ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2W5YSQ9 | MECATGCGTLRPRQPAGPDRSFRTTASQDFACGLAKAAHMVGKARFEAFSDGVFAIAITLLILEIHLPSLPAGAADVQQMSALLSLWPQYLVYAASFATIGIMWLNHHAMFIEIRQISHGTVIANLFLLGLISFLPFATEIIARYGMSPVTVVAYGIVLSLISAAYWLLQVQATRAVGKPHRLTLWNVVGLGVYPVASVLGYFVPLAGIVIFGLLAIFYMLPQNVRAATVRP | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 232
Sequence Mass (Da): 25061
Location Topology: Multi-pass membrane protein
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A0A2W5X985 | MKLAAEDRERLELYAVRLLEASQRINLTGAKGPEAVWSHIEDSLQLLPFVESPLVDVGSGGGFPAIPLAIAAGLEVTLIEATSKKAKFLQAIVRELDITGSVVADRAEAAAHDPALRGHFAAATGRAVGAAPVVAELTVPFLRTGGLAILQRGQLVAGEREAVEAAALMLGAAVEEKMAPSGSRLLLLRKIGKTPQRFPRRTGIPSKRPLGARFHGEHNGETANKGSR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 228
Sequence Mass (Da): 24041
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A0A961ZZW3 | MRSAANHYLKHRFCDTANKPRSNSHQTHTAGTIAVTAIAVVGLASFFLSSGPARLARAGRPDLVALSTIDPSIRQDMRYASARNFTGNRVHGYEAGECWLRPSVARALADVQRDLVENEAGLKLKVLDCYRPRRSVKAFVAWAGREEDGRTRNYYPNLSRPELLSLGYIGRNSTHSKGIAVDLTVVRTSPKDKDQRSVDANTACTRTSDHAFDPASLDMGTTFDCFDPKSHTARGGLTSEQHNARQTLKRYMERHGFSNYRKEWWHYTYGAADDGRSFDVPVHAAGRLRDASEVGGVAEKAGVYKAKAAATKAKRKATDS... | 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: 340
Sequence Mass (Da): 37310
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A0A397W426 | MNLIHNFLNKFWLNFLFVIGFGNLKHRKKGQNYNFLSDDTIFLKNDLKKTKKFQLFGGIPFEDIYNLFGLVIVSFIVRLYKIDYPESIVFEESHFGKSVSHYIKRSFFLDYDPPLVRLLFAFVGFLCGFDNDWDEEISYIELGIPYVALRFMSVIMGVLIIPIAYLTIKSAGFSKIAAFLVSALLIFENGLVTQGRLILHGSSFLTFTAFTFLMWVKFYTEEKRPFKLWWWVWMTLTGVGLGLTISACLEGFFTMVFIGLLAIKYLWDLLSDLRTSFTQIAKNLFANALCLIVIPIILYIIFFFIHIAILKYGGADELYI... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A940D7V4 | MKKERLSNAFLFLAAIFITALVVSNIVSFKLVTILGFVVPAGVFMYPITFAITDVISEVYGRKKAAQVVVAGFFSAAIVPFLTFIAVILPPAEFFKAQDQFSTVLGAIPRVTLASLIAYLTSQWHDVWAFHFWKKISKGKHLWLRNNLSTMVSQFIDTIVFITVAFAGAVPGVALMNMIFSQYLFKIFIAMMDTPFVYLGVKALTGHWEIKEEHYAES | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 218
Sequence Mass (Da): 24390
Location Topology: Multi-pass membrane protein
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A0A839NB01 | MTTAEELLAIADRAASYDGVDPFSEQTRLALRHTQPQQVISTDDTVTAGAYVADDGAVELVVDPDHRRHGFGGRIVQGVLGERPDARFWAHGDLPGAQALAAAAGLTVVRNLWKMARAADADPAIGSPEVPAGFTARAFQPGDEEAWLDLNRRAFDYHPEQGKMTRADLDERMAEPWWDPAGLILIFDDATGELTASHWTKIEPSEPDTGEVYVVAVDPGHQGHGLGKVVTALGLAHLKARGVIHIDLYVEGDNAAAVATYSRLGFTRASVDVMYAAQPARTT | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
EC: 2.3.1.189
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Length: 283
Sequence Mass (Da): 30414
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A0A9E3D609 | MTIAVYQGVDGAYSQLVVAHFLREAGFESSTVGVPTYREMATTVAGLRADVGVVPIENAIGGTVREGYDLLAEFDLAPIAEVHWRTDHRLLGVPGAELRDVREVLAHPLVIAECGRFLAGLRHARAIPCEDTGVAAREVARGGNAAVAALAPAAAAIIYDLAELAVNCADDPATYSRFLVVRSRHAADPRLLARPKSSRRKTSLIFGVEERTGSLARCLSILAEHDVNGDKLESKPYLGHGTERIFYIDFDGDVDDENVAAAVGELKQHCRTLTVLGSYDAHLGAPIGSNERPPIARSRDGASTARRVEPIPIAAETPFP... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 397
Sequence Mass (Da): 42189
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A0A9D5JD42 | MMTALALFAAKPTLPPFKGASPPPLALPANVFTQPTWGGQHPFVGGAIQFLFIVCAVALIILMSVQTTKNEGLSGSIGGRSESAYRGRIGLDEQLARLTGGVGVSFMVLAIVNFFISR | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 118
Sequence Mass (Da): 12378
Location Topology: Multi-pass membrane protein
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A0A1E3B3R0 | MDHLRLTFALCQQQGRPALVTYVTAGFPTVEETPAVMLGLEAGGADVIELGLPFTDPIADGPTIQKSNLKALENGVTVSSMLDMVREARQKGLKAPVLLMGYYNPLLRYGETQILADCKAAGVNGFIIVDLPPEEAIRFRNGCTKTGLTTEDRMKVLCGIADSFIYLVSRMGVTGATGSLNAAPCPHQARQGSVWQCARGCWVWYQHPRALSECDLRCGWRRDW | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 224
Sequence Mass (Da): 24505
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A0A401REW8 | MLTRRRPTGGGACAGSPPMSDQGEPKIEFKLVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPIEFFTNRGGIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVQMDPLLAAQYEQDLKNAQSTALPDEDDDL | Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Subcellular Location: Membrane
Sequence Length: 234
Seq... |
A0A0S7Y8F3 | MKFRQAYYDESLLFEKGSNETEPLEDGLIPSGLARKSLEIPNLPIHQIVRHYTRLSQMNFGVDSGFYPLGSCTMKFSPKFAEELAALSQATDIHPLQDISTVQGALRLMYELQEMLKIISGMDAVTLQPAAGAQGELTGLLLAKAYHEDRGENRTQVIVPDTAHGTNFASAAMLGYEVVEIPSKNGLVNLEALKKAVSERTLAFMLTNPNTLGIFEHHILEIADIVHKSGGLLYYDGANLNAIMGKSSPGKMNFDIVHFNLHKTFSTPHGGGGPGSGPVGVKEPLEPYLPVPTIKVEGNDYDLDYSKPKTIGKIHSWYGN... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
A0A2W5X9U6 | MRNHLALVGFMASGKSTIGKRLARKLHVPFVDIDAVIEADHGPISDVFYNHGEKTFRKFEHDAIAHALDGEPSVISLGGGAVTFEPSLKLLKKRTYRIFIKVPPEQILGRLRRSAVVRPLLGPQPALHKIKDLYIKRMPLYAHADLTIEAGDLSTPQIVDHIVDWMHRKKIAL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A924KXM7 | LRKECDFFANLRPATVFPELADASTLRADVVAGLDLMIIRELTGDIYFGEPRGVSGEKGARVGVNTMHYTEAQIRRIMHVGFRTAQQRGKKLCSIDKMNVLEAMQLWRDIAIEIAPEYPDVALSHMLVDNAAMQLIRNPKQFDVIVAGNMFGDILSDEASMLTGSIGMLPSASLDASGKGLYEPIHGSAPDIAGQGIANPLAQILSLAMMLRYTFNLTDWADRVDGAVKKTLSQGMRTKDIAKPGETASSTSEMGSAVVANL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylate... |
A0A1Y3SB13 | MKGNMLIAHGGGPTPVINSSLLGAVREAKAHGEIETIYGARFGAEGILAGDLIDLGKFSDEDLALLAKTPASALGSCRRKLTDADYPAVLECFKKFNIRYFFYNGGNDSMDTCNKIYNLSVETGYELRVIGIPKTIDNDLDVTDHCPGFGSAAKYAAVSALELAQDAAALPIHVVVMEMMGRNAGWITAASALYADLMPCEHLVYLPEVAFDKEKFLAAVKEKWAKGRGLLVTISEGIHYADGSPVADSGVVDGFGHKVPGGAAQALSDMIMQEAGLKSRSEKPGLLGRVSVALMSEIDQKEAEEAGACAVRSAVEGKTG... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-depe... |
A0A961W0B4 | MFDIGWSELMILGVIALIVVGPKELPAMLRTLGRYAGVLKRQAAEFRQHFDQALKEAELDQLKNDLTGFKSEMEGAARDAMTAAERQAESADRAMKSQKTAAAPRSPDPTDAGSAIKSVPPDAGPAGEPHQT | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A7Y3KIM6 | MSQHQKSSATALAVSVVALVAFALDQYTKRLVQRALLPGESMVAIPHLLRWTYERNFHGAFGLFGSNAALLIAMAVVVLVLFWFSFREAATQSRLVRLAFGLIVGGAIGNIVDRIHFGYVVDFIDLYRIWPNIFNVGDSCVTVGVVLLLLSSLLASRRRT | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A5D0MGG5 | MKRIHFIGIGGSGMSALALIAIQKGMDVSGSDIENNTKIEKLKKMGAKINIGHSRENISSNIDKVVYSSAIKRENSELVEAKKQKIKIEQRARYLAGIFENKKEIVVVGTHGKTTTTALGANVLIEKEGNKASYYIGGILKETGKNGNYGKGKWAVLELDESDGSFLNFNKDIALINNIELEHVAYYKNEKELMQKFSKFINNFKGKIYIEVQSFEKIKKLIDNRKNIITVGLDRGDSKPIDFGPKHFKVKEGKINLSLHGIYNTFNSYLLYTALMDNGFDFMTIKKGLETFTGVKRRQEIIYENDKITLIDDYGHHPTE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 450
Sequence Mass (Da): 51400
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A0A140L126 | MIYFRRVATPLGIFLVASSEKGVCRVGLPGEDEGGFTEELERIYGKSYILDEDACSIKNPFNDKLREELMGYFEGGLREFTVPLDLRGTRFQRMVWREVLKIPYGRVKSYGQIAKALGKPGAARAVGMANNKNPLPILVPCHRVVGCDGSLVGYGGGLNLKKFLLKLEGVKFSGERCIIDEVS | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A8I4A052 | MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYVQKKPTMYPPWDSTFDTHINKGRLMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMSEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.13
Subcellular Location: Cytoplasm
Sequence Length: 743
Sequence Mass (Da): 85155
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A0A8C7GJE4 | VFMWLVSSSCCFGTLSLVGPFFVDTELKCQINFSINLPPKTENGKCPVLYWLSGDQQAASEHGTIIGKNESWDFGTGAVFYANATQEPWKTLPRSLCSFFFFSQLSHLINANFPTDQENMYISALKNPGKHKACLCFLFATICNPSQKAFNGYLGKDKKFLSASHLLPDNLIASCSEKIPVVFRLQPGYDHSYFFINDHIKHHAKFLNP | Function: Serine hydrolase involved in the detoxification of formaldehyde.
EC: 3.1.2.12
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 209
Sequence Mass (Da): 23505
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A0A961WE53 | MRDPRDPAAAANSSRTTTSSDEVTSPPESAAGPAGTPGIPDKVVDGANSSERAAASRHHLAELRHDKDAIRRMFETGEYPYKARISRSVYEKQKAELQVELLKVQEWVKTTGQKIVLLFEGRDAAGKGGTIKRFTEHLNPRGARVVALDKPTDREKSQWYFQRYIQHLPAGGEIVLFDRSWYNRAGVERVMGFCSPNDYLEFMRQAPEIERMMVRSEIRLYKYWFSVTREEQASRFAAREHEPLKMWKLSPIDRQSLDKWDDYTEAKEAMFFYTDTADAPWTVVKSDDKKRARLNCMRHFLASLPYAGKDESV | Function: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP or ADP to ATP.
EC: 2.7.4.-
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Length: 313
Sequence Mass (Da): 35948
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A0A9D5GNW9 | MQSPEPTIAAAVEDCRKLLADRSQTPWLDARLLTSHVTGLDASAVIAYGDSILRHDLRRKLYDLVERRASGEPVAHLVGCKEFYGLRLRVDADVLVPRPETECLVAAVIDDWRTQAPRVLDLGTGSGAIACALAHSLPNARVLATDVSIAALSVARRNVEALGLCDRVTLEAGDLFSAVPPGSTFDAIVANLPYVGDDDAHALDDGVRAYEPHVALFAGGDGLDIYRRMFGDAPRRVRPGGALYCECGPFNARSLVSIARSAFPQAAVALHTDYAGLERIVAVRLPQAGSSDVEGRPL | 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... |
A0A518A6E0 | MEQKRLLLFVTLSATVIFVWQMFVVPRIAPRPQPAAQQQAENAPAQDEQEQDLPLVAKKPPKDGEVKPQPEQPEEQKPAFARNPRRTIVLGSLDPESGYFLEAKITTQGAAVMEASLNDPLYRDLNDKKKPLKVLDEFSGAKEVSRSLQIEMKQLDKKLEPFLTNTRRTDWKVLEEIKDPDDPNIIQSVLLGLTAPDGSIEVHKVFRLEKYPVPPDEDFREFRNTNQAGYLIHFDLKLINESSQGQVLDYQLLGPVGIPLENADNTRKFRDVRIGFLQNDMSIDTETLNAPDIIEEVQAKNVEKYTRAFQFAGVDVQYFA... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A925PUG0 | WRGVRTPVTFGAPVAAHSVAFVANDERPAFLAALPPATGPALRLMTHPADNRSKLLLVLGRDGADLKAAADALVTGGIAMSGPSVQVKRVEEKGPLQPYEAPAWVPLDRAVKLGELIDWAQQLEASGRAPDLDPVRVDLRMPPDLATWRGPGVPMTLKLQYTPPACVSEGYLDVSINDELLETQRLRIANEPIVATKEIFIPFYRVRSRSELAFGFRFALKDEAQCRDARAPIVKAAVLPESTIDFSGFPHYARMPNLAHFAAIGFPFTRRADLSETVVVLPEKPVAADIEAMLALMARMGEATGRPATRVRVATPKDAT... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 510
Sequence Mass (Da): 54754
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A0A8C7GWW3 | MVTIPEYYEGKNVLITGATGFMGKVLLEKLMRSCPGVKAVYVLVRHKAGHAPLARIADMINCKLFDRLRDEQPDFAEKIVAVNSDLTLPELDLSKVDQETLADCINIVFHCAATIRFNEPLKDAMLLNVLATQKMVALAHKMKHLEVFLHVSTAYANCDRTLIEEVVYPPPVDYKKLIDSLEWMDEKLVSAMTPGLIGKRPNTYTYTKAIAEYLVQQECGNLNVAIIRPSIVGASWKEPFPGWIDNFNGPSGIFIAAGKGILRTMRASNNAVADLVPVDAVINTTLAAAWYSGSQRHTRSVSHTLQLPGTQAPRDTPGQS... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Catalytic Activity: 2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) + octadecan-1-ol
EC: 1.2.1.84
Subcellular Location: Peroxisome membrane
Sequence Length: 649
Sequence Mass (Da): 71262
Location Topology: Single-pass membrane protein
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A0A8J7CE33 | MIPGTEGGAARVHAILERLSGLHPSRIDLTLDRVWRLLEALGNPQDHLNAPVVHIAGTNGKGSTAACIRAALETAGHTVHTYTSPHLVRFNERIRVAGDLISDDRLAALLEEVESANAGLPITFFEITTVAAFLAFARTRADAVILETGLGGRLDATNVVTKRTLGVITPVALDHQAYLGNTLEEIAREKAAILKAGTGVSARQEPEVLRVLEARARDAGCRLLVEGRDWSVESTGDGFRVHRAGGETADYPRPALAGAHQKANAALADQVLEVLGDRGGTEGAGLATTTAERSRAFSREVTWAARMQPLDRGRLVESRP... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue ... |
A0A8J7IG39 | MLANLVRKEGDPPSQDEAVNEAYDYSGDVYDFYKEVFNRDSLDDAGYPLISSVHVGDSFGGPMSNAFFNGRQMAYGDGDGKLFVRFTKSLDVVGHELTHGVVSRTSNLEYFGESGALNESFADVMGSLVTQWKNHQTADQADWYIGNEILGSEAKIKCLRTLKGEKAYENDPVFGTDPQPKHYKDLYTGSRDRNGVHINSGIPNHVFYQLAMTIGGYAWKKAGQIWYKTMLALNTKSDMKDAAKQSYIQAGSLFGNNSLEQQAVKKSWDVVGLPV | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 275
Sequence Mass (Da): 30501
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A0A2M7F9L2 | MIRSFWVWSAGVFLTLVCGAFVILFSFLDPTRRIIYFFAKLWARGILLAAGVKVQVQGLENLTSDSSQILASNHQGFFDIFALFACIPIRFGWITKKELFRIPIFGYAMKRFGNIRIDRSNKENAREGMQLAARKIREGQSIIIFPEGTRSLDGRLLPFKKGCFYLAEASGKPVVPISISGSFNIMPKRSFRVNPGTIHLVIGKPMRVQGAHENNRNAFTEQLRQTILENQVPTSGVRH | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 239
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A7R6P5Q9 | MKRIFILLLVIMFAGTWLGQKMIQDSGYTLLAYGQTTIEMSLWVFMVIAVALFFALHWGLNLLSRSLKSGTTLRLWSGSRKSRIAHNKTLKGLIALSEGNWWKAQRLLTLSADNADLPLINYLAAARAAQEQGDDDVCDELLQKARASAPEAETAIGIFHAETQLSRGQLEPCLATLLNLRKRSPKHSYVLKLLRKAYIQLEDWQALKALIPELRKQKALKPEKLTKTEQLCFQKLLEQSIALPDGTAAEDKRKALGETWHNMPSQLTNDNVLARHYTTLLVDIGAEAKAEPVLKGLIKSQWDDELVNLYGRIEGGNPKK... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 418
Sequence Mass (Da): 46801
Location Topology: Multi-pass membrane protein
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A0A0C1RR96 | MKVLLSWLREFAPIEGDPYELADHMSDLGMAVEETRPLNPLKGVVVARVASLRPHPEADRIQLVDVEVEPGNPVQVCCGAFNMSEGDLIPFATIGTVMPDGMEIAQRKMRGELSNGMCCSAAELHLGADHDGIMILPQELQVGASLMEQLGLVGDVLWDLEINPNRPDAMSVAGVARDLAARLNVPFEIPDWSVPVVEAREADLVSIHVEDEELCPRFTARVIRGVTVEKSPLWMQMRLTLLGMRPINSVVDVSNYVMLELGTPNHTYDLSLVPNGHIGVRRATDGEKISTLDDQERTLLSGDGIIVNEESAPIGIAGVM... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 792
Sequence Mass (Da): 86023
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A0A8J4PP03 | MTHHNEHHHHEDKHDPRKSFRIEDTFVPGGNGERIMIATQKELDENNIPLNYRDYCSHLLIELNKCRLAGFFLPWECSGLKHAYEQCQAAEYFFRQHKKQVRDYSIKEENKKKAEEKKN | 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.
... |
A0A0A7GF18 | MFGALARYVLSGLIQNGRYFPAGTLGVNVIGSFFLGFFMFSSEYFGLFSQEVRAFIAIGFLGSFTTMSTFSYESFRLLSEGNLIYFLANVLLNVAGCIAAVYAGRAFALALWRMVM | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 116
Sequence Mass (Da): 12785
Location Topology: Multi-pass membrane protein
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A0A7X8XPD9 | MDLEWSLRRGQLARQGACPGASLLLRASGFQAVLLAAFGGPESPEEVMPFLERVVVGRKILPSRLEEVATHYHHCGGRSPVNDHNRALEVELAGVGLDWPVYLGNRNWHPYFEETLVRMREDGIGRALALFTTPYGSYPGCRQYLEDLERARATVGEGAPELVRVRSYFDHPGFIQASIERTRQALESLPEVERPGARLVFTAHNLPLAMARTSPYVGQLRLACSLVAEALGRPDWNLVFQSRSGPSGQPWLEPDLLDFLQGLPGTEAVLLSPIGFLSDHVEVLWDLDVEAAELCRGRGLSFRRAATVGVHSSFVRGLRQ... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 357
Sequ... |
A0A9D5GFQ6 | MIVGLTGGIGSGKSTVAAMLAERGACVVDTDAVAREVVAPPSPVLESIRAAFGDGIMAADGTLDRAALARLVFSDEKKLAQLNRLTHPAILKRALATIAMLPKDALVIVVVPLLYESNFERNCHSVIAVTASEDTRRRRLHERDGLTDSDIQARMRAQLDASEYERRGAFILPNDGDREELRLAVDQVWKRLRVGDGHSERALPNAGPPV | 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... |
A0A0A7GET2 | MPVITLYWDELERMVGVDRNTILKKLPMLGCDIERIADDHLDVEFFPNRPDLYSVEGVARALRGFLDIEFGYRDYKVNEGNWKIYVDESVLSVRPRITGCIVRNIHVNEELLRSIIQIQEDLHWTIGRNRRKMAIGIHDLNRVNFPLHYTAVDENFSFVPLDFDRDMSVKEILEAHPKGQEYGFILENSEKYPMIIDAKDEVISFPPVINAEKTRVREGTSGLFIDVTGFDENVDKALRILTAMFADRGGVIESVEIIYPDRVERTPDMTPEKMNVSKREIFSLLGFTLNDDELRLALGRMRYGFEIGDDEVTVTIPPYR... | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 547
Sequence Mass (Da): 63235
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C0KTR7 | MKPQTRNTVARMDPDTFFYNFYNRPILSHRNTVWLCYEVKMKTNDRSRPPLVAKILQGQVYSKPQHHPEMRFLHWFRKWKLHSDQEYEVTWFVSWSPCPVCARNVAEFLTEDGKVTLTIFVARLYYFWIPHYREELRRLCQRRDSPRATMKIMSYGEFQHCWDKFVDNQRLYKPWNKLPKHYTLLHITLGEVLGHLMDPDTFTYNFTNDPSVLGRHQTYLCYEVEHLHSGTWVPLHQHRGFILNEASNNPGFPEGRHAELCLLDLILFWKLDPAQRYRVTCFISWSPCFCCAEKVAEFLQENPHVNLRIFAARIYGYQRG... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-se... |
A0A950MIM0 | MSLELLAQVSQIVGAIVFLIVAVLVWNRFIAPAVKAYTAAKNAELAEAESRREHMRADVAAARGEIETAEADAKMMAERAQLAVQRDRAKAIDDAQHEAERIVRNAEGELDRARMAARD | 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... |
A0A7Y3KPI3 | MRRRWKASICERSPRANYSRRVASKPQVGVLALQGDVEEHLAALERAGARGVAVKNRAALDACAALVIPGGESTTVIRLLDRFALAEPLRERVRAGMPLWGTCMGMIVVACAVAGLDQPTLGLLDVTVRRNAFGRQNDSAEVELAIPVLGEPAYPAIFIRAPWIESAGPTVEVLASYGEHGVMVRQGNVLGTSFHPELTEDPRVHRYFLGMLAP | Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
EC: 4.3.3.6
Catalytic Activity: H2O + L-glutamine =... |
A0A3N2IK40 | MTTFGIEEEFIFLDPRTLTPSDVGAAVHDELLGRARESRFVSHEFLASQIERSSPVFSTAGQAEADLVTFRTRLAAQAERRGVVAAAVGTPFMCAGWPSVTDSERYHQVEAEFRGLVTDHLINGTHVHVAVPSRDAGVAVLNRVRTWLPTLLALTGNSPYWHGADTGFASWRAMHMRRWSSGGCPPPFADADDYDRRLARLVGVAGTYDTRTVWWNARLAEGHPTVEIRVADAQLDAGQALLVAALSRALVVTSLAEAERGDPPPSVDPELLDAGLWHAARDGLGGDLLDPVALELRGSREVVHRLLVHVGDALDAEGDH... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 364
Sequence Mass (Da): 39457
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A0A8J6YJK1 | MTDDLLAHNVPELTVSELSGALRRTVETAFSRVRVRGEISQPKCAASGHWYLRLKDDEAVIDGIIWRGQAAKLPVRPEEGMEVIATGRLTTYPGRSSYQIVIDSLELAGEGALLKLLEDRRKRLAAEGLFDAARKKPLPFLPGVVGVVTSPTGAVIRDILHRITDRFPLRVLLWPVAVQGDGAARAIVAAIEGFNSLDPAGPIPRPDVLIVARGGGSLEDLMAFNEESVVRAAAASQIPLISAVGHETDVTLIDHAADVRAPTPTGAAEIAVPVRAELVARVLGLAERLERSTTRLFGDRRERLEALARGLPRLDRLLEP... | 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... |
A0A7X8XLK7 | MSLLTEALQNVKKHVVEREIGGQIMRLETGEVAKQANGSVVVTVGETVVLVTASANASPREGIDFFPLTVDYEERMYAAGKIPGGWIKREGRHPERTILTSRLIDRPCRPLFPEGFRNDVHIVGLCTSVDGENNPDMLALTGAGAALSLSDIPFDGPVAGVRVGYVDGEFLINPTESQMAESQMNLVVAGTRHNLNMVECGCEELSEEILVNAFEEAHRAIREIIDMIDELVAKGGKPKAEYPVYTPSAELDKLVRRYLHTGLAQAMRILEKQEREAAFDALNMDALKAAIQADAGLNDEERSAALALTEESGAGKDFGS... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
EC: 2.7.7.8
Subcellular Location: Cytoplasm
Sequence Length: 839
Sequence Mass (Da): 92... |
A0A2W5WYY1 | MLNRQRILVTGSTGQLGDEVVRAFGGRKVAALSHDDISIEDARAVDQAMEYHRPQLVVNAAAYHNVPACERAPRAALRVNCTGVENLARACAAGGAAFVTVSTDYVFDGTKGSPYTEADSPHPLNAYGRSKLAGEVVARAACAQTYIVRTSGLFGPLGSRTKGYTFIDRILGQAERGERITVVDDMIFSPSYARHVAAALRNVVDAGAPGTYHVVNGGFCSWYEFAREALEQAGLRADLRPISSAAWTDGVLRPPNSSLDAAALRAAKLPELPHWKQAVADYLSQRKAEREVRA | 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: 294
Sequence Mass (Da): 31613
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A0A9E0Z0N8 | MNLAHNAVRFFLGISRHYSRYGWIWMLALLIVVVLTHHWKLAYNYTNSLPQTLFAIQLGQKDVERGDYVAFYPPKSATAGNEMPFVKKVVCLPGERIRTYGQQIFCEDKPVAVAKKVSLKGEPLQKIQDQVLGEDDYFVLGTHPDSFDSRYSNFGPINRCRFIGKVHPIF | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 170
Sequence Mass (Da): 19511
Location Topology: Single-pass type II membrane protein
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W8FD66 | MPDSAKLTHLNDAGQPAMVDVGAKQPTRRVARARSRVVLGPEIMALMKEGDLPTRKGPVFQTAILAGIMGAKRTSELIPLCHPLGLDNCQVTIEVDGPDAVLIECTATVTGKTGVEMEALTGASVAALTIYDMCKALSHDILIQETRLVSKTGGKQDFHHAG | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diph... |
A0A3D3SVW3 | MTDLHTPTNPEPLSEDLLEVDEASELDQAHYNEELWFEVQPEQTGRRLDAFLAGCLRDHSRSRIQQWIAAGQVSLLNHAVTKGSQAVATGQSYRVRVPKPQAVEAGQPEAMNLAIVFEDDELIVVNKPANLVVHPAAGHWSGTLLNGLLHQWPELQQLPRAGIVHRLDRDTSGLMVVAKTLTSQTSLVRQLQSKSVFRHYLTVCWHRQAAGTGGQTGLMKGKVEAPMGRHPSDRQRMAIVNGERGKPATTHYQVLASGLLETQPVRLLACRLETGRTHQIRVHLQSIGYPIVGDPVYHLGAPRQAKPPIGRQALHAQGLG... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 342
Sequence Mass (Da): 37593
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A0A1G1NDC5 | MSDNFLEKILTHKREQNASKAEYFETLKKKMQHEKFSRYHLFKNAVSRPGQVNLIAEIKRASPSRGMLRQDFDVLKLAKIYVDAGAAALSVLTEEKYFLGKPMYVTSVSEHYSVPVLTKDFIIHEGQIFETFSCGSSAVLLIVAILSDAELKHLLEVAHAMDLDCLVEVHDERELARALKAGAEIIGVNNRDLSTFDIDLKVSERLIPQIPKDKIIVAESGIKTHNEVNLLKDLGAHAVLIGETFMKTPDMAGKIKEVMHG | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 261
Sequence Mass (Da): 29229
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A0A1V5LZM4 | MLERVRTPIGVLAIIFEARPDALPQIAALAIKSGNAALLKGGKEAGQTNALLFALLREALGAYATAFHLFEGREAVEAMLKSKDIDLIIPRGSKELVTYIQKNTQIPVLGHADGICHIYIDDTYENSSEEALAIVLDAKLTYPAACNSLECLLLDKKLSAAFKLKLCQELVANQVELRLTPSLYQLLESQSFFQPSLCKRALASDFGYEFGAAILAVEEVDGLDAAITHINTFGSGHTDALLSKSPAIFERFFQGVDSASVYHNCSTRFADGFRYGFGAEVGISTGRMPPRGPVGVEGLLTYKYRLRGAGHITAPYGKSK... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
EC: 1.2.1.41
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequence Length: 330
Sequence Mass (Da): 35823
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A0A932W791 | MSNRFDFVETKISGLYVLNRLVNRDARGQFQRLFCSDELRACGWSDPIVQVNQTHTKTMGSIRGMHMQLAPYSEFKIVTCTRGKVFDVVLDLRPGSATFLTWVGEVLSAEDANGLVIPPGCAHGFQTLCDEVEMVYCHDRPYAPMHEFGVHAFDSRAKISWPIEVTEMSLKDSSFPFLDEGFNGVDYARTA | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 191
Sequence Mass (Da): 21510
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A0A2T5BXU5 | MSVELNMEFIIKLQDLIETESSAEVLAMLEGLHPTDIAEIMDKLTMDEAKYLYLQLDGEMASDVLLEIPENMRRRFLRVLPPEVIAHQFVEHMDSDDAADIMGELEEEVVEAVLSEIDDKEQAGDIADLLEYDEDTAGGLMAKELVKVNENWSVQTCLKEISSQSEEIDEIYYVYVVDNDNILKGVLSLSKLIQKPTHSKVKELSNEDIQSVRTDTSQEEVAQIMEKYDLVVLPVVDQIGRLKGRITIDDVVDVIREETGKDYQMVSGITGDVESTDNVWRLTRVRIPWLLIGTAGGLTGAQVLSSHQDTLNHIPAMAFF... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 453
Sequence Mass (Da): 50331
Location Topology: Multi-pass membrane protein
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A0A950J1X0 | MIGAGRTGEACAEVLSTRGIEVYVTDEQPPAKLERALAAIRSSGGRFVAPDQLGAILSKIDRAILSPGVPVAGALAQKVASAVPLVGEIEVAYELCEAPIIAVTGTKGKSTTTALIAHVLRCAGKSARVGGNIGNPLIREAAAAKRNEWVVAEVSSFQLETIKTFKPHISVLLNVSDDHLDRYASLEEYTRAKYRIFEHQDARDIFIGNLDDRLVHAAHSQIQAQTFWFSVNGSNAQAVAFVDRNAVWYRPPDGRPRKVIERSDIALPGDHNLENVLAAVLAATSAGATLINLAESIPSFEPMDHRLQMIAEVAGVRYVD... | 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-... |
A0A1F9TUR3 | MFYSLLLIIHIAACLLMILVVLLQTGRGAGLMVFGGGGDSLINTPSGSSFMKKFTAGLAITFACTSLLMTLHSSRSGMSSVTSRVAAPAAQPAP | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 94
Sequence Mass (Da): 9648
Location Topology: Multi-pass membrane protein
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A0A973B9N0 | MNGLGSTFVEVSKLSDALDQIDIKNDVLLCPPATLLAGLSQKFSSSKLAFGGQDCHSQASGPYTGDISAEMLRDAGATCVILGHSERRIRYNESSSAIKKKAAAAHRAGLNSIICVGETLDERQKGLAIKTIDSQLTASLPSGCNANNVTVAYEPVWAIGTGLTPSVHDVGGMHTHIRDTLSKKFKNGEKFRLIYGGSVKPENVSWLAGADNVDGVLVGGASIRAKDFLEIIVKCGVVHDDFR | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 25742
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A0A8C7D744 | MEKTEVMTPKSLDDLIKLLHKLFESDKINVEEVQQIMEAYDSNPQEWKKFAMFDPTRYTRNLVDEGNGKFNLILLCWGEGQGSSIHDHTDSHCFMKMLQGELKETLFEWPKNKTQDVGDMVQKSQRILKENQCAYINGKIQGSLVFPQHCVSDNIRRHLFIFFTHIICMYIFYKQPPTSEYLYFQVFDYLKTSCTCYILYKFLMDTV | Cofactor: Binds 1 Fe cation per subunit.
Pathway: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
Function: Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine ... |
A0A212JHH3 | MAAQGLTILEGERAPAMAERTTLRLGGPVMGEAVLTEPAAAALLPGIAKRLGGRLACLGAGSNILAGEGPLDLVLVKNGMAPDISVLGDDGKTATLRASGSARLPVLLGRAAALDLGGLEGLSGIPGSVGGAVAMNAGSYGQCIADSLTALEIVTGEGEVRRFGREAVAFGYRAMDLPEVKGWWMVTAAEFRLTREEAGAVREKSRELLDKKRATQPVTAASAGCVFKNPSPEQPAGKLLDAAGFKGKRLGGMIFSPLHANFLVNEGRGTSTEALELMDMAKQAVFAASGIILEPEVRIWV | 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: 301
Sequence Mass (Da): 31061
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A0A950QB12 | MRPAPKSRRATTCRSASCTTGSPSRRDVEALIDALRGAASVLVLSGSGMSAESGLPTFRGVGGLWRERRVEELASAEGFAANPQLVWTWYNERLAAHRRAQPNAGHHALARLEQALPDFTLATQNVDSLHLRAGSRNVVELHGDLRGARCTRCDARRSLAERGLPLGEIEHECGGRFRPNVVWFGESLPIHAWRTAEAAARRADVILVVGTSAVVYPAAALATGYNKNAFLAEINPEATTISGAARCVLRMPAARALPAIADALA | Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-l... |
A0A950MB34 | MDSAGVGALPDALAYHDAMNANTIGNVAERSGGLHLPNFERLGLGHITQVRGLSAADAPLAAVGRLRERSKGKDTITGHWEMAGVITEVPFPTYPDGFPAEVIERFTAICGKPPLGNVAASGTEIIAELGEEHQRTGRPILYTSADSVFQVAAHEETVPLATLYDWCEKARAMLVPPHEVNRVIARPFVGSPGNYARTPNRRDYAIPPPPTVLDRLEGRGVPVHAVGKICDIYSGHGIASSVRVADNGEAVDRALALADATDHGLVFVNLNDFDTKYGHRRDVRGYAEALARLDARIPELIERIRPGDSLVFTADHGCDP... | Cofactor: Binds 1 or 2 manganese ions.
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 1/3.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
EC: 5.4.2.7
Subcellula... |
A0A7J5BL47 | MTVTSQTGAPAATSAIDLDRIAVTLRSAVEALRKGLPVLVADDEGRENEGDAIISAAMATPEWIGWMIRHTSGYLCAPMTEELADRLDLPPMVAHNQDPKRTAYTVTVDAAEGVTTGISATDRCRTLNVLADPASTADSVLRPGHIVPLRARDGGVLVRGGHTESGVDLMHLAGLPAVAAIGEMVHDDGEMMRFPDLVLIGAEYGLPVLTVAQIAAWRRAHPENAPMSGLAAPGATPSIADQQNMIQHEREQVQA | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
E... |
A0A1V5MD12 | MSEPNASANGDLKIILASSSPRRIQLLQNLSLQFEIKPADIDETVPPGLSPPQIVCELARQKGEKILSTLSLSQLGRYLIIAADTLVARDDQVLGKPIDRQDAVKMLMSLSNRSHSVYTGVHLILTAHNLGEPHQSRTFFGDTKVVVRSLQLKEVEAYVATGEPDDKAGAYALQGIGAFLIDHIEGCPANVIGLPVPLLVKELRDMGLRVMGL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A5D0RK14 | MSHIVIDGGIPLKGKLRASGSKNAALPILAATVLIDEKVTLKNVPDLKDVHTMLSILQHVGKQVTFYNNTVTVDSGKLLIGSIPYELVGKMRASFNLLGPLTVACGWAKVGKPGGCNIGQRPVDYHIDGLKAMGFNIFEEHGDIHSKMIDNSAKKISYKLPFPSVGTTEQLITSAAFLPGMELELTNVAREPEIEDLQNFLNSTGAKITGAGTDKITVIGSHNQSGTEYEIIPDRIEACTYLLAGVVTRGEVTVEGSFAKYSEALLKKLEEMGVDVQANEKSVGVSTKDKIKPLKISAKPYPGFPTDLQPITTAVLCTAE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 2.5.1.7
Subcellular Location: Cytoplas... |
A0A8S0U8W3 | SFNFYFLQFCSSKVLSKFKLVPHTSSKIEMEDKESTESGSPGGKSESESPPITSGGDTVGGAAPGGDTVSCGGGVALQAMNMSIERSVGVIDAPAITVGGILGVGGGSGSGGGKKRGRPRKYDSDGNLRVPLVGSPPGGVILPPAPSVGFTLSPNPASKYSSGSKKGRGRPTGSGNWQILASLGELFTTTAGGDFTPHMITVYTGEDVAGKIITFAQKGPRGICVLSANGSVSNVTIRQPGSSGGILTYEA | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 251
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 25257
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A0A962F1U1 | MPASSALVLFSGGQDSTVCLADALTTYDRVETVAFAYGQRHDIELKTRVELLQQLKDCFPQWSARLGQDHQLDLPTLGRISETSLTRSVAIEIAESGLPNTFVPGRNLLFFTYAAALGYRRGITTLVGGMCETDFSGYPDCRNDTLQTLAAALSMGMDKAFEIVTPLMYVDKAGTWEMAQQIGGDKLVSLIINATHTCYLGERNKRHAWGVGCGTCPACELRSKGWEKWQRMKLPTPN | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
EC: 6.3.4.20
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguani... |
A0A967AE04 | MNIAIDVGNTRVKLGVFSAENKYVNAVLKEEVEDELNFIFSKYDSIYKSIVSASGKIDQKWINLLKEKTQLHVFSPSSKVPFISNYTTPKTLGLDRKALVAAASVDFPLQNVLVIDLGTCITYDFIDSKNCYHGGAISPGIKMRFQSMNNFTENLPLIKKDAKAHRFKSIGNSTENALSIGVFEGIIYEIQGFVRQYRRQFHDLTVILCGGDANLLAGRLKNSIFANSNFQLKGLNHILEQNTN | 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... |
A0A8C6F953 | ADDRKVAVPKDGPSVVSWVPEEGEKLDQEGKDQVKERGQWSNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFFPYFIFFFTCGIPVFFLEVALGQYTSQGSVTAWRKICPLLQGIGLASVVIEAYLNVYYIIILSWALFYLFSSFTPELPWTACTHSWNTEHCMDFLNRSAAGAAAPPVNFTSPVMEFWERRVLGISAGIHDLGALRWELALCLLLAWVVCYFCIWKGVKSTGKVVYFTATFPYLMLVILLIRGITLPGAYEGIIYYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDS... | Function: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation.
Subcellular Location: Membrane
Sequence Length: 615
Sequence Mass (Da): 68940
Location Topology: Multi-pass membrane prot... |
W7URF2 | MDIRITPSVLRGRLDVPASKSCAHRSIICAALAEGVSHLSGVTMSKDIEATIGAMTALGAEFTVNGEDITVRGAGGMKTGKCAVDCNESGSTLRFIIPVASVLCSETEFSGRGRLPQRPIDIFIRELGKNGAAFDYNNTMPFTVYGGLKSGIFEIEGDVSSQFITGLLFALPLLEGDSEIVLTSHLESRPYVDITIDTLRRFGVYAEETERGFRVKGGQKYLPHDEKIEGDYSQAAFFCVANALGSQVELHNLNENSVQGDKKILEIIRNMCYNGNIGHYNADCSDIPDLVPVLAVLGAFGSGDSVIYNAKRLKIKESDR... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A1V5M656 | MCSVLDYALVFDKRKERAVKVSGKLFIIATPIGNLSDISTRMESSLKECDLLFVEDTRVSIKLLNHLSLSIPMLSCHKHNERERLQALEKVAAEGRNAGLMSDAGMPLISDPGDPLVRRAIELGMTVIPVAGPCAFVMALVGSGFDLSSFVFEGFLPDGNAPLRQKLNQLKGERRTLAFYVSPHKLKHTLEMMREVIGNRRACLARELTKFYEEFLRGDLSRLIEICDERELKGEMVLVLEGDQAVEKDMSEWLSKPSLHDEVMEHVRGGLSQGLKLSKACQLTAQYFSIVKADIYKEAVRLFRDQV | 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: 307
Sequence Mas... |
A0A2T0XKN7 | MARAWHAAKNSWRGLVFAFNEESAFRQELTLALVLSPIAIWAPVTGLDRALMFATLLLVLVVELLNSSVEAAIDRISFEQHDLSKRAKDFGSAAVFLALLLALVIWATILTPVVTTLLI | Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosp... |
A0A1Y3SD00 | MLSKHTGEQEEMAMIRGIGIDTVVIGDVEGLLKRMSKGTLSKVFTQGELSAAQEKAGPAEYLASRFAVKEAAFKAIAPRLADKGFDYRRIETRNNEDGSPYIYVDSFLQAILDCAEITSLFVSITTTGGMATAFVVAES | 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: 139
Sequence Mass (Da): 15033
|
A0A7C6DFK4 | MKNLVLQNNKKKLNQLIKKMHPYDILDELNTFTEDEKTRFYEMLDEKEVARIVAYLEPEDAASVIDNFELDSQQEIIDHMDLDDAADIFVHLENQDALIDTEENKDIKEILTYDEDEVGAHMSDAYITLPIDLDVKQATKKVIKEAGDIEDINHLYVIDENNQYAGVVELKTLIKAKEPLTVQDLIQQQPYVFVDDDIEDAVHKIQNYGLYAIAVLNRTFEIKGILTVDDAIEIYHEEALEDYEKLAALPDTQTKGFFKSAIKRLPWLLMLLVLSIPIALATSSFEEVIASVAVLALFQPLILDAGGDVATQTLAVTLRI... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 433
Sequence Mass (Da): 48215
Location Topology: Multi-pass membrane protein
|
A0A0B7K3Y8 | MSGESDAYRADGMLFSVWAGHCHTSLVIGAEPLCIILEHMVQKLDGEQRANRAGQRLRYEMSWLPRINLTPQRLYDIDGITIDRPLGEEGCTKDFVDSSSEVSSAVFTSEPLSEPDHVEEASVLQECNSLKTGESQHAPTDPRNSWAKLRAIHREAFSEFLATGVAVFLGLSGTLTVSLSLDSPVHYGTYETSCWSWGFAWMFGIYLGGGVSGAHMNPAISISLSLFRGFPWNRCAIYVAAQFLAGLAAGGLAYGLFADSLHHIDPELTSVSASFFSTPQPWVSRGSAILNQVVASAIMSMAVLSLGDDRNNPPAHGMSA... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 434
Sequence Mass (Da): 47091
Location Topology: Multi-pass membrane protein
|
A0A6H2BEY3 | MTMPHTENLEFMTPTIVSKKNTAKKNTAKKAPAKKTPAPKAPALPAKKLIPRDVSWLAFNARVLQEAADTSVPLRERIRFLGIFSNNLDEFFRVRVATLKRMMSINKVHKMHLEENPGKILDDIQAIVIDQQREFDRIWKDIANELETMHIFLRTEKHLNREQQKFVLNYFNEQVRTNIIPLMIESIQQFPILRDKSIYLGVVLARQDNSVRQKFALIEIPSNVLPRFIILPSKPGEHDIILLEDLIRFCLPHIFSYFGYDKFSSHIIKVTRDAELDIDNDISDSLIHQIEKGLKDRRKGKPVRFVYDKDIDPLLLEYLI... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A969G7W8 | MVFKVLGIILLITAGILAFVRSQGLNKLSSLAKARPTNAGEIKDTVAAIAEEIGQGNWRDYVQVWGDITCGEPLISPLAEERCVYYEMKVTHEYDQTITKQDSDGKTIRTTESRSDIISQNQRSIPFELRDQTGTVLVNPEHADIAKIKSMDEFRPGLSTEGLIRMGTFSLALGNTMINPIGDRRTKGYRYQEWIFPIGRKALVVGQISDETGTPTLTQPTAKENKYLISLNTKEELLAKESRTVKNTTTAAIFTGALGLILLVIGFL | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 268
Sequence Mass (Da): 29625
Location Topology: Multi-... |
A0A3R7T028 | MFINNFDPVAFEILTFSIRWYSLSYISGIILGWFLCKKVFIEDAKLSEKFDNFITYLIIGIIIGGRLGYVFFYNFKYYKNNIIDIFKVWEGGMSFHGGLIGIILVSIFFAKQNRESSFLYMDLVALVAPIGIFFGRIANFINSELYGLPTSVPWAVIFIKIDNLSRHPSQLYEAITEGIILFFILLHFRNKNYLKKPGLISSIFLIFYSAFRFIIEFYRSPDEQLGYLFFNLTMGQIISVLFIIIGIVLFYSKNESKQLK | 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,... |
A0A7D4TIN8 | MSWLYEPNNSFDLDEDDVRIRPNPKGSKPRTKRRPNFDDAPLGMVTEVHLARYQVLMENGQTVTATLAKELRRQGCVTCDQVRLDGVVTAEKGTLARIVKIEPRSSELTRSSDESDSADQTIVANADQLVIVMAAANPEPRPRLVDRYLVAAFNAGLKPILVMTKCDLADPGDFLKAFEGFDLRIFKHSSENPKLEQLITWLEGHKSVFVGHSGVGKTSLINLLAPNYERATGSVNEVTGKGKHTSSSAKAIPAAGGWIIDTPGVRTFGLAGINSQGILKGFADLAEGAKSCPRDCSHLESAPDCELDAQLQRGELSAQR... | 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... |
A0A401T2L3 | MALIPSQVLRVAILLSYLSILCNFKALDIPAHQTYGGSWKFLTFIDLVIQTVFFGICVLTDLSSLLTQGTDDREQQRQLRKLIFLRDWLMAVLAFPVGVMVVAMFWALYLYDRELVYPKILDSFIPPWINHGMHTTVLPFILIEMRTTHYHYPNRKSGQAAVSIFSTGYILWICWIHHITGMWVYPFLDHLSNILKAVVFVASLVVINVLYVVGEMLNSFIWDESRCIEEKVDSKNKMD | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 239
Sequence Mass (Da): 27653
Location Topology: Multi-pass membrane protein
|
A0A925SHW1 | MLSRPFSAFVNHLLAQAAWARESLAEHTGKVALFDMFPVRVAVSVDSDGTLRPAPADASPAVVIRLTHATVLQILSEGEDAWRKVNVDGDTGFASAISKVASNLRWDVEEDLSKVFGDIAAHRMAEAGRTAGAWPRQAAASLAGSVAEFLTEEKHLLVTPLRAAEFVRDVDDLRDAVERLEKRIERLQQQVHGG | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A956QLN0 | MTKERFARLHKALSQRQPDLTVLLDGVHKAWNLSAVFRTAEAVGLFEVHAVFDQDIEPELSKAHSSGVAQWVGLRPHRQTEKAIEELKTEGFQVVGVDLTPDAIDFRAYDYSQPTALVMGAEKFGLTPTARRLVDRSLVIPMMGLGVSLNVSVAAAIVLYEAQRQRVEAGLYRQSRLSTEVFQRILFEWAYPEVTVFCKKEGLPYPIINEEGEIPDRVGGLSLAEVRAQVRQQEQKPGRPGNDRRGTKGFSGG | Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
EC: 2.1.1.34
Catalytic Activity: guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 253
Sequence Mass (Da): 28187
|
A0A9D5GPS0 | DRRARGLPLGNIASVASCFVSRVDTAADKRIENAMKSADAATRTRLQALLGKTAIANAKLLYRCYQRSIAGPRFQKLEASGARRQRPLWASTSTKNPQYPDTYYVEALVGPDTVDTMPPATIDAFRDHGKVSDTLVSDVEGADETVRALESAGISLKSITDQLLADCLIAFEE | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A9D5GAL5 | DATNEAFREWAACSDETFYVIGSVVGTHPYPYMVREFQKVIGVEARAQMLERYGRLPSDVVACVGGGSNALGIFAAFAADPDVRLWGVEAAGLGLEASDTAASLGAGSVGILHGSRSYLLQTPEGQVRNTHSISAGLDYPGVGPEHAYLKECGRAEYVAVTDDQALAAFHRCAAREGIVPALESAHALAFAQSLAGERGAGGCVLVNLSGRGDKDVGQVRQRPRNGMETRASR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 233
Sequence Mass (Da): 24510
|
A0A8C7GMT6 | DQLLHSSFELGNKVPFCPMVGSEVCSSEIKKTEVLMENSRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTGKGTKQLKLDPSIYDSLQKERVEAGDVIYIEANSGAVKRQGQCDTFATEFDLEAEEYVPLPKGDVHKKNEIIQDITLHDLDIANARPQGGQDILSMMGQLMKPKRTEITDKLRAEINKVVNRYIDQGVAELVPGVLFVDEVHMLDIECFTYLKLLLPCRSTCVVTGCVTENRVCVI | Function: Proposed core component of the chromatin remodeling Ino80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 262
Sequence Mass (D... |
A0A7Y3P3W3 | MAKEELALLETSYPDAVTALIYRNPFELLVAVILSAQCTDARVNLTTPALFAAYPNPKALASARLPDVERLIQSCGFFRTKAKNIVAAARALSERHAGRVPETREELEALPGVGRKTASVVLSVAFGEAAFAVDTHVFRVAHRLGLTTGTTPLAVERDVTALLPEAQWRHAHHWLILHGRAICKAPTPLCERCPVRSLCPSAPIVAKTKAARANRGAAGAGARRRVRSISKASKA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A8H7NLW5 | MLLSAALVALTATVVGAVPTLEIKGSDFVVPKDGTKFEIVGMAYQPGGSSGYDPAHGKDPLSNADVCLRDAALMQVLGVNAIRVYNVNPDINHDECASIFNAAGMYMMIDVNSPRVGEAISSFEPWTTYYAAYLNRTFAVVEAFANYPNTLLFFSGNEIINDIESAKEVPPYMRAVTRDLKNYIKNNIKRQIPVGYSAADVREVLWDTYNYVTCAIDGKEDDVSRADLFALNSYSWCGKDATFKSSTFDKLVDGLKESPVPTFFSEYGCIETKERWWNETKSIYGPDMYDTFSGGVVYEWTLEENGYGLVKIEDSQTTLQ... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
EC: 2.4.1.-
Subcellular Locatio... |
A0A8I3W023 | MGFSLNFTLPANTTSSPVTGGKETDCGPSLGLAAGIPSLVATALLVALLLTLIHRRRSSIEDMEESDRPCEISEIDDNPKMSENPRRSPTHERNTTGAQEAHIYVKTVAGSEEPPLDLTSMEVLPRSAWCKLGYK | Function: Central nervous system-specific myelin protein that increase myelin genes expression during oligodendrocyte differentiation. Promotes oligodendrocyte terminal differentiation.
Subcellular Location: Cell membrane
Sequence Length: 135
Sequence Mass (Da): 14596
Location Topology: Single-pass type I membrane prot... |
A0A5D0MJ62 | MKKYLKLPVALLIITFISGFLLSYANKITEPKIQKLQEEKEQKARKKVLPDASKFEAKKLGIQSKFIDNEYWIGYDKNNNIVGFVAKVFKNGYSSRINIMVGVLPSKKIQSISILKQAETPGLGAKCEQNWFQEQFDKLKAGSIEVLKSDVPEDKNAIKAITAATITSKAVTDGINNGINILFNNISNKVENSDTKEKGDK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 22443
Location Topology: Single-pass membrane protein
|
A0A2M7FBI4 | MGAMIVLKAIVLGIVEGITEFLPISSTGHLIVFSSLLNYPEASRETFEIFIQLGAILAVACHFAKPLHGLIRSASNETRAQALIAKVFLAFLPAAAVGLLFHKTIEAHLFRPMVVAASLVGGGIIILIVERRQRRFEVQTIESMGWRHALWVGVSQVLSLIPGVSRAGATIIGGMLAGMNRPSATQFSFYLSLPTMFAASLYSLFKARHLLSVSDALPFGVGFVAAFISALLVVRAFVTFVQRHDFTGFGYYRIAAGLVIALFFH | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 265
Sequence... |
A0A142XLS0 | MVPLTWHFRDRTLHIGPRPLVMGIVNVTPDSFSDGGNFRDTAAATAHALRLVAEGADILDIGGESTRPGAEPVSLADELRRVVPVVTELVARTSVPISVDTMKAEVALACLEAGAAIVNDVSGFRDPAMIEIAKMFRAGAVVMHMRGDPTTMQLNPQYTDVVSEVTDYLQERLRVLGESGIPPEAVCLDPGIGFGKTLDHNLELLANLNSLAGLGRPVCLGVSRKGFIGKLCGRELAARDPGSLAIASFAAARGTAHVLRVHDVAGARDAAILLEAIDQHRR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A949MTS7 | MIDFTTTILAFVVAIGVLVVIHEFGHYWVARRCGVKVLRFSVGFGKRLFSWRHGPDQTEFAVCALPLGGYVRMLDERDETQQVPANEAHRAFNRQTVGKRFLIVLAGPVANFLLAILLYTSLNLAGVLEPAARLAPPPAGTIAAAAGLGGGETVVGIRDRDGSVTPVRSWDDLRWQLLDPIVSAGSITLVAGGNQAGRDYRLNLAGSHIGADDDFMRRLGLQPATQIFVSDVMPDESGAQAGLLAGDQVIAIDGQPLYSAATLVSAVHADAGRAVQLTVLRNGKTQTLAVTPRAQRDSKGNLEGKIGVVLVNRMHTVEVR... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 358
Sequence Mass (Da): 38493
Location Topology: Multi-pass membrane protein
|
A0A8H7KCA2 | MNSPAPPPAGTHPPSTPSQKPMTPLSRSNSSFFEELPMTSKPRSASRQSMRTESPAPPMSPPKGPPMSTPPLGQHPSLAPAAPLHPSEPTPQPSGIASLVAPEKTNPYASLQHPSQAAPPPANQASRYSPAPAHNAHMAGVPPAVGSRYSPAPPVPRQVSGYSPTRVVSGASPALTHLPRTSSPLAHFETSTEGGHIRERRLSSSSYEPRLNRMPSLPPTREVDEEDDQSVAGVSLGINQEPRNSSVPPTSRQTPPPSASRAGSATLSPPRHSSSNYVPGLLIPGLSLPETVNSISRWCFLCTNARSRFSPPMHSASESK... | Function: Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 598
Sequence Mass (Da): 64143
Lo... |
A0A7Y3JEE4 | MFRFFQRKPAAPESAQAHAQQAQSAAPVAIPVAAVEGPPSAPMGGRGVVRPDDAVRPDADQPAHESIGPVHGDAGTEAAAGWFSRLRQGLRKTGSGLSVLFGGSRVDEALYEELETALILADAGMPATQFVLEQLRKKVRAARAETPQQVRELLRDVLAELLVPLEKPLDIGKSTPTVMMMVGVNGAGKTTSIGKLTRHLQQAGCKVLLAAGDTFRAAAREQLTAWGERNAVQVIAQQGGDPAAVAFDAVSAGRARGMDVVIVDTAGRLPTQLHLMDELKKVKRVIGKAMDGAPHEALLVIDATNGQNALAQLRAFDDTL... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A401RYY2 | MVISCWGALIRKLLMMKPKVVFVLGGPGAGKGTQCVKIVQKYGYTHLSAGDLLRSEQSKEGTQYGELIGSYIKEGKIVPVEITIKLIKKAMDEKMAQDAAKNTFLIDGFPRNTDNLNGWNKQMNDHADVKFVLFFDCSNEVCIQRCLERGKDSGRTDDNVQSLLKRIQTYMQSTKPIIDQYEKEGKVRRVDGAKSVDEVFVDVQKIFDSEN | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase... |
A0A542W6L0 | MTAAVTRHAPGKLFVVGEYAVLEPGHPAVLVAVDRHVGVTVSAADGAEVVIESDLSPRGARLRRGAAGLVADADDEPRVLGRLGHVVSAIDVVDGLLAERGRRAPPIRVSVTSRLHRDGTKFGLGSSGAVTVATVTAVAAYYGMELSPDARFRLALLATARRDPRSSGGDLAASVWGGWVAYRAPDRAAVLALARRGGLEHALREPWPGFSVRRLPPPRGLALEVGWTGEPASTASLTGRLETGQWRGSTAQREFVRRSDACVEAAIRALERGDDDELLHRIRGARRMLADLDGAVRLGIFTPVLTALCDVAEGVGGAAK... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequ... |
A0A8I4A1S2 | LSYSMKGGENGNPGIQVYSFYREISYSYKTWSSKIMHRSPRWEDPLRLIFVFLVETYPDNTWVMVSQNLGDRHPKLYTPGTCPARDPDMFHPPPGPTLPSSRSWDGRPLLGRLSGQPWWHKPSEAIMVGLSASFFNSFLKIIFWPKIKMGVCAWFQLTLKTEKKHMVNPYRHIPRTHG | Function: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Subcellular Location: Membrane
Sequence Length: 178
Sequence Mass (Da): 20670
Location Topology: Multi-pass membrane protein
|
A0A8S0PNL9 | MARRNLSSCFLFIILCVQLKISSSQLSSNYYSTSCPKALLTINAAITKALFKERRMGASLLRLHFHDCFVNGCDASVLLDDTASFTGEKTAGPNNNSLRGFDVIDTIKSQLETLCPKVVSCADILAVAARDSIVSLGGPSWVVQLGRRDSTTASLSAANSEIPSPLMDLSDLISAFSNKGFTSEEMVTLSGAHTIGQARCMAFRDRVYNESTILSSFATSLKTNCPNTGGDDNLSPLDAASPFSFDNAYFRNLVNNKGLLHSDQQLFSGASTDSQVTTYSTNPASFRADFASAMIKMGSLSPLTGNDVVFFIIFMLFIGS... | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 492
Sequence Mass (Da): 52484
|
A0A5D0MKS1 | MKMLIVNDDGIYSDGIFYLWKKLKNIHDIEIVAPLHEQSAASHSITLFQPFRFTKVKRKNEFSGWAVEGTPADSVKIALSYLFKDIKFDCIISGINKGFNTSNNILYSGTVSAATEGYLAGIPSIAISTSFEGDYLDEIAEFVKKFLEGWKESDFFESSVLLNINYPNEKKENIKGIKITNQGKSFYKTRLEKRKDPMGKNYYWYSGDLKIDENSNSDDRAIYEKYISITPLKFDLTDYDSLTKMKREKDDLWKKLKY | 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: 258
Sequence Mass (Da): 29765
|
G8ZV97 | MGQMDNKKALECESLPLEKGPYRTYQPVNSYWHNDLGRLKLHDVLVSITITVAFIAYMVRFHASEFTSNPSEAENEILIAIEYYKLGKFRLVALPPFGIQLLSLVPLNKEILRQLSLTFSSLTLAVLYLTLRRVDTYLPFALGCVTAIASLPLYQEESVSVSVDTLQWLLLALSFYSWRTVLCSRIFSKKWFNYMILLSITLGLSASTKFAGTFVCIWIATLAMKGFWSVLGDPKLSVSYLLKYTLFKVLFLGIIPFAIFTSSYALQLGHWSEDSPEFSQYMTPNFKAYLRGPIEQPKFLYYGSIVTLRHVDSLGGYLHS... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 656
Sequence Mass (Da): 75170
Lo... |
A0A8S0U8B4 | MGPTSITRRPSTTGIHCAVMLDTKGPEIRTGFLKGGKPVQLKQGHEITISTDYSIKGDENTICMTYKKLAVGVKPGSVILCADGTISFNVLSCDKVQGLVRCRCENTAVLGQRKNVNLPGVIVDLPTLTEKDKEDILNWGVPNNIDMIALSFVHRGSDLEDVGKSLGEHAKSILLMSKV | 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: 179
Sequence Mass (Da): 19320
|
A0A2W5XZ34 | MELAALAEAAGDVPIGAVLVVGDARFEARNEKESLGDPTAHAELLVIRQAAQRLGTWRLSNSTIYVSKEPCVMCAGAMVAARVDRVVFGCPDPKGGAAGSVLNILAHPALNHRVEITAGVLQEETAAQLQAFFRAKRSAKEDSA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 144
Sequence Mass (Da): 15150
|
A0A976HLU9 | MKLEPPLKISVTNSRKSSKTLLLTGFEPFGDDPGALSLNPSTAIAQALHGTKIGNWRIAGHVLPCEYGGSVRVLKTLMREYAPQVILCLGQAGGRSAISIERIAVNWDEAALVDNAGILRTGQPILKTAPAAYFSSLPIHAMRDALLSKGLPAEISSTAGHFVCNHVFFSLMHSLRGRKTPAGFVHVPYLPEQAAQAGSNVPAMSLPQMLDGIKLAIKSI | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
EC: 3.4.19.3
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 23430
|
M8E5N8 | MTAFGASLSYLAGVLAGAYLSIAWLFLFAGLLAAVCVFIPKEAGKKLSLVSLICIGSGFYFHAYDSMHQSYLRVPAAEESLIHFRGEIATPVKRDGDSARFILLVESVGVSREQMEDLPGAERIAFRVGLEQEQEAMAIEQWLPGDRIAGKMLLSLPAGARNPHAFDYARYLRWQGVYVTGEAEYGELVRGAARTGVMRLFHQWQNDAKERLDRVFRDDETSGYMSSLLLGVTDGVSPETQEMYANLGISHVLAISGLHVTLVSGMFLWGIERLGVPRKTALVCTIGMLAGYVLLVGASASAVRAGIMGGIGLLYQAMSR... | Function: Counteracts the endogenous Pycsar antiviral defense system. Phosphodiesterase that enables metal-dependent hydrolysis of host cyclic nucleotide Pycsar defense signals such as cCMP and cUMP.
Catalytic Activity: 3',5'-cyclic CMP + H2O = CMP + H(+)
Subcellular Location: Membrane
Sequence Length: 794
Sequence Mas... |
A0A8S0VMB6 | MAATLKAGFFFQTKPGGHSLPRIKPFRFKPPMATLATVPTVGLSETFSKLKRQGKVAFIPYITAGDPDLSTTAQALKVLDSCGSDIIELGVPYSDPLADGPVIQAAATRSLAKGINFDKIIAMLKDVIPQLSCPIALFSYYNPILKRGIETFMTTLKDAGIHGLVVPDVPLEETEILRKEAVNNNVELVGVPN | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 193
Sequence Mass (Da): 20752
|
A0A6J1WGH0 | DNIYVFFSEVLRLWPPAIATDRICNKDYNLGKANNKSTEDYIIRKGEGVTIPTWTIHRDPKFFPNPTKFDPERFSEENKRNIHPFSYMPFGLGPRNCIGSRFALCEVKVMLYQLLQHMKVTPCEKTCIPTKLSTESFNVRIKGGHWIRLKIRS | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 153
Sequence Mass (Da): 17867
Location Topology: Peripheral membrane protein
|
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