ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A961FXR1 | MDPEERARKLKMAEEVVMEAPDYDALAKPFYDQVAEHGKLAAQVRAAVVTAYEALPKPDDPAIRTPPGREKLRAAAADYAHLMETLTRVEKTLPKWRHDKPVSRTRGVLMFFAGRDWVTNSSWHDFYGLLPLLTGSFLISVLALVVAVPFSVASAIYVNQLAGRREQNLIKPAIEFIQAIPSIVLGFFGILVLGSFLREWSQGQLHVSPHGFVGSLPVIREIFTGICGFLNWVAQYVPGFPMSERLTMLNAGLLLAFMTVPTIFTLAEDALNNVPHSFTEASFALGASKLQTILRVVVPSSLSGIVAAVLLGFGRIIGET... | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 400
Sequence Mass (Da): 43801
Location Topology: Multi-pass membrane protein
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A0A1H3DD93 | MESFSAIKKRMKSVDDISQMTNAMKLVSSAKMRRSQLLHDNMYPFFLFCVESMQEMIRKNEHLDNPFFVLDQKQEGDTWKIGYYVLSGDQGLAGAYNNNMVKITEDHVRTKILDNTQKGMSTSYELNVFGRLAREKLMKNGYNVNSEFSFPISEPTYFDARQVSAVMRHRFLNDDFDLVYLLYTRMESSVKMEPVALRLLPVDTKSISRVLPDKLEDAGIATLTGADLEYFPNSDAVFDYLIDSYTNAMVYGAMVDAFATEQTARLTAMENATDNAEEMMKKLELLSNRARQAKITTELTEIVNGAQQADKM | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 312
Sequence Mass (Da): 35633
Location Topology: Per... |
A0A1H3EG41 | MAKRVFLVVADSFGIGGAPDAGKFGDEGSNTLAAVLSYSNDPYPNLAKLGLLAIDGEDDPRIISYKKAQESIPSPIGSYARVREVSAGKDSTIGHWEIAGIISDKAQPTYPDGFPDEVIKALEKATGKEYLCNKPYSGTDVIRDYGEEHMKTGKPILYTSADSVLQIAAHEEIIPLEELYDICAKARAVMCGEHAVGRVIARPFVGEPGNFTRTPNRHDFSLAAPSSTMLDLLKSEGFDVISVGKIYDLFAGRGLTESNPTKGNTDGINKTIEFMDRDFNGLCFVNLVDFDMKYGHRNDIEGYATAMHEFDNALGVILGK... | Cofactor: Binds 1 or 2 manganese ions.
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to ge... |
A0A6P6KSZ6 | MPDAMIRRSMLFFTLLVHFARGQVSYSIPEEISKGSMVGNIAQDLGLDLQRLKSGKARIYTRDSTEYIELNRNTGLLLIREKMDRESLCAKTTPCALHLQMILENPMEFYTITIEIMDINDNAPSFQKKDFSFEISESAVAGAGFMLGGAFDADVGTNDLQSYSLKPADKFQLELHSQADGSKNVEMILEKPLDRETQSSFTLLLEAFDGGDPVLSGTVQIHITVLDINDNAPVFTQKVYKTTITENAPKGTVLTVVSASDADEGSNSVVTYYISDTVNKNVADMFLINEKSGELILNGHIDYERVNHYELNIQGKDQGG... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular Location: Cell membrane
Sequence Length: 951
Sequence Mass (Da): 104689
Location Topology: Single-pass type I membrane protein
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A0A0G1CMN2 | MGTLYIVSTPIGNLEDITIRALHTLFSVDAIACEDTRVTGNLWELLKNKYNDLISVTHKPILIPYHNNNEQTITPELIQLLKQGKNIALVSDAGTPLVSDPGYRIVTEVQKQNIPIIVVPGVSAFLTALTGSGLQTNTWTFLGYLPEKQSRRITKLRNMKKSSVMLSSTYICYVAPHKFIQTMKDIHQSLGDIPCVIGRELTKIHEEYWKGTPQEAFGHFSHPKGEFVLLFTL | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mas... |
B4L4H7 | MQSSVFILTVIFAIIASNAPQIDALLRRCYQCRSRGELGSCKDPFTFNATDVDNEPGLSAIPCASGWCGKVIEGGGPYALDDYDTAIQRMCVQRGPDDNIDRCADTIYNYKKVYMCFCQGDLCNGTDGRWRQHHLLLLLTPTSIVFNMIVNKIFV | 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... |
A0A960ND91 | MKSPRFERIALCAALLLCAGSAAFAQRKLPTISAFELGYSVRGWTVDDGLKGPYVGAFVQSPDGALLFSDSEGVIRYNGIAFEDLIETAPPGVPRRNILAIHEGPDGRLWTAGLNGQAMREADGRWAAVGEDRGGHSGVGKFARGPDGRLWCAVSTGSGLVLSAWEDGRFQPVPEKPLRTGYVQELMFDSAGQLWLSVADQGGGPPVYRLEGDSLVPESAADDRVGVLFHKEGDTRLWLATEQGIRVREGDAWREMVAFSDELPEKNGFSACSVDREGNYWIATRSLAVWVCRPDGEVSRLISEVVKLPNLVRDLFARRD... | 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... |
D6STN3 | MQYFLDLALKTAQGNMLADSEQKTLLELPYEETHRLFPGAELLRRNFCANKIRVCAITNAKSGKCSEDCAFCAQSAHHNTSINSYPLKNPGQMSLEGRNMSAQGVNRFSLVTSGKGLEAEEVQQVCRVTRELASQGISPCASLGVLKQQELQELKDAGLTRYHHNLETAPGFFPSICTTHDYSQRTETVRLARQTGLSVCSGAVFGLGESDAHVLELALTLRELDVDAVPVNFLVPIPGTPLENNDQLTPLRCLKIICMLRYMLPRHEIIVCGGRLENLGELHPLIFMAGASGLMTGNYLTRQGRGVAEDMQMITDMGLE... | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a ra... |
A0A0P9DNX9 | ERGGEKRNAVLLVDFNFKTIDDLCRRVSLGKKGYVYIIDESAGNIVYHPQQQLIYIGLKYENVEQALKYTYGNYLDSSSGDMRLITIATVNNIGWKIIGVSYMDEIVTAKKEIGGFIAWLLLFVVVFVLLISAFMSAKISQPIRRLERSMSKVEQGVFDIHIQVQGDDEVGRLSRRFNYMVARIRELMGQIIREQEAKRRGELEVLQAQIHPHFLYNTLNSVVRLAGGGKSEEVITMITALSKFFRISLSKGRTVISIQDELEHVRNYLIIQKMRYKNKFEFAIEAEPEVLGCRTLKLILQPIVENAIYHGIEMMADEGF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 410
Sequence Mass (Da): 46406
Location Topology: Multi-pass membrane protein
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A0A961B7C0 | TLYVTLEPCSTRGRTGACTDAILEGRFRRVVIGTADPNPKHSGAAISILRNRGVEVECGCLESKATDLIRFFAKHVTTGRPYLIAKSAITLDGRTTLRNGDGPWISSKESRRDVQRWRRRIDAILIGGETLRRDNPRLTLRGAFAKGRPQPWRIVLSQSGDLPEEAYPFTDSHRDRTRVFVGESLEAVLDRLGAEGVTSAMLESGGRLFGAALSAGLIDEIILYVAPFLGGGSTGLGSPGGFLADLESPTFKRFGNDIRVTGRPRLRPLS | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
EC: 1.1.1.193
Sequence Length: 270
Sequence Mass (Da): 2940... |
A0A951US31 | MAAPGWVEEGNPTFGRVVGLRLCETQPTILLNTKRIEFKETLNYSNLFLPILVGIISTFIFSYLSIAWLLRYLQRQSTWVFVWYRLAFGIVILGAIFSRN | 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: 100
Sequence Mass (Da): 11561
Location Topology: Multi-pass membrane protein
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A0A950GYA7 | MAGLAVAEALDRARSYSHAVVSFVGPDGYPVNVAAPFAVHDGGSLEIGPLGRDVQPAPGSTVEVTFSHIRPQPGIGYDERRYVNVWGTGRLDGPLLHVAPTRAAGWDEAETPFFEYAERSVPAGRAYIAELGVEPRLSPWWTFFLATRLPFLTATFIPVGLGGAVAAYDGRFEGLWFALALVAAVAVHLGLNMANDLFDDASGADAANVTPTPFSGGSRVLQYGLVSRRVMLVGCAACYAVALGLGLLLAVERGWPLLAIGAVGIVLSLVYSGPPFRLVHRGLGEPVTALGFGPVMAEGTYFATTGHWSGAAALASIPVA... | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 327
Sequence Mass (Da): 34180
Location Topology: Multi-pass membrane protein
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A0A849Y758 | MRARTGYFITFEGSEGAGKSTQIRRLASRLRRAGHRVIVTREPGVTSLGRRIRHLLQFSRAGQGMTEEAELLLFGANRAQHTREVILPALRRGEIVISDRYADSSVVYQGVGRALGRGFVERMNRFATGGLAPDLTFVLDLDPVEGLRRARGKTRRADRMEAQKAAFYRLVREGFRGLARAEPRRVKLVDARAGIAEVAARIEALLPARFRGGREKGARAAPRQTVFPKE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 230
Sequence Mass (Da): 25650
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A0A2E6X9T7 | MTSRGSSPIVLAAGGTGGHVFPAEALAAELTGRNYRLILFTDQRGCAFSGVLRDVETYRIHSSSSLRNKIPYFVRSGFKLALGLFQAIHLLRKLNPCAVIGFGGYASVPTMLAASLGVYPTLIHEQNAVLGRANKFLAHRVNNIATCFTVVEGLPETISSKVLVSGMPVRSGIIDYQNCDYHTVTPESPFHILVIGGSQGARVLSDVVPASIASMPEPIRQRFKIVQQCRPEDIERVHATYASAGLNAELASFFDDLPVRLAAAHLVIARAGASTIAELTTIGRPSILVPYPYAINNHQARNANAIDEAGAGWVLTESSF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A0L7RGR2 | MANPGDYISCGGFAFYNNFDSANLSRVELVKEPEILEKDGCESENKSCKSSNSEDTADYEFNLWTKHDCHGTQFQNNNRTWFYFGVKASTPGACVKFNIVNLNKQVKMFSQGMCPVFKIVPGHLHWERIRDRPTYTLDQKGSDFTLSFTYAIPENPKAMTYFAFTYPFSYNDLQNYLRRVEARVSKRAITSADDVYYHRECAIKSLEGRRMDLITISSFHNISTEREDRLNNMFPDKNEERPFKFWDKKVIFISARVHPGETPSSFVFNGFLNFLVNREDQIAAHLRRLYVFKLIPMLNPDGVARGHYRMDTRGVNLNRV... | Catalytic Activity: C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate
EC: 3.4.17.24
Subcellular Location: Cytoplasm
Sequence Length: 873
Sequence Mass (Da): 98779
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A0A2E6W4B9 | MSPVYNSIGVLLAGGLARRMGGGDKSLREVGERMILEWVVERSRPQVERLLLNANGDVTRFKHFGLPVVPDVLDGFVGPLAGVLSGLEWAIGSGCDVRWIVSFATDAPFIPINMVERFEAEAVSTDSDIVCASSGGRRHPVFALWPVTIAEDLRKALVYEKVRKIDRFTANYNVQVVEFDTDPIDPFFNVNDPGNLEEANTLYRQLKYERAI | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2D8YX43 | MTDISTFLDMGGYAGFVWPSYGAVIGVLAVLLWLSLRGLKAAERELAQLEGEAPRARRASPTNDGAAQP | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 69
Sequence Mass (Da): 7334
Location Topology: Single-pass membrane protein
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A0A2E5MVP3 | MEKTTIPSDIAKLSFEDALEQLEKIVRELEEGSGELEKSIEAYERGAQLKFHCESKLQEAQTRVEKVVLADDGEVALVSAELD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A1H6HGU4 | MRLFAAGLAVFLSIAPVSAGAGDLPEDFVRLRDIDSTISQDIRYAGPHNFIGVPVDGYLRAECWLTRPAALALKGVQDDLRAQGGGHSLIVFDCYRPQRAVDHFVRWAADPADTLTRAEFYPDLDKRDLFRLGYIAERSGHSRGSTVDVGLTGPGARPAQPYRAGQALTACTAPYRERFADGGLDLGTGYDCFDSRSHPASTEVGAEARENRRILAEAMEARRFVGIAEEYWHFTLRDEPYPDRRFDVPVE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 251
Sequence Mass (Da): 27793
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A0A847CKS2 | MKKIKIFVLVLLILSLTACKQKNEEEISMYNNATVNAGFDTYISISVATTSQEKFDEYFNNLISDFKYLNQLFDIYNNYDGVNNIKTINDNAGIQPVEVDPIIIEMLELSKEYYDISDGQFDITLGPVLKIWHTYREEGLLLLEQGKLGSTPNIEDLIEANKCKGWDKVEINKENSTVYLNESCASLDVGAIAKGYATEYVAEKLEKENIKVGIVDAGGNNRTINTKLDGTPWNVGIQDPTGGSGSIIVVKSEGSKSFVTSGDYQRYYVSEDGKQYHHIIDPRTLFPSNYFHSVTVITEDSGVADVLSTTLYTVDFDTGN... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A0D6JBV4 | MTNSAAPDSRNNTKPVQSDAEPAVGGAQLGKMLLEVGPLGVFFFANSQGGIFWGTGCFMAATLVALSLSFIIYKKIPIMPLISGVFILVFGALTLWLHDDLFIKIKPTLVNTLFGSILAAGLFFNQYLLKYVFGEVFRLRDEGWKLLTIRWAMFFFLLAALNEIVWRNFSDEFWISFKLFGIMPLTLVFAMAQVGLLKKYDASPKTP | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 207
Sequence Mass (Da): 23094
Location Topology: Multi-pass membrane protein
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A0A9E4D280 | MQSESPRLSILGWDESHREQLEAPGPGRVLARVATEHRGYYDLFGLEPDPLVVADNAVVSPAFRRGATGPLDFPSVGDWVTVSPAAGAEGADVIETVLSRRSLFVRRAPGREPRPQAVGANIDHVLIVTGLDGDLSERRLERYLAVAYGGHAQPSIVLSKADRAGHSDDIADALVAIDRVAPGVRVIVTSSVSRRGVDELADLAADNSTVALVGSSGVGKSSLVNALVGEQLQLVQETRQDGRGRHTTVRRDLIPMASGGLLLDTPGMREVQLWDDSGLDQAFPEIAEAAADCRFGDCAHSGEPGCAVAAAVDTGLISAA... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
B8CWJ4 | MIDVSSKKVAVIGLSKRTGVSVARTLVNCGAEVIVSDIKEKKDLKDEIEMLNEYEVEFDLGGHSNKLLDVDLIIVSPGVPLNLPFFKSISEKGIPVISEIEFAYHLTEANIIAITGTNGKTTTTALTGEILDKADIGEVRVGGNIGKPLIDVVQGLKKNDWVVAEVSSFQLETIRDFKPHISAFLNFSPDHLDRHLSVENYWKAKKRIFENQMSGDYALVNYDDYKVLKAVEDCSARVFGVSLKDNIEQGIYLEEDKLIINSADRSEVVLPVESIPLKGKHNIYNIAFASLIAYLAGASTEAIKEGVYQFIPEPHRLEEV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A1I0NN14 | MTAYTATVTVRLKRGVLDPEAETTKGALERLGFELEDLRSADRFEIDLEADSADGARERASEMAERLLANPTIHDYDVEVAER | 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 ... |
A0A7W2CBB9 | MSFSLWIDPSFGASGDMLLGAFSEMLDDPDQALFPLRNLPIEDWKIDFEETLRNGLTATKAEVSYRETSTERKWSEIDALLKESSLPHPVIEGSRRTFLILAQVEAEQHGVTLDEVHFHEVGAVDAILDVVGTWLLRFALEDEVGAIEEIAIGPVGIGSGSVKASHGTLPLPAPATIGILKDCPVTNVSTNSETCTPTGAALLVSMVNRWGNIPNGYIRKSSRGAGTRNPTEYPNIISMVLTENSKTHKSSKTKYLIETNVDDVTPEILATTIEKLLELGAEDAWITPIIMKKGRPGQEIKVLCSADYLQSLQDLLLAST... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A284VLB0 | MGNRANFKGIKGKDMNWFYLQKYLPEYLTSEDMAAIDENAATLGIPGLMLMENAGAGTARITKENHKVDEKRIVIIAGTGNNGGDGCVAARHLLNLGASVCVILLGQPDDIRTHEAKTNWEVLSNLDVGIKVVKARNPSDLELLRNEIKSSDIIIDAILGTGIKGSIREPIATAIQLMNESGKPVVAIDTPTGLDPSTGDVKGDAIKAELTVTFHRMKKGLIDMEEYTGKVYVCDIGIPIEAELFTGPGDVRRVVKPRSLYSHKGDYGYVLVIGGSDVYSGAPALAAMASLRTGAGLAISGVPESASSAVKSYAPDIIVH... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A061IGF8 | KLSSIHSALHTCLVVQRKKPTAWATGHHTLQGTMVSQYKPGQLIHASWNFTIDEKYSFCFIRYNKNNKIWEVINYNATGILEKWEKNAELAQDLAVLSMGDSRHCLEEYLKHQKEMPSEDEPPLSKAGKDVVLHLPTDGVILDGRESTDDHAIVHYEWTLKQGDPSVDMKVPQPGTLKLSHLKEGVYIFQLTVTDTVGQRSSDNVSVSVLPRTYSMGGCSSVCSRYHFFCDNGCCIDITLACDGVRQCPDGSDEDFCQNLGLDRKMVTHTVATSAQPGTTGPSEGEGDPWFEKPQKVTPHNQPAIVPHSEKRVHSTQWAP... | Function: Acts as a ligand for KLRK1.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 45744
Location Topology: Lipid-anchor
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A0A960E2Q6 | MSDQTTPTPVEEPTQHGVLSRLYHGETDWNIVGRWKLWFAISGVMLLIGGTAVVTRGLNLGIDFTGGTVWEVPAGDATVAEVESAVSDLGYNDVQVQEFTQVSGEGDARSLRVEAESQTEPTAATTDALDTALADLRSAADSVRGGSADRLNGVGNQLDGIEGPFDDEIPAELTDLQDQLDGFADGLDAAEDQTAYVTEVADLMAADVDALAEAEQAHREEVGRSVSEALAELTGSDIDQVTVDTVGASWGQQISQKAETALVVFLIVVLLYITLRFEFRMAVATVAALLHDLLIVIGVYALFQFPVTPATVIAILTILG... | 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: 473
Sequence Mass (Da): 50653
Location... |
D6SP88 | MIFDQYQGQRVHLGITGSVAAYRTLDLVRLLQKSSLSVSATITSSGCAFIGPLTLSALGADPVYTPDYSPVEQPFAHLSSQFSPHVFMVAPATANILAKASSGIADDLLSTQILSYPGRVLFAPAMNPNMWNNAATRHNIRQLRDFGHEIIEPDSGKVACGEQGQGRFPDIASLYYICLRELTSKDMVSTKVLITAGPTHEYFDLVRYWSNPSSGRMGLAIALALWLRGAEIHFVHGPMQPLLPLPGFHIYPVTTARDMYDKCSALWPDCTLGVFSAAVADFAPEKATDLKFKKQGRSALQVKMNPTLDILAEMSASRAR... | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
A9A4N9 | MSESKEPNVVGINVLKQNGVDVDELVNELIKNAAVEFTAYYYFTNLRAHCTGMEGEGLKGIIEDARLEDLSHFESCIERIYQLGGSLPNDATEFIKISGCEFLQLPPNPTDHKAILEKCLKAEQGAIVNWNKICKMTLGKDPATYDIAKDILAEEIEHESWFLELIYGRPSGHMRRKYAGERPHTRKHSRALDMA | Function: Protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, which prevents hydroxyl radical production by the Fenton reaction.
Catalytic Activity: 2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O
EC... |
A0A940IAY3 | MVKLSRDNRGVTLVELLVVVVILSIIATVSVIAIGNIIQTQRDKAFVGNAYMLVEAARLYLTEQQIQGQSVGRIPYQLLVERDWMEELIDPYTSTKLNHQENHSYVSVKDGTVEGVCLKGHTKNLCFFDGSVQPIPLKALSVELIREN | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 148
Sequence Mass (Da): 16554
Location Topology: Single-pass membrane protein
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A0A3E2HLS2 | MPTIPCPRKGEADPVHAIFSLYVRFRQAYHAVKDRILAILYYHHRTPELIQKDVKVLSRLPQHLSVILKLEDARRGGAGLETLVDEVAEIASWCACAGIPMLSVYEKTGILKGYIPATHKAISRKLSSYFGPEHPILSLRAPNVSSLESVTSTPRGEPTEHPVPHVSVLLLSAEDSQDSLVDLTKTLAEMAQRSKLSPNDISQDLIDAEISESIMGEPDLLLLFGPVVELSGYXPMANPTYRNISCSR | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 248
Sequence Mass (Da): 27344
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A0A6F8PRK1 | MKLVVTWTLALLITTALATLMLYDNGIVSMAWGGWIVETSLSFFVGGFLVLFIAAYFAVNFIIKIWRFPRYWRNRSQMRRYSKAQGAMTEGMIALEYGEWYKAEKALIRGAKQSEAGLINYLSAAKMAQNQNAFDRRDKYLQQARDAYPQEYMLIGLVEARLLLEQAPWEGLALLQALHEQEPKHETVLAEFCKVLVQLQQWDELERLMPLIRASKALVRDELWSLQRELWAGKLSQTKDVDALDHLWHQLSSKEQQEPVILAEYVEQRIGFGEEVGVAELIEKALKRQWDNRLCHQFGRLTLGPAFELLKKAEKWSKSQ... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 391
Sequence Mass (Da): 45148
Location Topology: Multi-pass membrane protein
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A0A0B8NXY2 | MLPAGVSTSTALQFLMLSVGAIILLTTNVDPKKIVNTNVFIAGMSAVIIIFGIAWMSDTIIAHNKPYIISLVEDVVKAHPWTFAIAMYASSVFLKSQAAVLTIMLPLGFALGIPAEVLIGVLPACYAYYFFPFYPSDLAAITFDRSGTTKIGKYILNHSFLIPGFIGVLVATFIGYSLSVGLLPIWLWAVAIVALVFGVNSYMNRLSSETLKLA | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 214
Sequence Mass (Da): 23089
Location Topology: Multi-pass membrane protein
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A0A1Q3MPB6 | MNLMQPTHLLILLVIVVLLFGGSKIPELMKGVGKGIGEFQKGINESKMDNDGKKSDEKEDAKS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 63
Sequenc... |
A0A9D5NDP9 | MNGFFYIDKQSDWTSRDVCNKVQKIFNLPKVGHIGTLDPFATGLLIVCVGKATKASAYYDDNEKEYVATLKMGKKTSTGDLTGEVVEEKEIVSFTKKDILDVFKSLTGEIEQQIPMTSAVHVNGVKLYQYLHKGVEVDRPTRKVVVKDISLIEVGEDYIVFKATVSKGTYIRVLGEDIASKLNNLGYISSLRRTRIGDVKVEEAKTLGEVKDSDLVSIASLLKDIPSVVLSGERLIKAKNGMTISFDDITKSDRILLIDENNNVIAIYGYDHLNYYKCLRGLY | 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: 283
Sequence Mass (Da): 31608
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A0A960XLW2 | SFARYRRIFHHLLDMVCRRQPELVVLVDFTGFNRRFAHALRERIARQSPVFGNWQPRIVQYVSPQVWASRPGRGRKLAADIDLLLCLFSFEQDWYARRVPDLQVEWVGHPICDRHPAQWQALTGDDASDSGGDRPPLLLLLPGSRRSELQRHLPVMLEAARQLGGRKPLRARIVLPGEHLKALALRIAGAVGARAPAHSRDETAPSRLSLPLGGRGNNLTVELRVGELAQSLGEARVAIASTGTVTLECALFGVPTVALYKTSRLTYQIAKRLVTVDCMAMPNILAGSRVFPEFIQDAATPENLANAALELLTDDTRRRT... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A7X0SNG3 | MLRSFFFARQSIRAKIFLAFSCVTALSLMAVSAVLYIHMSGEATRNATRFASDNLRHSNEVMQMILEDVDRINTVVVADSGSVDVIAALRSDAFDPSYEWFREKQGVTALLTNLIAYKTPITSIAVVGLNGKMYTSGTPEWVEKQRLTDDAIRQVSEGAGKHVYILRRGADGEPEALMVGRPIHYNNRPIGAVITELDYRQIERIYQAGLTPGVANDVVAQDGRIIVSGNPQLPADAALHTLAAEPPAVPKASSRIVINGERYITVSSAMPYAGWTAQSAIPVRTLLPRYQQLRLQMAETAAAVFLAVLIVSMGVAAGIT... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 600
Sequence Mass (Da): 65977
Location Topology: Multi-pass membrane protein
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A0A1W9P4G7 | MCMLKIGKAVLGKQPKIVLTIGEIKPHLLKPSLLKKVDILEVRIDCFKDIEEGNVVSFIWAVKKACLRATRKEKPIIATIRSKKEGGARYISPLIRLRLFKAVMPLVDGVDIEINSPILRKVFQEVRAKRKKVILSYHNFKQTPPDNKLKEIIKQAREKRGDIIKIACFAKSKKDTLRLLNLLFKHRGKNIVAISLGEEGIISRFLFPFFGSLWTYACLDKPFAPGQMNAAKMREALDRISNCSNV | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DH... |
A0A927WX26 | MKLVIVESPTKAKTIERYLGKDYKVLASFGHVRDLAMSGYNDLGVDIDNDFTPKYEIVPKSERVIKQLSAKAKDAEEVLLATDPDREGEAISWHLAELLDLDIDDTKRLEFHEITKKAILEAIENPRTIDMNLVHSQEARRITDRIIGFKLSALVQKKLNARSAGRVQSVALKLIVDREREIESFQKEVSYKIEAVFKIGKKEYTSILVNEKGKEVEFENKEEAMKVLSILSNQMKVLSCDAEEKQNYSLYPLTTSSLQQEAFSHYKYRASKTMKIAQSLYEGVDLDSGRVGLITYMRTDSIRLSPKFIYAAKEYIKDTY... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A924RSK0 | MRLFYALPLPLEVQNALEVAQKKLRGNWRAVRPDHLHITFAFLPKAPEGALQTLVKLGHKVGRNFAPFKVRLRGTGYFPGAGSPRVWFVKAEALLSGGEEGDEMGLISSELRSGLTLPFEDKPFKAHITLARKKGPAPRLEPMIFPLEWEAEEFVLIESQLHKSGPEYRTVKKFSLTGPKRPPKPLKPERLPEAEASRVSPLEPEELEVPSLLEPSQTNPRPNDL | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 225
Sequence Mass (Da): 25220
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A0A963N9C2 | MSAAMFIVMLLCFAFSIPIAVSIGFASIAGIQLFGSVPLLVVPKEIFGAIDKFALAAIPFFILAGNLMEVGGISRRLVEFAKAIVGGLQGGLAMTCVLTCLIFAAVSGSSVATTFAIGAILIPAMIKHGYPTGFATSLQATSAELGVIIPPSIPMILYGVSAEVSIGELFVAGFGPGLLIVAGLIVFVWIWSKIKGFGKDDHLGRLPFGTAFRQAALALMMPVIILGGIYGGIFTPTEAAVVAVFYALAVGMLVYREIRFEHLFPIFKKSV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 271
Sequence Mass (Da): 28397
Location Topology: Multi-pass membrane protein
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F0SEG5 | MSEEIEKNKIYPTFNFTQGEVLLINKPYKWTSFDIVGKLRNSLKPLKLKVGHAGTLDPLATGLLIICTGKLTKQIDSFQAEEKEYTGTITLGSTTPSYDLETEPDQFFDISGISENQIKENTKHFIGDIEQFPPIHSALKKDGERLYLKARRGEEVKVSARKVSITEFEITRIELPEVDFRVVCSKGTYIRSLAHDFGKQLGIGAHLSKLRRTKSGNFRIDNAFEIMELVNHIKEIKQDPEFK | 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: 243
Sequence Mass (Da): 27651
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A0A6P6P6U1 | MNTVVIISIGTQFMHIALFHQAGYLNQAQWDGLTGRIVLNKTDGLRKEFNLDLISLKEDGTAKRAADAASRPTKLWTKIGVWNSYTGLNLTEMIDSKNITDSLANRTLIVTTILENPYVMYKKSDKVLYGNDRFEGYCLDLLKELSNILGFTYEVKLVSDGKYGAQNDKGEWNGMVRELIDHIADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLTPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNSSSEVIENNFTLLNSLWFGVAALMRQVSSGVMDLMLVKRGL | Function: Receptor for glutamate that functions as a ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system.
Subcellular Location: Cell membrane
Sequence Len... |
A0A832NGN6 | MGSSKRIAALDFGEARIGVAVSDPLRLFAQGVAVVCASEGWEEELASLLKRYEVELVLVGVPIREDGQPSHQAAKVLSQAEALIALLPEVRFAFVDERYTTKLAHSYLREVGRGMRRAKELSDMVAAEILLQEYLDAQRKEGSDGER | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16216
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A0A357QZ06 | MQQYFINQALTLNQPFSLSNEQKHHILTVMRYGVGKHVRVIDVDAKTFICEIVSTNPFQLMPFEQRVELTEPSVDITLIVGWIKKERFEWMLQKVSEAGATRVIPLISAYTVVKEKEDTLDKKLIRYNKITEEAAEQSRRTRSTEVLAPISLAAVGDYLSD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A520XS58 | MYSFLASHIDWIKALHVIAVIFWMAGMMYLPRLYVYHSQAVPDGEMEKALIGQEHRLLRIIINPAMIVAFLLGLVLVVLRHDQLAMISWLWIKLFAVFILFYIHGILAADRKKFARGERPRTEKFYRILNEVPAILIIIIVIMAIVEPF | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A357QYK5 | MYFNSMDIRRVSLCPIRKSAIYLMKKENVYMNKQLVIATNNGHKVEEFKKIFEPIGFEVTSTKDLGIDLEVEETASTYQENALIKAMAYRDLVSGWILADDSGIEIEALDFQPGVFSARYLGEQTPYEIKNRMILEKLEEETNRRAQFVCSIALVNEEGSYWVTINTCKGSIAHQILGSHGFGYDPIFIPDGYEQSFAQLPPEVKNEVSHRGKASKAAATYLHYLSEESYHE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
B8D0R7 | MEHKRLGRREVKTIFAGEFYVTTSSDVIISTLLGSCVAVCLSDDFNSVYGMNHFMLPTRVRESNNVYSGKYGEDAMELLITEMEKRGARINYMTAKVFGGGQVAGTTHSNVARANIRLAIQFLKKKGIPIIARDVGGKHGRQIYFWPRKNVFSRKIKMTEIKDVSVNE | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 168
Sequence Mass (Da): 18927
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A0A9D5RWF1 | MKRYRRILKSEEFQEIIHHKRFFTSPSLCLYSAPRKKENSRIGLSVGKKIGCAVVRNKCKRQLRMMAIDIIPFEDNRDYIILARANYFNYSYEENKKQLENLYKKFKIRKEKKEKQNEIQ | 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... |
A0A2P7EER4 | MNDAVIIRGLRLWAHVGVLEWERKYGQWFELDINLYLPLAXAGENDDLTKTLNYADVIESIRQLARQINCQTIECFSEQXIKTIDSIYGVMPXEXELRKCNAPIAGFNGCVAVRRRRD | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A5C8P6L4 | MLARFNLMLAFLLVICALGLVTSQHRARKLFIDLERAQTHAVEHEVRWDQLQVEQTELAKASLIDERARRELGMQAVPADRTLHLSVDPVTRSVSLSQPWIERPSGARLSGVRAAATGPRKPDNASGTRRASPAGAPRAAPTGAPPAKGVRQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 152
Sequence Mass (Da): 16541
Location Topolo... |
A0A1Q9NIP9 | MLQTCTITELIINCCYFVGLYEDINSMTFPTSPNNKRIKGNILDNTKINLKDYFSLTKPRIIVLLTVTGIGGFFVPQPNMIGVSFLDLLIFVFVGYAAAGGAMTINNYIDRDIDILMDRTKDRPSVREEGLEPIKVLQFGIVLTTLGIVTAGLYFNLLTALFLSWGALFYLFGYSLFLKRKSILNTILGGLASPAPVWVGYAARTNSIPIEGWLLGAIVFIWTPSHTWALSTKHMADYKRANIPMLPVRLGMEKTAKITMFAGIITMIYGTWFAYYLESSSLVIIALIIPNMILFYGLWVFYDKPSTHTADICFKAHNAW... | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A5C8P3F5 | MSEWLAMGGHGFYIWSSYAMMALCVAAEMWSLRQRRKAAWQRVDEAREEHESARPARRTETE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 62
Sequence Mass (Da): 7319
Location Topology: Single-pass membrane protein
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A0A0L7QU56 | IFFVLVTLISTYAFVLAYKNTKFMLKQKIEVKTEDVVTMDMSRKLTEDKKISMQEKDERLWKKTEVANYKTTTFSIFCNNALFLALV | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 87
Sequence Mass (Da): 10242
Location Topology: Multi-pass membrane protein
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A0A663EHH9 | MNWGVFEGLLSGVNKYSTAFGRIWLSVVFIFRLLVYVVAAERVWSDDHKDFDCNTRQPGCTNVCYDHFFPVSHIRLWALQLILVTCPSLLVIMHVAYREAKEQRHRAAGGDDGRCIYPNPGKKRGGLWWTYLLSLIFKAGVDVVFLYIFYHLYRNYTLPRLVKCELPPCPNTVDCFISRPTEKNIFTLFMVVTACVCVMLSLVEAAYLIGKRCRECLLAGSGDSHQHGQDCALSPHRARGHGGAGFPRGGLQTSHGLHPRHGLQPRHAVRGGGSSLELPGGKQEPLTCPAPSSSSSSSSSIPPVQEPWGWQHLGVGLCSK... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 466
Sequence Mass (Da): 51108
Location Topology: Multi-pass membrane prot... |
A0A6F8PYB0 | MNRIFIDVGNSRIKYAVSEDGHYEYLGAELVQDFLANIEQSLFAEVNDIDEVYFSTVGSLQNLDELTSAIQQHWNIIPTQLNAQRSCCGLTSGYADFHKLGSDRWLAMQGALAITTQPFIVVDAGTALTIDAVIDGQHKGGFIVPGLSTMHNSLATGTALLEMPTNNDLPEDMSQNLLANNTASAVLAGTLYMSAAFVNQVVVDLNQQLQTQFKLFLTGGDAAQLASLLDYQYSYIPDLVLHGMCSVVESVKKS | 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... |
A9KV33 | MTDQELAPSIAQCGIALLLAAFLHIALTAAVFWSPAVITPTGQAKAVGNGGIEISLGPAGSAASALQQTTAPVAEQKSEPITEQLDKPEPLPPVAKKVTPTPRPKPKPITPTPQDELTTQSEVNEQHSSPTETPSPTALAASANEVGQSGEGHSAEQNKAASGDNMTGGGLLGDTQDYTATLLAWLEQHKEYPRTARNRRQQGTVMLYFVLDRQGRVSASRIEQSSGYQTLDAEALKMLERAQPLPAIPDAMPNETLELVVPVQFFLR | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A3C2CY67 | ESFKLYIFLSGIIFLVIVLSLVTYVLISLLLKKMYNLKDSMKRVAKGDFNFDVDIKGQDEIAELAFHFKSMLGKINSLIADAVNKQATAKETELKALKTQIDSHFLYNTLENIKMMAEIEGKYDISDAITSLGEMMRYNLRWKNDFVVLEEELNYIKNYVDIMNLRMDGLLTLKIEVPKDLLEQEVLKMSLQPIIENAVKHGIVPNNLSREGVITVKASYVDGSAIIDIKDNGVGMSPAHCELLNSRIQSDLDPQYEASKTGNGIGVKNVYERIKLYYGEGYGVSVTSVEGEYTVVTVAIPGKIMKGGSRSV | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 312
Sequence Mass (Da): 34943
Location Topology: Multi-pass membrane protein
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A0A396TWK6 | MTNDKFDRELNSLYQQRQSQITPPNVCVSEKSSAPKRTPLQFIAVFVAGGFASFAIMAFISHLSSAPEPDMAIPLTHVEIDINDVVDDDEDQTVIVIKQPLPKPPTSTQPLAQESMIPSPVAPITPLLAEDIVISPATDTRLPTINLSAFKIEPVLKVMPKYPRNVTLKKVSSIQLRYTITTDGAVKDIVVVKSDVANTLEKATKKALLQWRYKPHATYPIQNEIIFEFEPNEP | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A9E6FAN0 | MPDFEYVANALDLRERLDKVLVKAMPGFSRNRIQQLIDFGYVLVNDEEVKRNTKVRENDIITAEYPEAESLEVVAEKMDLDVLYEDSDLLVINKPKGLVVHPGAGNPSHTLVNGLLYHCQDLSGINGITRPGIVHRIDKDTSGCLVVAKNDKSHHELSHQLQERTLKRTYWALIHGVLEHNSGRIEAPIGRDKSDRQKMTVTAINSKPAVTHFKVLERFKNMTLVECQLETGRTHQIRVHFQYIGFPLVGDLKYGLHQTLDTDGQCLHALAIDFIHPTSEQAMHFEAPLPTYFTTLIQKLRSGDAV | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 306
Sequence Mass (Da): 34620
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A0A2E3L3L1 | MTSSDASACFLLAGMFFSIVFLLAPSVSVTVQIIALGIAVSVLGLPHGAIDTYIARQNGLWLSSSGLATFTGVYLLITFFVIGAWVVLPVLSLSVFLIISAWHFGTDANAQNFAERWLFGSLVFCLPALFHPIDVANLYEILSGPLARNIVSITCVWAPISAIIVIFMICTQLSDRPQRRKDIATILGLITFAWVLPPLVYFAIYFCALHSPTHFCRVIKLIPASDRRRAIMHTIVFTVITLTLAGLSLNMLFGELPVEQSVVQIVFVGLAALTVPHMVLIDGICRSKLG | Function: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal
EC: 1.13.11.63
Subcellular Location: Cell membrane
Sequence Length: 290
Sequence Mass (Da): 31583
Location Topology: M... |
F4XGH3 | MSKKPQYDPEEIRFPDQVIKTAPLVKEMEDSYIEYAMSVIVGRALPDVRDGLKPVHRRILYAMYEDGLTSDKPFKKSATCVGDVLGRYHPHGDQSVYDALVRLGQDFSMRYVLVDGHGNFGSIDGDPPAAYRYTEARMSKLSNEMLRDIEKETVDWDPNFDESRKEPRVLPSRFPNLLVNGSSGIAVGMATNIPPHNLTEVINAVICVLDNENATLDDLMEHIQGPDFPTKGMIMGRSGIRAAYATGKGHIRVRARTEFEEFGKDRTRIIVTEIPYQVNKRMLIKNMADQVEDKRLEGISDIRDESDRNGMRIVIELKRD... | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of ... |
A0A960EU19 | MPDDRCEVVLYHPDHNARLSRLPLTHVRKVVDLWAERSTGLGARDDVNYVLVFENHGAEVGATIAHPHGQIYAYPDVPAAPAHQFARLTAGHQLLEESEELTIVERDGWRAWVPSAPIHPYGLRIAPLAVRPDLPSLDDQERDGMASVMSEALARLEGVFDPPMPYMFWIHQRPFDGDSWPGAHMHVEVVGPHRSPGVMRYVAAAELGSGQYLNPVVPEDAAERLRAVKLGDAG | 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: 234
Sequence Mass (Da): 25904
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A0A2E6W1M2 | MWRKHYMNINKSIIRTADICDEYPEASVIQINFKDYGKKHEFQGVAVIYSTFEDIRGIKELLASDGEGKVLLVNGQGSLRRALCGGKIAAKACSSGWEGLIFNGAIRDQHEIVEIDIGIKAIGSSPKRPSQDGIGGLKKSTVLGDVVVNSGDYIYADRDGVVVLTANAK | 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:... |
A0A7C6H149 | MPVLSTIIYILLFLFFISLLIIFHELGHLAAAKAFNVYCLEFSVGMGPLIFKRKRKGGETQFSLRAIPFGGYVAMYGEGVELPEGVKIDKSRSLNGVKWWKRAIILLAGILMNSLLALVFFAVSNTFPQQILYRNQLNIAASSIASDAGIEDGTIFKIYQEFNYDDPVSESKKTFYLIDKETTINDDDSIKYATCLNYESLDSFSKRDLADYIFIYEQVDNNPDFAKKVDMSLITTAKINFTSMVKDVESGEMVADQIYPIVISKEGDKFASFGASLYLETWTNDFKGVVTQTFTDFGNSSVLLFKAIGDLFTKPSSWNN... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 420
Sequence Mass (Da): 47032
Location Topology: Multi-pass membrane protein
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A0A960MWX1 | VDNGVLHFRIVRKAPGRLVGEALTEGQMGSRRHINLPGVRVNLPSLTDKDREDIALAAAIDADYVAISFVRDAGHVGDLRKALEAQGSPARIVSKIEDQEAMRHLREIVEASDAVMVARGDLGIEVHIEELPVVQRTILEECARVGRKVIVATHMLESMIENPVPTRAEVTDVANAVYEQADAIMLSGETSVGHYPVKCVEIMDRIARRMERERGARFCEAIELTTEKQHTVRS | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 234
Sequence Mass (Da): 25874
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A0A4D8XQY1 | MHQLVTGPEILELDKSVGIPPIIMMENAGLSVSNYILNRLVLKNQYLSVAVVCGGGNNGADGLVVARKLHSLGHHVEVFFVSPRVCGDVDSVLSSFKSEEGLLNAQLALVTHEIPFHTTLGHLGKFSVIIDAILGAGTRPTSDFAQETRLQCVFDAINDLCKEALVVSVDVPSGICPTSGICLYARPIRPSATITFGRVKSGLAFYQYVGELVLATISYPRHVEFKSDRGIMSFCDIPILSSRDPLGHKGSFGKVFVLAGSGRYYGAPMFSSMSFLKAGGGYARLFCPNAVGAVVAGSAPEVVQLGNEWTEVVEEFLITD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
B8CY37 | MLNTIKKWLIAIRPFGFATTLVSTTLGASLAFYHGSFNPGLYFMTMAPLLLIHTGTNLINDYYDYKFGLDGEQSLSSSGLNRVNGQIKLNQIYTVAIACFLASIPFGAYLTLLRGPIIFILGTLGALAGYFYTASPISYKYYGLGGPSIFIFMGVMMVWGMFYIQTGINSWYPVLVGLPVSFLITGMQHSNELRDYENDMKNGIKTAPVIMGFERARYYYYFLIISAYISLVLLITYNLLPLWTTLAFITIPLAYLPVKKVATATSQNDLKGIDYQMARLNIQFGIFLSGAIIISKYM | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol... |
A0A0G0BBB0 | MSKEILHIWGPFSIQSYGLCMAIGILVASWLFLRDKRRESIISYDQFNKVITFAIIIAIVGGRSLFLAEESESITDFLGIFKIWEGGLSSLGAILSVLIFVPIYLNSLGVNFIRFFDLAALYAPIIECIARIGCFTAGCCFGMETSLPWAVLHKEYTSLGQTVYKYVHPTQIYSSIVALFIFILMQIVVQKRLKKQGQLIAAYLMLTSLARFSIDFLRGDRTYFDNTASFSSLSSSQLISILICLLSFISIILIQIYSKKTKNK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A7V7BN84 | MLTITDLKQFVYCPRVIYYTYVQPVPKKPTFKMVYGREQHAELNKKEKRRGLKQYNLIEGERIFGYPIRSLEMGLTGKLDILIDTKDENGQRYFPVECKDTDRGIYNNIKYQLVAYAMCLEEMTNSIVSEGFIYIIPEGKAHKIEITSEQKEFVRKMISMINKIIKDEYYPEPRARKRCWDCEYIRYCNDHDISSQEEQKEKNLELVKRLFNMEERI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A832BA78 | MELTGAQSLIKSLENQGVDVVFGLPGGAILPVYDPIIDSSIRHILVRHEQGAGHAAEGYAQVTGRPGVAIVTSGPGATNIVTPLANAYMDSTPLVVVTGQVATNSIGTDAFQEVDITGVTSGVTKHNWLVTDAQDIPSVIAEAFHVATTGRPGPVLVDFPKDVANAVTTWQDPGPVDLPGYRPSPSPDPAAVAAAADLILAAERPVLYVGGGVLKADASQALADLVELTGIPVVTTLMARGAFPDSHRLCLGMPGMHGNYTAVTAMQRADLLVALGSRFDDRVTGKVSGFAPHAKVVHVDIDRAEIGKVRRPEVAVVADC... | 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: 462
Sequence Mass (Da): 48624
|
A0A3C2CUL2 | MGDFEIFGIPVSLGTMVYQAVLFTILVFLLKRFFFTKLVNAMEKRQQTIDNQLQIAEKTRMDAERLLYDQQAAAAKARLEAKELMLKTQQQADAILQDARKDANKIRSQAREDLKSRRSVSQK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A350IY65 | MQNFMNWMEAHVMPVAGKLGTNRYLKAISSGFIAIMAATIVGSIFTLIGNLPFTGWTAWLASTGLNKILALPGQCTTDLIAVYAVFFIAYNLAQTFEVDGKGAGLAALVSFFVVTGRATYFASAAEDAAAVSALSTGFLGAKGLFTAMIVALIGARIYVFIVKKGWVIKLPDSVPPNVAGSFNALIPSFFVVVVFLLVAMGMSFTSYGDLHTMIFTVIQSNLMRFMGDNIFSWLFFNFMTNILWFFGLHGGNIVGSITNPVYTPLALENLAAFEAGETVMPYIITGAFGKTFTFGGVGSMFGLAILMTFFAKSKQYKMLG... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (D... |
A0A7X8AQA5 | MSKEKLSFEQKLARLNAIVSELESGKLSLDASLKLFEEGNALSKELATELNEAKLKIEELQGK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A847CJU8 | MLENLVDEFKDKKVLIWGLGLEGNSTYTFIKNILPDQQLFICDRNKPDQSMFKNDIVIDEKDLDTSEYDIVMKAPGIKVKKNTGNISGQAPLFLKYFKDNVIGVTGTKGKSTTASLIYHVLQGKFSNIYLVGNIGVPCFDILKFMTLDSIVVFEISCHQLEFSTSSPYIGVLLNLFEEHLDFYDSYELYKNAKKQIYLNQTNNQMAIINYDIINEVEDPERFMWINKDIYADGKTLVTPYDSVTINETRLIGSHNMSNLAVVYYITHVLYGITNDMFLERVKTFKPLQHRLSFVGTFNTITYVNDSISTIGQSTIQAIKS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A960J075 | FAMGSSTENSAFGPTRNPRDTTKVPGGSSGGSTAAVAAGFAAVGLGSDTGGSIRQPAALCGVVGMKPTYGRVSRYGLVAFASSLDQIGPLTHTVADTARVLEVIGGHDPADTTSIPEAMPALESVLGDGVAGLRVGVVRELMGEGIAPDVAARVREAAEVLAAAGAEVGEASVPAVTYGLSAYYLIAPAEASSNLSRYDGVRYGLRVDAPTTPEMNLASRTAGFGAEVKRRIMLGTYALSAGYYDAYYGKAQKVRTLIIRDFAAAYESFDLLLAPTSPTTAFPLGAKVSDPLTMYLNDICTIPSNLAGQPAVSVPFGAGD... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A520XVB1 | MARNARDHSVLAAFGAHHRGRTRVVLLGLDPPGNHRVIKPLVEGDEALVLGLGLYGVAVARALRSRGISVTVAEDRPTDLTATLAEELDVTLLAEPAVEALVEALARADAFVPSPGVPQQHGAFAAAVATGVPTISEFDMARWWDNRPIVAITGTDGKTTVTMLTVEMLQRSGVAAAAAGNNDLPLIEAIDDPQTAVFVVEASSFRLAHTQRFAPRAAAWLNFAPDHLDVHLDLTSYEDAKASIWADLPVGGLAVATLADPTVMKHVPTDRRVSTIGLTEGTSRVVGDELSIDDVPICRIDELPRHFDHDITNTLTAATL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
Q65Q75 | MRKYLTLILAAFAGFAVAEEPSSSLTMEQIPENIAPAYTNPQKDAGNIPTTFPFQPPLVPHSVRGLQVTKNANQCLSCHSPEVSPTTGAPRVPESHFLDRDGKPTEGTSPRRYFCLQCHVQQTDVNPIIQNKFESIRAKQGK | PTM: Binds 2 heme C groups per subunit.
Function: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB.
Subcellular Location: Periplasm
Sequence Length: 142
Sequence Mass (Da): 15647
|
A0A8N1S5Y0 | MCRSMKRVKIVPDRPNRLFESWLEEWRDEATLRNSELRSHFTKALDSLKRYPLPLETAGIKEDCTTTLRQKPVVEKCDVEIQTETVVAKQDKIIKKNAPRRLINASEAKSKEVARQICLKPSTFDIILLVDTQETCGSKTKPQHDATLKELTQLSVLFEVRRLTIGDFVWIARCRETNDELIIPYIIERKRMDDLSASIVDGRFHEQKVIQECFL | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A8N1S7G1 | MLARAFEIYGQFCSGHPLEVIVTISTLTVCLLNLDTGNGQMREENLSDAYCHHDRCDTMDLKATNVIVMTIIRCLAVLFTYHQFRNLQRIGSKYILGIVGLFTVFSSVVFTSSVVSFSRSDIADLKGRLIFYLLRINLSKAATLAKYALSARNQEEVKANIARGMSLLGPTITVDTLVEALLIGIGSLSGIRRLEILCTFACLGVIVNYIVFMTFYPACLSLTIEISRGNNNMRQLSADRIFIMQPLNEEDQKPNPVVERVKMIMIFGLLVVHVHRYASPLSFLGASALTNEEVIQLVKHKDIAAYQLEKAVGDMERGVD... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
EC: 1.1.1.34
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 730
Sequence... |
A0A960E020 | MEQPADDRHQERMSDLESLMWGLEADPMLSSTFANLSWLDGPPDPERLRARMWRATREIPRLRRRVVGGFGPLAPHWEDDPDFDLDRHLRWTRLPPGATDADVRALAVELAAAPFDRERPLWEFVVVDGLPDGRAAMVQKLHHTITDGEGGIRMSLAFIDLERDGPELPPLDDGPPPPADRRPWDGALDAALDLARRNAQGARRLVESATDLARDPLHVASILAELPAETAATTRSMVRQLAVVDSHRSPLWSDRSLDRALATFDVPLDAVKAAATSLGGSVNDLFVAAACGGAGAYHRRRGVGVDELRMSMPVSTRTDR... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 475
Sequence Mass (Da): 51701
|
A0A2N4X764 | MKILLTRRRTNAGNYVSDVKEADEYTIANEHIASIDLMERAARAFVNFFESKYSVSYKKIVVLCGLGDNGGDGLAIARMLYHSGFEVEVIVLDYSERKSDNFKTNLGRLVNKIDVRLCKADVDLPLINPDYLYIDALLGAGLSRPLEGILKTLVINLNASAAELVSVDIPSGLFADSPNGSDDVIVKANQTITFQTPKLAFFLPQNAAYVGDWWVVNIGLHDGFISQLNSGYEYTDAPMARQLIKPRNKFSNKGNFGHALMIAGSFGMIGAAVLSSRACLRSGVGKVTVYTPACGYTILQSSVPEAMCLPTDNQKELEDM... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A920VGH6 | MLLVSAFLGLGSLLRPSRNTPQKVMNYESGFDPQGDMWSQSNIRYYVFALMFVLFDVEAVFIFPWATRLEVYGVFGLVEMAIFIFILALGLFYAWRKRLLPMDLSRRR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 108
Sequence Mass (Da): 12627
Location Topology... |
A0A927WXX3 | MRILVSNDDGFDAPGIHSLAKALCPLGEVTVVAPATQQTAKGHSLTIGSEIRVQKRFFEEGIPGYAVWGTPKDCVDLAVDALLERRPDLIVTGINEGPNLCNDCVSSGTIGGAIAGFINGIPSIATSLDTGDHFDYDKCAPAIRKIAGWFMKMPYNREFALSVNFPNTDEDFKGIVVAESGGIHTFDAHYTVVREDSDSQYYVIPGGFVVLNDVIEDLDHDIYAMLQGYIAMTPVHFDMVHHTALDTLRKDWNEYDR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28170
|
A0A7I8V4A2 | MLELYKNLMNLCESSEVAKFFYKDFTGPMDGKFRVFSYHYASYSEWLKPDALECRGIMFEMDGDTPIRIASRPMEKFFNLNENPLTMGIDISDVEYIMDKADGSLVSSYVDDGYLYLKSKTSLYSDQARQASALLNSEEYSSLHQVILELALDGYTVNMEFVSPNNRVVLAYQEPQLFVLNVRDNTTGEYIKYDDLYANAKIRPYLINAYGISDPTTWVEGVRELEGVEGYIAVLNTGQRFKVKTEWYSALHHTKDSITSNERLFASVVSANSDDLRSLFAGDEYAIKKISAFEQAYLDYLGKSLELCQSFYDEYRGRAR... | Cofactor: Binds 2 magnesium ions that perform the catalytic activity via a two-metal mechanism. One of the catalytic Mg(2+), which is coordinated by 5 water molecules, engages the lysine nucleophile and the ATP alpha phosphate while the Mg(2+) orients the PPi leaving group.
Function: Involved in countering a host defen... |
A0A9D9GWK3 | MINIINDIEAKNIDEITIKKGIASKELMKRAGVGIYKEIKKYLAKDSKVLIVTGRGGNAGDGYVLANELLKHNYEVNIYQIEKNKEIKNLEAKFYQEEYIANKGKFIDNLVDQYDIYVDAIFGSGLNKEISGEYKEVINILNSFNGLKISIDIPSGVNGSTGEIMGIAFKCDYLYTIEFYKIGFIINRGRNYFNKVRIVHIGLDGSDINNNCFCLNKLDFARFFPKRERISNKGTYGRVALIGGCKEYLGSILLSYNAISALRCGVGYTTLCIPQSLVPLYSLHYPEIMYKGMSDNDGHIKFNKDDLDSLLKMNAIAIGM... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A1W9P3S5 | MHLTTGIDLVEVKRMKAAVERWGERLLNRVFTPQEIEYSTRGASFYPLRNPRRRRGIPETCGVSSNMVYQHLAGRFAAKEATIKCLGEEIKQRPMAWKDIEIVNNSEGKPEIRFNQKKRRNKKRISLTISHTKDYAVAQAIAYS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 144
Sequence Mass (Da): 16649
|
A0A6A5ZFE7 | MASCIPIIRAAFFALTHAHGGVYTYNIDSKNYTGLKSPYSEPRYGLPEPNRPYTLSLFTDYVPIKSGGSVTAWWSNTYVWDKNAWSCDDEYLSDPAHECGLSNWIHAHGPMMVYMAAYPGSCSDVRPSTLSWFKITQEGLRPGHKAGDAAGWLQGDIMGKPLTVRGWIVKIPKSLKSGNYLIRHEILGLESDCPHLYPQCAQLNVTGTGIETKAPGMEYLVKFPGAYRPSDLGLNVYT | 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... |
A0A1Y1SDR2 | MNNRHHLQAVAPPSRALGENLRQAELRAPRYTSYPTALEFTGQVGPAALLEQMDKTNQEPIPAALSLYVHLPFCAAACFYCGCNRVISRSAQRRSDYLDLIEREISVLAPHLDRDRPVVQIHFGGGTPNSYRPLELARLIRTLSSQFSIHADCEISMEVDPRQYQPGDALAWAALGINRISLGVQDVSREVQQAINRLQPREQIAELVDEARKADMHGINFDLIYGLPRQTLAGVDDNVDLVALLQPDRIAVFHYAHLPQRFPAQRVIDESELPGLATRLAMQARYSELLTQLGYRHIGMDHFSHPDDSLARALAQGTLQ... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Catalytic Activity: coproporphyrinog... |
A0A7H4PCN8 | MKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLIEFQVPGGQDFKLAHKELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSALKLLDEAGLPGELRLRQKLALVAMVGAGVTRNPLHCHRFWQQLKGQPVEFTWQSEEGISLVAVLRAGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFAREQTTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAIEQDEESLFLWMRAHPYDDLVVLDVTASAQLADQYLDFA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 551
Sequence Mass (Da): 60954
|
G8JT40 | MRIWAENIKRSNYYRYAVPFVKFVLMCYGSWAYCHLFCFVELRDHLHHNAVAVFLTCMNIFLTLILWYIWIQIVVIGPGKQPTVLPFRIIPDAPCDEGTASKDETVVVSVIPPDIYQCDPQGYPMWCSTCQSLKIERSHHSELLKYCVPRFDHYCVWLGTVIGRKNYKLFMQYVMYFTIYLVTASLTIALFMKRIVDYNKEHDLTLNLNIIVLFILVLAFAFFVTPLFAVFSFYMSCNRTSLDIIQKKAIKRHRKAYFCVYNPEDRYRYVVDCLPAEQYNIWNKRNAWLNIKEFIGSNIWLWFIPIGTNISDFQVSRNEE... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 372
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 44019
Location Topology: Multi-pass membrane protein
|
A0A927X0I0 | MIHLNVHSCYSFLSSTIRIDSYLERLVKKHEDSAVLTDINNMCGVMEFIKKCEKSNLKPIIGMEVSVFKYDAEYKVILIALNTNGYYNLLKITPLLNRDLTMEKLFEYQDDIAFIIPSTRSYFGNAIHKDELEVAIKEIEFLKENIKLLYIGLEAYNKIDLEDVKTIRNLKTGVTLLALNEVNSLEKDNETLSVLKAIKDNKLISEVKTDFSQRYLKSEAEMAKLFLQEEIDNTHKVASLVTKYEFSSSIKMIKYCENSKEFLNSLALKGLSKRLNGKINKEYKDRLEYELSIIDKMGYNDYFLVVYDYVKFAKSNDIIV... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+... |
D7B6X0 | MSADDRAPRSRHVAAMAGIAACGGAAGAVARHLVAQAWPTPDGGPPLATLAVNLAGSVLIGVLVAAAAGPRPAPPWVRQLLGTGFLGGFTTYSAHVLDTGALAASGRVAEAAAYMALTLVGAVAGTALGAWATGRAVRALVRRRRP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 14438
Location Topology: Multi-pass membrane protein
|
A0A518XJM8 | MSAMKNSCLLIGLLALYYLLPLEFRGLWQPDETRYAEISREMIEHGSWISPHFFDLRYFEKPVGGYWINNIGQLLFGHSNFAVRFGSVFSTMLSALMLYWLSARIGMTRNAAIAAVIIYLTSLLVYGIGTYAVLDPMLTLWMTAAMSSYWFATEAQGRRQSICRYALFGFFCGLGFMTKGFLALAVPALVIFPWMVKQKRFTQVLIYGPVAVISAGLTCAPWAIAIHHEQPDFWNYFFWVEHIQRFAEDNAQHKAPFWYYLPVLLAGSLPWLALLPGAIKKGCQSSANTYLLSWAVIPLIFFSIAKGKLPTYILPCFAPL... | Pathway: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-arabinose-lipid A biosynthesis.
Function: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic ... |
A0A950ZAG5 | MKILELIQKTTAFFQKKNVPEPRLNVEWLVAHALRIKRLDLYLQFERELSEGELEPLRELVRRRAEREPLQYILGETEFFGRKYHVDRRALIPRRETEHLIEAALLKLPADFACRGVDLGTGSGVLAITLALERPASKWLLIDASDDALALASENARQHGLGKDRVEFRRSSWWSAVSADERFDLIVSNPPYVRADELERLQPEILRHEPAAALDGGADGLAAYREIIAGAAAHAAESANAILEIGFDQAEAVASIFRQAGWKPAKPIRDLQGHARVIMASR | 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... |
A0A1G3FWS8 | MSRLIPLLVPCLIGLAGFSSAQTAEPPALPLQQAAPPQEAITAPPAAPLPPAGAAIPGAPAAADMPAAAPQASPAPQAPAEGITAPPATVEATPAAPATVAPAAPVPQPPAPLQPAAPAPAEPAPAAPMAPANVAATPVLPGPTPETLPSVHDLSPMGMYAQAHWVVKGVMLLLVAACFLTWTVWLFKTVELIVAKSRARHSRRVLHDAESLAAATAALSRRRDPAAFMARAVQEELVRSDALLMAAGPEGMKERGGSLVDRIETQALARIRRGTGLLATVGSVAPFVGLFGTVWGIMNSFISIAETKTTNLAVVAPGIA... | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.
Subcellular Location: Cell inner membrane
Sequence Length: 377
Sequence Mass (Da): 38451
Location Topology: Multi-pass membrane protein
|
A0A7Y1U2U4 | LFLIVVGILSALGIYAGTSGLLGAGINDFFGWGVGVFRYFAPPTLIAAGLAVIRRSDESHQLLPRWIVGGAITLFATVGLVHLAGDSPGWGSTVEEFSAAGGVLGLAIGGPLMAIASFWGALLILIALLIGGLTISTGVPLKTIIDGTAAKAKPLAGAAASGTKSLFVMRGDADTIDLRDEPPPLPSMLVDGKPTDFVDPAGNELDATIEIPVPSAEPPEPSPEPAKDTTAEPVFDQDGDEVEPTVVVPQPPIPPQQLEAAELAVTTQGDRTWILPPMSLLQRSGSQSVDEQAVLGRGRVLERALADHGVETRLVNMVVG... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
A0A1M6KNE9 | MKDVALVLAAGSGTRMQSETKKQFIVLDQKPILYYSLKAFEESGVEKIVIVTSKEDIDYCRKGIVERYHFSKVTEIVEGGAQRFHSVYRGLKAVGDCDNVLIHDAARPMITTELIEDIRSALREHKAVITAVPVKDTIKSSDPDGFVTGTPDRKALWQVQTPQAFRFDLIKAAYGYVIREGMEDVTDDGMALERYTHGSERIKLLEGSYENIKVTTPEDLLIATVFLGKRDKNQVDTKYK | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A0T2Z023 | MTINYLSLAVREVSLLSPYVPGKSIDELERETGMASHRIIKLASNETPMRPNPHVIQAIQDELRNITRYPDASGFRLKAKLSEKFGLKSEAITLGNGSNDLLFMIAQAFLGAGRNAVFSQHSFSVYEAAAKATGASTQEVLALNWGSDLDQILTAINRETRVIFLANPNNPTGTWFDRRAFEAFIDRVPRETIVVLDEAYIEYADDPSLPNGLDYLHSYPNLIVSRSMCKAYGLAGLRIGFAASSPEVAGILNRVRQPFNVNSLALAGACAALDDDTYLQRGRQVNRQGQQQLQEGLSRLGISWIPSRTNFLAVNFERPA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 372
Sequence Mass (Da): 41189
|
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