDCQERELAVSALCDLSKSELVCGKVSELNGAVLILCKVCGSKADNPTIAEKAEKTLENLDRCEKNAVQMAENGRLEPLLNLLIEGSPETQLLMASSLEKIVLSNDLKILVARRVGSLFGG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 828
Sequence Mass (Da): 90856
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A0A1X7PJT5 | MKIFSNTICAAIALTFAAGSALPVAAAPLVAPNAQTEAAGGNVLDVQMSGEQRQRRFDRRQDRREDRFEHRQDRREARFERRNGRYYYNGHRGYRERRDGYRYYNGYWFPAGAFIAGAIISGAINNATQSSGSAHVNWCHDRYRTYRSSDNTYMSSAGYRKACNSPYS | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 19173
Location Topology: Single-pass membrane protein
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A0EVG3 | MHTKKERIEGGRRERDLARRQGHHQCRRTSRSRPPAAQRPAELMSVLVGVHTMPGKHSRRHLIRMAYALQQQTPALRAAARVDVRFVLCARPMPPEHRVFVALEARAYGDVLVLDCAENAEEGKTYTYFASLPTMLGSGSGGGGGRPYDYVMKVDDDTFLQLDALVDTLRSAPREDMYCGVGLPFHDRQFPPFMLGMGYLLSWDLVEWIATSDMVRREAMGVEDLTTGKWLNMGHKAKNRVNIFPRMYDYKSAKGEDFLENTIGVHQLKQDLRWAHTLEHFNVTRLEPSSMLLHNF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 296
Sequence Mass (Da): 33783
Location Topology: Single-pass type II membrane protein
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A0A0D2DP74 | MAPPVMTTGSILLRYGCSHPIATLSALFLAWKSLLLLIIFTSPRLGYDTSSSLLLSVGGKNENENAITGYLSGTPNQIESPWLKFVRWDAIYFTQMAEHGHVFEQEWAFGIGISSTIRWTAKIIGRTMDIGNLTASFMVAGVCLSHVAHWLAVLQIWAIASHLMGAGGGGSNRKSQKESSSEVPFLAAVMHIISPAGVFLSTPNTESLFACLSFCGFLAFLSATSQFHQGTVLRGACTMVASGLAFGLATLIRSNGILAGIPFLIEAVSIAFAVLSSQGVSLSRVVRLGSVVVGGLLVATGMVLPQVLAYQEYCAGQSPG... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 499
Sequence Mass (Da): 53988
Location Topology: Multi-pass me... |
A0A344VW42 | TLYFIFGAWAGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAXNFITTIINMRSSGITFDRMPLFVWSVGITA | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1D6I179 | MGGGGGFRGSCRVGAVLLFSAWVALAALSRLLRPVPNGCVMTYMYPTYIPIAATPRNISSDRYGLFLYHEGWKQIDFAKHIRGLRGVPVLFIPGNGGSYKQVRSLAAESFRAYQNGPLEPTFYQEASSSLPGDGLNNFSIPSRYGRMLDWFAVDLEGEHSAMDGQILEEHTEYVVYAIHRILDQYKESHLERSKGGAQSSPDLPSSVILVGHSMGGFVARAAVVHPNLRKSAVETILTLSSPHQYPPIALQPSLGHFFSHVNEEWRKGYKTGVSHAISSKLSNVVVVSVSGGIHDYQIRSRLASLDGIVPSTHGFMVGSS... | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 600
Sequence Mass (Da): 66160
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A0A7Z8PFP6 | GLIIPLIAAHLFVFYFGLMADVTPPVGLASFAASAVSGGDPIRTGFQAFFYSLRTLALPFLFIYNPTLILFGVDLGTAAGLAQAAFIFIVATFAMLLFAAATQGYFLARSRYHESAALLLVAFTLFVPNFWLDRIQPEFERMAGIQFEEVITGAAPGQELRVEVEGPDFNTGQPRSLTLVLNVEDVPPEQRVDDTGLFLMPEEDRMILDEPMFGSPFQSDLGDFDFYGAEPVELVAVLRPADRMPEQIFYLPALLLLGLVILLQRRRQTVPAF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 273
Sequence Mass (Da): 30136
Location Topology: Multi-pass membrane protein
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A0A7C6F9D1 | MCGPDSADCALQPKTASKSLTCRTKRKRAGMRSSRRSLTPSLPKRPATTRLARSIRSCAANRALRRRCPKMLLWADRQLEQLARLFAVIGGAAIFALMGVTVAAVIWRYFLNRPIFGIEDLSVLALIIVAGASVAFGDRRDAHISVDVISYFLGEKARRFTNLAMRLAVFLITGLASYALAVKACGIEKACVTGNLSIEQRPFYYYLSVAFAFLTAQAAVRLLIEIFGAAGGDANRAGD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 239
Sequence Mass (Da): 25995
Location Topology: Multi-pass membrane protein
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A0A1B8BYZ8 | MSTNPTFCVTDVNGVDIRCYLDPSLPATQTMSVAAGSQVGFTASPAIYHPVPLQFYMAKVSSGQTAASWDGSGQVWFKIAALRPTIISSSIDFPAVNMAKVYATIPKSLPSSDYLLRVEQIGLHVASTVAGA | 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... |
A0A142B8R1 | MRVLVLGKTGQIGHELCKLLDSKDITYDAPDRSELDICDAVQLQSCLKHYQPTIVVNAAAYNNPVMAENEPSRCFAVNRDAVAELADLCNRMNIILIHASSYRVFDGEKQEPYSEKDPTNPIGVLGTSRLQAEQQIRERCPEHIILRLSWVISDRRPNLLRRQAEQMVKHREVYVTPDQLGCPTPASDVARVIVAVLQQVNCGAKAWGTYHYCASEPVSESGFAEIMIAEASQFWELKVRKLIMAKMDSREGFKPPANATFHCTKILNTFGVHARPWRNALSDIIRLYHEEQKNN | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen 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(+) + NAD... |
A0A3Q7SSB7 | MDVITSTSFGVNIDSLNHPQDPFVENTKNLLKFDFLDPFFFSILLFPFLTPVFEILNIWLFPKKVTDFFRKSVERMKESRLKDKQKHRVDFLQLMINSQNSKEMDTHKRKRKELQRAIDEVAQKQGVVPRCGGRFLADGILAN | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2... |
A0A2E8QA97 | MKIYTKKGDQGETRLLYGDAVSKDSIAPEAYGSVDELVAALGLIRYEKKLPKETKKLILQIQRELFIAGAELATSKENRSKLVPDETLVTTSMIENLEKNIDFLTEKNGIPEFFVVPGENSISAKFDWCRVVS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphat... |
A0A2P6FMR7 | MTVKTLNDYELQNKKILVRVDLNVPLNQAKILDSSRIERLVPTVRKIIKEGGRPILISHFGRPKGKYDKLLSLEQLIPELSRFLDCRVKFSTETTGTEALKKVEGLANGEVLLLENTRFNPQEEANELNFSKSLSELGDIFCNDAFSASHRAHASTVGVANFMPNCIGLLMQQELTALKSVLSKPKRPVVAVVGGAKVSTKIDLLSNLIQKVDHLVIGGGMANTFLHAQGNPVGASLCEKDLKGTALNVLKRAYERGCEVHIPHDVIIASDFKPNAKFTVVEAGKVPEGKLILDIGPSTCDKINQIFNKCETLIWNGPMG... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 395
Sequence Mass (Da): 42884
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A0A6P6GGN0 | MGRSLFLPTNIPLSFSGIPRLRSPPNLSHGSLPLSIRIKFKHGFQIFPCSNTKEARTLCTRAVLSEIPNQKQYPKMGAQSTGPIAPSRLIQVAETAASTGAQVVMDAVNKPQSITYKGLTDLVTDTDKMSEAAILEVVRNNFGDHLVLGEEGGIIGETSSDYLWCIDPLDGTTNFAHCYPSFAVSVGVLFRGKPAAASVVEFVGGPMCWNTHTFSATAGGGAFCNGQKVHVSQTHQGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLVPYE | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 278
Sequence Mass (Da): 29897
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A0A6P6G3N8 | MKFYISTSGIKKVTISSSGKGAPATASRRVSSRTFLPVVLVLGILLPFLFVRIAFLVLESATACSSTIDCIGWRFFRGSDSSLVSVATLLTKIPFILLFTEGNVNNEEENESFNELVKDMTSKRQDLKAFAFKTKAMLSRMEQKVQSARQRESIYWHLASHGVPKSVHCLCLKLAEEYAVNAVARSRLPPPEYVSRLSDPSFHHLVLLTDNVLAASVAVSSTVQNSANPEKLVFHIVTDKKTYTPMHAWFAINSIKSAAVEGKGLHQYDWSQDVNVGVKEMLEIHRLIWSYYYI | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 294
Sequence Mass (Da): 32896
Location Topology: Single-pass type II membrane protein
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A0A545B9N7 | MIVRDFNELKNTDKAVANERWTSVRMLLADDNMNFSFHITTLEAGSEHEFHYKHHFESVYCMSGKGRIIELDNDNKTHEIQPGVMYALNLHDRHRLIADDGADLVMACCFNPPVTGTEVHREDGSYAPADTLQKA | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotect... |
A0A3B9K6B1 | ICDCIGLEKEREFRNMSSFLHKAHAAAPETEMDRYLSRTDVWAIAFGCIIGWGAFVMPGTTFLPIAGPGGTVVAMAVSAAIMLVIGMNYAYLMVRRPGTGGVYTYTKEAFGRDHAFLCAWFLSLSYLTIVFLNATALFVVSRTLFGNVLQRGFHYAVAGHEIYISEVMISVTALVVTGLLFIVHKPLLQRLQTVLAILLLLGALAITLICLPNIDPGSVFHFFGEERGISPSVILTIVLLSPWAFVGFDVISLETAHFRFPVRLSRGIIILSILMGGFVYAAMSIVSITSVPDGYPSWQEYIANLDALEGVATVPTFFAA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 679
Sequence Mass (Da): 74840
Location Topology: Multi-pass membrane protein
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A0A804QMG3 | LPASSAPPHRPPTSHLLPPLYCLRLSVIRPSATVVIPPPSVHPPPRVHPPPWRDEWRMHPMVGATPRLSICIVAFRIYLVSEASYNCLYRPSGDHHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A6P3ZWX9 | MSHSLKTHSLTLLLLFTLSSTATSHFSSSSSTSTTQPSTWSEWRSARATYYAAADPRDIVGGACGFGDLVKAGYGMSTVGLSESLFERGQICGACFELRCVNDLRWCIPGTSIIVTVTNFCAPNYGFPADGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPIQYRRIKCRKEGGIRYTISGSGIFMSVLISNVAGAGDIVAVKVKGSRTGWLPMGRNWGQNWHINADLRNQPLSFEVTSSDGVTITSYNVAPKSWSYGKTFESKQFES | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 268
Sequence Mass (Da): 29148
Location Topology: Peripheral membrane protein
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B5YKC3 | MSIFKEEDLALLIDSKGRKYLVSLKKDATFSFHKGYVQFNDIIGKNDGLKVFSSMGEKLYVFKPTLEEYILKMKRGAQIIYPKDISRIITLLDIFPGAKVFEAGTGSGALTLYLLRAVGESGKIVSYEKRKDFHETAKVNIEKFMKNKSYGELTLENKDISEGIDEKDFDRVILDLTEPWLFLDKVIDVLKPGGIIGCYLTTVLQIYSLMEEFDKKFYDRLYKIGIFELLERKWEKEGLSLRPALRMVAHTGFIVAFRKLS | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
EC: 2.1.1.220
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 261
Sequence Mass (Da): 30002... |
D7S9V8 | MLIICGIISLVFSLHYFFLSIMCYLVSVNDFYNSLIGWEYLGFVSFLLILYYSNYDTSRAANITLVSSRFGDVGIFFIISTKSAIFPFSSWLLEAMRAPTPVSCLVHSSTLVAAGIWFF | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 119
Sequence Mass (Da): 13444
Location Topology: Multi-pass membrane protein
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A0A317Y966 | MSDSTYITSRAILSTWNDWVDMINAKMIDRFQGEHMVYHSFDSAMDDPHNYYPPEFLNTLTPNGLPPHVLKLKIGCPVILLRNIDPANGLCNGTRLVVRGFQRNSIDTEIVLGQYAGKRIFLPRIPLCPSDDEIFPFQFKRKQFPIRLSFAMTVNKAQGQTIPNVGVYLPEPVFSHGQLYVALSRATARLNIKILAIPAVDGKKRSRKGVRKNPTVDCGTYTKNIVYKEGGKNIIKFEGDHNSPRPQSYYDSVFIFFYKSLHPPLLSAARSKLHMGAFKIGLLVDVSKTYVTYAIKFVKLHDVGYLSDWKTKKACNYFFF... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Membrane
Sequence Length: 551
Sequence Mass (Da): 62323
Location Topology: Multi-pass membrane protein
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A0A1D6G6E1 | MAGRRPAPAALLLLAVAFAPISSAVRPVSDAHRSAAEELFAPSADGSFGDLESTYEAVKTFQILGLEKYNSLSGKACKFAAENLASTDSTAKDLFHAVRISGALGCGVDAGVYDGVVARLKAVIKDTNSLLEFYYSVGGLLSIKEQGHNVVLPDAESTFHAIKALSQSDGRWRYGTNSAESSTFAAGIALEALAGVVSLADAEVDPSMMVVVRNDIVKLFDTIKSYDDGTFYFDEKHVDATEYKGPIMTSASVVRGVTSFAAVASGKLDIPGDKILGLAKFFLGIGLPGSSKDCFNQIDSLSVLEDNRVFVPLILSLPTK... | 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 m... |
A0A6P3ZKW8 | MQKMAQGWFSGGTGSEVTEKPSSSLLSDWNSYTAAQASEDSSSLGLGFDLESAVRSANDTVSGTFNVVSKGVRDLPGNFQSATSSVPSGKALMYFGLLLATGVFFVFIAFTMFLPVMVLMPQKFAICFTLGCGFIIGSFFALKGPKNQLAHMSSKERLPFTIGFIGSMVGTIYVSMVLHSYILSVVFSVLQVLSLAYYAFSYFPGGAAGMKFLASALTSSVMKCFGR | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 24223
Location Topology: Multi-pass membrane protein
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A0A967CKC9 | EERWRDFAQRLGLSHVPTNNPAQTLWLHAASNGELNSVLPLLSRLRDRGMQMSILITCNSVTGVRLAEENGYVAQLAPLDFRWSQTRFLKTHGISTHVTIESEIWPNRIHALHARGIPCIVLGARLSATSLRKWQRVQKIAKHSLEKVAFFSAQDSQSKERYMTLGLRPEAVGVTLNLKSLFQTKTPELARSARANTCLAASTHPQEDELILEAFKTARESWPKLRLILAPRHPKRAADISAAIKKFGFRHVSRSASGSFDTDKHDILLADTLGEMDRWYAQSGVCIIGGTFQSHGGHTPYEPAAYGCAILHGPKVENFQ... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A804M3C3 | MAPRTVASAVLRVQMALLDGAAVSSEALIHAAASVLLSSADYDDVVTERTISDACGNPACPNPLPSSSAAATGPRFHIALSEHRVYDLEEARKFCSERCLVAYKALAASLPHDRPYAPHSKNPSSVLQFQDGTKKKKGVSSNYLSLRRLAVWLAEPAVRMRLMAVLVDGCRGLRGGAMAVCTVSHQNLHFILHGAPPGGLLLVSKDPDNIREIALREYTELVIDETEVSEATPAVADGLVGEESYAQVQIGRQILGKGVGLTWEEAKLQVVASMDWLEITKGKLYVVVVLHMRTTAMTRRERSSREIDVRNLPSSSRATD... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step 1/1.
Function: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
Su... |
A0A1D6J8E9 | MSSSDEIPSVKQLFLALVLGYVSTKSDMLHQEPLSTALSAVNLLMHFTGWLSFFLLVNYKLPLRPQTKRTYYEYTSLWHIYAILSMNAWFWSSIFHTRYEIARGLQCILQFGYITVICNNI | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 121
Sequence Mass (Da): 14107
Location Topology: Multi-pass membrane protein
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A0A3Q7RCY0 | MHSGALWWSGRLKLAWSDSAGKLAVFDTWSALAVHIAMDNTVVMEDIRRLCRGSLPCAGAAALPADSSRHCNGFPAGAEVTNRPAPWRPLVLLIPLRLGLTDINEAYVETLKRCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEFTDSCFIPDESFHCQHPPSRMSIGELDPSIAVGFFCKTEDDFDDWCQQVRQLSLLGGALPMFELVEQQPSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
W6K9S0 | MAAERPLSSFHRALDRLSGLFALGGGMLLVAVGLMTVVSIVGRWLFFVPVPGDFELMQNGCAVAIFTFLPHAQMRRGHVAVDLFTRSLPPSIQKGVEAIGFGIFTLIAALLTWRLSLGGLSFLTSGETSMILGLPLWWSFPPIVASCALLTLCCLSDLIGSLRR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 17662
Location Topology: Multi-pass membrane protein
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A0A162IVY5 | MYLRDCIVRENSCIASSYYRMVVEIPEELLESKPGQFFMLKSLQDSFSLRRPISIHQLNKKERTMEFYYEVKGRGTKSLSMFKEGESISLQGPLGHGFSLVKKKKVLVLGGGMGIAPMKYLLDALKEENEVTFVAGGRNQEAIEILDSFSFQKLRAYITTDDGSVGMKGNVVMKLKELLESSSYDQIYVCGPHGMMLAAAEVAQEKEVSCEISLENRMACGVKACVGCSIQTVEGMKKVCHDGPVFDSKMIVNYEPKEKSTICCRN | Cofactor: Binds 1 FAD per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate ... |
B5YK60 | MEKILMLGCDAIARGAVEAGISYASSYPGTPATQILEYIAKNSSVKAEWSVNEKVAYEVAYGVSLTGRRVLCSMKHVGLNVASDPFMTSAYLGIKGGFVLVLGDDPGAYSSQNEQDSRFYASFAKIPCLEPSDAQEAKDMTKLAFDISEELGLPVMIRSITRLLHCISPVTLENIKPEKEIKLEKNPEYLLAIPKNVVRLHSELNKKQEKIKKLLEKYEFNKIFSGKGKTGIIACGITYLYAKELGEDLPIFKISAYPVDEDLIKNFVKNLDEVVVLEEGYPFIESLVKKYCPNVKGKLSGDLPLEGELCVEPLLKLFGK... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.8
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredo... |
A3RES8 | SHPLIKIINHSFIDLPAPSNISAWXNFGSLLGVCLILQILTGLFLAMHYTSDTLTAFSSXTHICR | 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 membra... |
A0A7S1VN64 | VPKAVASMQSKSILNAAKAIMTTDRYPKVRSVVLSNGARVVGIAKGAGMIEPNMATMLSYILTDATVEKKTLQSILSDVVDKSYNSISVDGDESTSDTVALVASNQKPALEDNAEFQAAVEQVCTGLASDIVRNGEGTGHVMRVVVANFPGTDHEARRLGRHVVNSPLFKCAVSGNDPNTGRLAGAIGSFMGKFKEDESTAKMTLTLGGRTIFNQGKFVLEGDDVEKEISNHMKDAQFDDAGIFPEHQKFVEIGIDFGTGSGKATVLGSDLTEEYVKVNADYRS | PTM: The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities w... |
A0A1D6KTN0 | MLSVQTYSLTFNVSVSVSIYPLKSIFWRTEAIQVEGTVTDSCSPWYSRPVIACMAAGRTLGSQRIEATTDGNRANGQPLLVNDQNKYKSMLTHTYSTVWMIRGFAFIIYMGYLYIWAMVVVIQIYMAREFSSYSENPMKRNNCQGSGS | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 148
Sequence Mass (Da): 16760
Location Topology: Multi-pass membrane protein
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A0A251WG73 | MPPSASAPERVSTSPSIRRILRYVEWTVLTVILVILLVAPTLPAWKWLPTWMVFPFLGMVTAMSFGMPLDQPAWQRRSYVFIEFLLVFACQLAGFNFDVLLYLLIAKSCFLLSRRDVAITVLGIGCIWLPFQIMLFPLSLKFIQQLNQPQIPQFVFSNVINYTGSYITASVFVLLFSYAIVAEYKSRQRAESLAQEVETLAATLERTRIAQEIHDSLGHTLTTLDIQLEVAQKMRDRDPQIALQAVDTAKQLASQSLQDVRHALQTLRSSTVNLNEAVMALVEQTRQHNSFTIQAQLDLPPLPLQASHQLYCVIKESLMN... | 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... |
A0A258BS88 | MPHIVRLPLVAVMLMAGACSEAPKETAPAQTGNEAAAAPASALTVLKDASGKEVGTAQFVQQDGGVSVDVAAAGLTPGLHGTHVHMTGKCDGPDFKTAGGHWNPTEHQHGLENPQGSHKGDLPNMDVAADGTGAVRFVIPGAVLTGGANALLDSDGAALVVHAGPDDMKTDPAGNSGDRVACGVILGS | 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: 188
Sequence Mass (Da): 18664
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A0A6L5GP12 | MTEKLHDFQVAFHTPPPETPTDGFVRKSRALHLVSGVIAAAAIVAAVMCFVLGAARVSGNSMAPAYRDGTFVWFVRGGSTFSRGTVVSVTMPSGDHYIKRVVAGPGDTVDIADGKLIVNGKTVDEPYARGRTERQADGLMVYPYKLPASKYFVLGDNRAHSADSRIFGPVSAAQIQGRIVSTK | 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: 183
Sequence Mass (Da): 19570
Location Topology: Single-pass type II membrane protein
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A0A6L5X702 | MEKGEMMTGTQADAAREQSDVQNVPPERIWSQIIVLGITGGVGAGKSTILTALHEQYGALIIECDEVGRALQQKGAACYEPMRQLFGDGILFPDGTIDRKAVARLIYTDAQKRDMLSCIVHPAVKAEVRRQLEAFDRQTEAGFSGLFQNHGASEDRTACQAGEQSMPAPGLMAAGRLPDRAPDPQREEAGKVHPGKRRALAVVEAALLIDDHYEELCDEIWYIHTDDEKRRVRLRERRHYSDERITRMFEAQRSDASFRRHTQLTIDNTDDFVQNTFRQLKEGLKSHFPELFL | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A0W0SSW0 | MAITKDDLENVKQLAYLNAESSDNIKLAEEVSAIMDFVEQLKQVDTTGIAPLFHPFHLHQRLRTDEVSEKDCTEQLAEIAPLFGDNLYWVPKVIDSGQ | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
W0RJ39 | MAERGREFYKMCGSGNDFVFFDARDQAPGALETPELIQRMCARGTGIGADGVVFLERSAAATVGLRYFNSDGSPASLCGNATLCTARLAVELGAADPSGFTIATDAGVMAARFRDARPEIDFAPVQELTADAPVRSGAAERRIGYARAGVPHLVVEVPDIEAVPLASRGRELRFDAALRDGANVNFVAPGPDGAWYMRTYERGVEGETLACGTGAVATAAVLGAWGAADGPATTIVTRSGRPLVITRGAAGRGPSLAGEGRIVFVGRLREVE | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
R6XMW5 | MLVLQSLFPGAQDIIDKLFPSGWQPFLVQFIAMLVLVAAFFILLFKPVRKIITTRQDHIEANIKEAEEKRLSANEYLSKSQEEIKVAKIKAQDIIVEAQKTAENEKNKIINATKEEVRNLKIAADKDIEESRRRAKDDIKREIIDVAFQASEKILQREINEDDNEKVLNNFIDSLNEEEK | 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: 180
Sequence Mass (Da): 20809
Location Topology: Single-pass membrane protein
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A0A7S4KZX6 | MASLKRAVNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGTWSFGDYFKKEAIAWAWEILTEVYKIPADRLYATYCEGNLESGGTIPPDEETRQLWLQYLPADHVLKGSMKDNFWEMGDTGPCGPCTELHFDRIGGRNAAHLVNQDDPDVLEVWNLVFMQFNREESGKLKELPSQHVDTGMGFERLVSVLQNKRSNYDTDVFMPIFAAIQARLNIPPYTGKIGAEDEGLKDTAYRVIADHARTLSFAIADGAIPSNEGRGYVLRRILRRAVRYGQQMLDAPPGFFADIIPTVVERFKDIFPELAEKEKMIIEVITEEENS... | 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 tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activ... |
E4L8K9 | MKFLLIGITMLISVLLIVVTIAQESKQPGMGSSIGGGTQAMAGGKARGKDAVLAKFTVIFGIAFAVLCILLGRFMNTF | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 78
Sequence Mass (Da): 8135
Location Topology: Multi-pass membrane protein
|
A0A356VSP1 | MAVQMQVDIVSAEGSIFSGKAEMVFAQAANGEVGILPNHSQFLSSLKPGQVRIVSGDEEDFFYISSGIIEIQPTVLTILADTATRAEDLDSAVAEEAKLRAEESMEQAKSETDIARAQVELAEAVAQIQTITKLRDRLQKTGLA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 15496
Location Topology: Peripheral membrane protein
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A0A2M7H3G2 | MEHILIPPHGNTLVNRVLSEAHAAEAKTRLAGKFSLTLDDEQVKDVKNIARGVLSPLTGFMNESDFVRVVEEMRLADGTIWSIPFVLDVSEEDASNMNTGDEVALQDATGNLIAVLHVGDIYGYDAAHVARFVYGTDDSAHPGVAHWQAMKSRLVGGLIDLIDNTKEPYYEVNLDPAETRYLFKERGWKTVAGFQTRNVPHRAHEYLQRCALELTDGLFINPIIGKKKTGDFQDEVIIKAYHFMIENFFPRESATFSILPARMNYAGPREAVLHAIIRKNFGCTHFVVGRDHAGVGDYYGTYAAQKIFEGIEDEIGIKIL... | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
EC: 2.7.7.4
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Length: 387
Sequence Mass (Da): 43124
|
A0A1F9VP31 | MGTSPKALLKRSAQTSWKKDIARAFPSAKWDEPLKYHTTFRIGGLADCYLEVRNQKELIRLYRLARTHDLPVFILGFGSNLLVRDGGLRGLTVRFRGSYERIRMAGKALVRAGAGVRLPKLAMYCAAKSLSGAEPLIGVPGTVGGGLVTNAGTRDGEIGSLVREVEVFSIPKLRCEKRSASELEFSYRSSNLKRRVILGALLKLKPGRRAAIMRKITAYQRARLETQPVHTFNVGSIFKNPPGRFVARLIESAGLKGLRCGHVQVSCRHSNFIENDGHGTSRDVLDLVKRIRRSVLRRNGIRLELEMEIVGEK | 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: 313
Sequence Mass (Da): 34804
|
A0A0G1DVN7 | MFWADSIAEDIIQKNPDKKKFIIRDEKTLSGRVHVGSLRGVVIHGLVAQALQERGKEAEYYFEFNDFDPMDGLPVYLDEEKYKPYMGQPLYTVPSPDPAHKNYAEYFGAEFLEVINRLGFTPKIIRGSDLYLSGKYNKWIEKIIAHPAEIRKIYKEVSGSQKPDDWYPLQVICEKCGKVGTTKVTGVKGDKVTYKCEPDMVKWAQGCGHEGEVNPYDGRSKLPWKAEWAVKWCGLPVDIEGSGKDHNAAGGSHQIASRICKEILEMPVPYNIPYEFFLIEGAKMSSSKGRGSSSKEIADLLPPELTRFLMIKNQPKHPID... | Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 522
Sequence Mass (Da): 59306
|
A0A1L6BW86 | IMSFLLIGWWYSRADANTAALQAILYNXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEHNNLTTPLMGLLLAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLFTXXXXXXXXXXXXXXXXXXXXXXXXXIVTIGINQPYLAFLHICTHAFFKAMLFLCSGSIIHSLNDEQDIRKMGGLYKSMPFTTTSXIIGSLALTGMPFLTGFYSKDLIIETANTSYTNAWALLITLIATSLTAAYSTRIMFFALLGQPRFNPLILLNENXXXXXXXXXXXXXXXXXXXXXX... | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 458
Sequence Mass (Da): 50818
Location Topology: Multi-pass membrane protein
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A0A3A8JQS2 | MGITPASLSLGAQPLDKGRTRFRVWAPRRHTVEVLLSEPQGIRALPLQEESHGYFAGTHAVAVGTRYKYRLDGGDAFPDPCSRFQPEGPHGPSQVVDPSRFAWTDAGWKGIEAHGQVLYELHVGTFTPEGTYSGVASKLALLKDVGVTTVELMPLNTFPGHHNWGYDGVSLFAPCAVYGDPDDLRRLVDEAHRMGLGVILDVVYNHLGPDGNYLAQYSKGYFNSKYPNDWGDPTNFDDGKDAGASRDFFLQNAAHWIAEYHLDGLRLDATQSLYDASPRNIVGELVSRSREAAGGRRILLIAENEPQDVNIVTPPEARGQ... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 627
Sequence Mass (Da): 69612
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A0A2R6AJB1 | MLERLKQLSIGYIISYVYKFYTIRLEKSVANGAKPKHIGIILDGNRRWAKWRGYPPTYGHRVGYNKAKEVLDWCWELKIPTVTVYALSLDNIRRRSKEEVENLISLVDMAVTELMNDRRIMERGVKVKVIGRRSVLPKELLQKVEKLEQTTANNKNFNLFLAVGYSGRAEIIDAIKKITEEVQAGKIEIAQIDETLFSKYLYTAGVEDPDLILRTGGESRLSDFLPWQAIYSEFVFIDVPWPEFRKIDFLRAIRTYQLKERRFGS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids... |
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