ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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E1BL96 | MVTENHSTVTEFILQGLTERPELQLPLLFLFLGIYLVTMIGNLGMITLICLNAQLHTPMYYFLSNLSFVDLCYSSVITPKMLVNFVSGKNIISYAGCMAQLYFFLVFVIAECYMLTVMAYDRYVAICRPLFYNIIMSHRVCSLLMVGVYAMGFIGSTIETGLMLKQSYCEGLISYYFCEILPMMKLTCSSTYHVEMTVFLLAGFNIIVTSLTVLISYAFILSSILHISTTGGRAKAFSTCSSHLAAVGMFYGTTAFMYLKPSTASSLAQENVASVFYTTVIPMLNPLIYSLRNKEVKAAMQKTLRGKQF | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 309
Sequence Mass (Da): 34586
Location Topology: Multi-pass membrane protein
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A0A9E1I0P8 | MIALIFTSFLYVIAGHLLMTGISDDKSKPTEKRKGLYILLATGIVVRYIGATIYPGYISDMNCFKGWSDMMYKLGPGGFYTSEKFTDYPPVYMYVLWLIGAIRNLIPMSAMATNLIIKTPAIICDVVISALLFRLANRKIGEKAGYFAAVLWLFNPAVFINSSLWGQVDSVFMLLVLLTLMLVMEKRLVPSFFIFAVSVMLKLQALFYTPILLLAIVEETIYPQFKPKELLRYIGFGVLAILFALAICVPFGLSNVIEQCIGTLSSYQYGSVNAYNMWSALGFNWAKLSPAMSFIGTALIVAVVIAAVVFFFRMESESKY... | 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... |
A0A2I7SPR5 | MGFKKFTAFAVVSTMVFTLATANASAAPGEQPPQAKPEKKAALERLSKNSKGKEKVTWNKEKGAATFVAGKLSDKQAKTPADVKRIIEENKALFNLGSANSELSLISQEKDSLGFTMYKYQQVYQGVPVFGNELIVHTDKNGTTTSINGYYDPEVKTAGLNTKATLSLAQALNKAKVSEGVANVSKFDIQKGKLHVYETEKGDYRLVYVITLSTLEGKQPVYTDLFVDAHNGAIVHKIDKVNHAAATGTGTGVLGDTKTLNTDSYSSGYYLRDITKPMYSTGGKIETYTANYGTALPGTLLTDADNVWTDRAAVDAHYYA... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 556
Sequence Mass (Da): 60660
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A0A9D1T391 | MERIPIILASASPRRLAILRALGVRAEVRRPHCLEVTLRDDPAGTVGVNARRKALSVRASHPNAAIIAADTVVCFEGRVLGKPRDTEEARAWLTAYAGKTQTVYTAVALLYPGAQEPSLRIEATSLQFKNYDAHTVEAYLALARPLDRAGAYDVNVRGDLLIAGRVGSFTNAMGLPRGVVRDWLASHGLLGAER | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A2J0KYW0 | MDKILTGLDLGSSKLRAAVAKIHQDGYMDLLGVEESPSGGISRGNIIDLGEASSAVENIMYRVKDKYGPKIFKVIISIGGLGFSTDKLNAYIVLQGPPRELTQKDIEKVLQTARNMNFSLDSCILHEVVESYKLDGQDGVKNPVGLFAKKLEVNLYSLLHSLAHIQNVMRCINYAGYDTEKIIFSGLIGAGCIVNEDELENGVIFLDVGCDTTKIVVASDGKIKFCNVLGLGGLDITNHISEKFKIPSASAERLKLDASITEETKGDKKISIIIGGKERTFLRSEVNAAVREKTEDLLTAIKSELDNSLVADSIKSGIVA... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 43991
Location Topology: Peripheral membrane protein
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A0A0R3JWR3 | MAKDYYQILGVDKNASDEDIKKAFRKLALQYHPDRNPGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGQGFEGFGGFGGFEGFGGFGDIFGDIFGDFFGGGRRQRTGPQKGADLEYTLNLSFEEAAFGAKKDVEIFRHETCEVCSGTGAKPGTSTKTCDKCHGTGQIKVERRTPLGSFVSINTCDKCHGEGKIIEHPCNVCGGRGKVRKKKIISVNIPAGVDSGMTIPLRGEGEPGSKGGPAGDLYLHINVRPHKIFKRQGSDIYCTIPVSITKATLGGEILVPTLEGEEKYTLPEGTQPGTVIRLKGKGIPK... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0A8C3ZVM5 | MNSGRHSLNHLIVDDRHGIIYCYVPTVACTNWKHIMIILSQSLFWHRYGRISHHLMRIKLQKYTKFLFVRYPLVHLMSDFRNKFATAHEAFEAGLQPSFANFVQYLLDPETEQDEQFNEHWRKVYRLRHPCQINYDFIGKMETLDEDAQHLLHMPQLDHEIQFPHGPRNRTSERKKDFGYSRLKSLLIECGILIFNFLLLLPVQVLWYGKTT | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 212
Sequence Mass (Da): 25400
Location Topology: Single-pass type II membrane protein
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A0A372BTG2 | MIEAWIGLGANLGDRAATLDAALGRIDRLSDTHLCAVSRYYFTPPWGDTDQPEFLNAAARVRTALTVGELLRGLLGIERDLGRERSKRRWGPRVIDLDLLLYGDQCIEGPELTVPHPRLHERAFVLVPLLELAPDLVIPGRGRADALLGQLDDNERAGIRPGPEAGYLPPNDDAKKR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A2H5VPN0 | MISPARKLAFGILRRVAAQRGHASDLLASPRVDRLPERDRRLAYELVLGVLRWQRQLDHLIAHYSGRSPDRLDEPIRIALRLGLYQLRFLERIPAYAAVNEAVALAKHYGPPWGAGLVNAVLRRAASTPDEHPWERIADPIERAGVELSHPSWLVRKWTADFGAEEALALMRANNQAPPVVIRFNVLAASTEEIARALAREGIEIEPSPYVPGAYRVRSGSLSPNSEARQRGWIYIQEEASQLIAHLVAPEPGMRVLEICAAPGSKTTHMAALMGNEGMIVAGDRHLARLRVLKQLAERLCVRIAYPLVFEGRGPIPLLP... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 447
Sequence Mass (Da): 49833... |
A0A354DLI2 | MSQSIPHGGKLINRINPDYDYSSIHLEIQLDSIALSDLKLIANGGYSPLVGFMGEDDYLQVVQNMRLANGDVWSIPITLPVSEEQAKQLKAGEEVKLVKEGTVYGVLQIKELFAPDKQVEAEKVYRTTDLNHPGVKKLMERGPVYVAGPIIYVEQTTKGVFPTFELDPIETRQVFEERGWRSVVGFQTRNPVHRAHEYIQKAALETVDGLFLNPLVGETKADDIPADLRMKSYQVLLENYYPKDRVHLSVFPAAMRYAGPREAIFHALVRKNYGCTHFIVGRDHAGVGNYYG | Pathway: Sulfur metabolism.
EC: 2.7.7.4
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Length: 292
Sequence Mass (Da): 32864
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A0A2T2QZF6 | MEAVLAKLGKIGFNWKMALFNLINFLILYFILKRYFFDAVLNNIEVREERINQGVEDAKKAETELRMAKRKAQDIIDEAKVDANQIIADAKEDAEAIAKDMKQEAKEEINSLVSQAKRNIARDREEMKENLRRETISLAIEAAEKVVEKEMDKEADEEFIKEILATKTTD | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 170
Sequence Mass (Da): 19625
Location Topology: Single-pass membrane protein
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A0A377ZS91 | MAVIAAIRRHAGPGGMDYLVSLAERMLRRHPKYITFLAPLVTWFMTVLRWHRPIPPSPRCR | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 61
Sequence Mass (Da): 7112
Location Topology: Multi-pass membrane protein
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A0A377XSB7 | MERYETLFAQLKNRQEGAFVPFVTLGDPGPEQSLKIIDALIEGGADALELGIPFSDPLADGPTIQGAALRAFAAGVTPAQCFEMLAAIRQKHPTIPIGLLMYANLVFSPGIDAFYAQCAPRRRRLGAGGRRAGGRVRPVPPGGDAP | 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: 146
Sequence Mass (Da): 15456
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A0A8C0EN92 | MATLGTGLLFGDVSRRFSCEWANAHFRFRQPCSDLAYALEAEKVNVKAQRRASSPQGLSRSRELRRVSGQEQGEALAAALADTLWAAAAGGRGGGGGGRRAVVCLLAAAAHVVPRGDYEADSFTERVSMSTPAANRIFFKDTFGEGSHGVILFLYSLLFSRTLERYISFFKRFPLAVLSLLLTGRAGPHDLDGSRETPQLPVWLCGLAGRHGVLFSTDSQLLSDWKRERVFHLHFYNGQARAAHLTIDTHSHPWEEDPSEGPSSPGKRRPPVEMAIRSKWAGASISWNGTGPFF | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting... |
A0A3Q1N531 | MSARGAGRSTGGGCDEAAALGPAELLATEEGERPGALRQMWRYRSWDVPQIPAEVPQSQKAITKSGLQHLAPPPPAPGAPCSEPERQIRSTVDWSESATYGEHIWFETNVSGDFCYVGEQYCVAKMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQS... | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 862
Sequence Mass (Da): 96411
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A0A3Q1NNL4 | MESRELIKNSEALGAARRPSAPVGTWRCPRCGACRRRSAPSAPCSSRPWALRAGAVRELRTRPALLSVRKFTEKHEWVTTENGVGTVEISNFAQEALGDVVYCSLPEVGTKLNKQEEFGALESVKAASELYSPLSGEVTEINKALAENPGLVNKSCYEDGWLIKMTFSNPSELDELMSEAAYEKYIKYTEE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular Location: Mitochondrion
Sequence Length: 191
Sequence Mass (Da): 21122
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A0A2H5VK99 | MGLLLQTDPIYGYLPILVLFLIAVLFPALVLGIGRLLRPAKPEAPKLSPYECGVDPILDARERFSVRYYIIAMLFLIFDVETVFLFPWAVIYDKLALFGFIEMVVFLGLLIVGYYYAWRKGVLEWT | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
L0DYN5 | MIGVLGGTFDPIHFGHLRPALEVHEQLRLDELRFVPCHVPPHREEPATPARHRLAMVERAVAGVPGFRADRRELDRAGPSYTVDTLRDLRAEIGPQAPLVLIMGMDAFSGLHTWHRWRAIPALAHVVVAHRPGAETPPGTAFRRVADIAPDPEPLRNRPCGLFHFQPVTQLDISATAIRGVLQTGRSARYLLPDSVCAYIDEHGLYPVITRETRSSQEPPDAK | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A507CDQ6 | MESLTKSVSSGALIAVAVALIHDPLLVSLCLSVLAAYWTYHAISLVGGVFVAKGQFGKDLLKPNMPVLPESQGVVAGAVYFAVMFLFIPIPFVQWFAWGSIEHGGGVPTFPHEKLGQFLSGLLALLSMLLLGFADDVLDIRWRVKLWFPMFASIPLLTVYYVTYGVTHIKVPLLFRAFVGTDLVDLGPFYYVYMSFFCVFCTNSVNILAGINGVEGGQSLILALSIVSNDLYQTYTSDNRLTVEAHLTSLFFILPFIGVTIGYLFQNWYPAKVFGGDTYAYFAGMIFAVVGILGHFSQTVLLFHIPQIFNFLYSCPQVFG... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 429
Sequence Mass (Da): 47769
Location Topology: Mu... |
A0A1Q8V3C1 | MSLPSHGANPHYFVQAMGLLLPEHAIDFSENVNPLGIPQVVRDRWNQYIEAITTYPDPHASQLREKLANDLNVSIDQLIVGNGAAELILLIANYFRKKRVLIVEPTFSEYRDACLTYDCEIIRYQLLQESSWDIQVESLLEAINGVDILFLCHPNNPTGTTIERSTLIQVFSRAREKNVTVIIDEAFYDFCTENVSVIPYIEEFHNLVVLRSLTKMYAIPSLRLGYVVARKEFVSELKKFQQPWSVNGMAQQVGLDCISDEEHAIDTKTFIRAERKRMFKLLSDIGYEVSPSVVNFYLLKPKGTNDDLTPLITFLIQNGV... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
EC: 4.1.1.81
Catalytic Activity: H(+) + O-phospho-L-threonine = (R... |
A0A498QIS1 | MSLMLDQQLKEPAHRVTGRSSGARRRQLTSSFIHGLLLLVMIATVGVLVWVLAYVAGQGLKYLGPEFLTQTPPGNPSQPGGGFLNGIIGSLIITGIATLMAVPVGVAAAIYLVEYGGRLAKLARFFTDILVGVPTIVTGALVYAVWVVFFGFSGIAGGIALSLVMLPLVIRSTEEMLRLVPHDLREASLALGVTKARTILSVVLPTASSGIITGVMLAFARAMGETAPLLLTALGNDLFVELNPTQRMSTLSLQIFGNAITGFKAAQARAWAGALTLVVMVLLFTVAARLIASRSSVSRAH | 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: 301
Sequence Mass (Da): 31664
Location Topology: Multi-pass membrane protein
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A0A378H1T1 | MKRNWERAIALKAKVVGINNRDLRDMSIDLNRTRQLASRLGPDVTVISESGIHTYAEVRELSHFANGFLIGSALMEQADLETAVKRVLLGENKVCGLTRPQDAQVAWESGAIYGGLIFVPTSPRAVNDAQAKAVIAAAPLQYVGVFRNAPLEEVVARAQALGLAAVQLHGDEDQAYIDALRDALADNVRIWKALSVGETFPARTFRHVDKYLLDNGQGGSGQRFDWSLLQGQDLRNVMLAGGLGADNCVEAAKSGCAGLDFNSGVESQPGIKDASKLASVFQTLRAY | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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: 287
Sequence Mass (Da): 30963
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A0A7S0BZC5 | VSHNFLHIFSTEFATIHYQRNKMKFSVSALTFSVLAAISADAFSPSAFSGAPMAKVASSSSLKMSLEKYSDELKATAAQMVRPGFGLLACDESTGTVGARLESIGLENIEKNRQEWRQLLFTTPDLGKYISGAILFEETLYQSSTEGTPFVKLLNDNGIIPGIKVDSGLKALTGGGEGETWCSGLDGLYEKCARHYEQGARFAKWRTAVRIDVEKGLPTQLAVQEAAWGLARYARICQEAGLVPIVEPEILIDGVHDVATTAKVQEGLVTTVYKCLQENGVLLEGSLLKPSMTVSGVDCPNKPKPDEVAAMTVQTLQRCI... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 357
Sequence Mass (Da): 38599
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A0A136MUE7 | MKLINIDDVSKSKKKLTVQIEPTDLTVEKEEAYEELGKEAVIPGFRKGKVPRKFLELRFDKAVRKEAFGDAVFKALDDISKDRDLRIIGKPVFDPPEFDDLADKVCEEPVEMGVTIEVIPPFELPQYSQLKLPIELETNVEQMVDSLLEVTRQRSAIFTTVDDRPTCEGDHVVIQCTTTRGGEDFPAITAPRLMVNDLGDSGFPAAFEKGLVNLEKGANFDFDFSIESDHPLFLADGENSCHTRGKILSISEKDIPALDDDFAKDHNFESLAAFRKRLTEDVQHNEDRHLATKKRDTIQNYLLDNTDVVVPSSLIQNDYL... | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 446
Sequence Mass (Da): 50448
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A0A293MUY4 | MNIGFLGAGRIAQALAKGFITAGVCDSSRIIASCPVADRHLLEQIQKLGCRTSHDNRDVIREAETVFLAVKPPDVPQVLSDVSSSVQKHHLVVSLAMGVKIHDIESALPERSRVIRVMPNTPCLVQEGACVFSRGSSATAEDGKVVHRFLSSVGICEEVAAEGMLDAVTGLSGSGPGYVFMMIEALADGAVQQGMPRDMSYRLAAQTLLGSAKMVLETKRHPASLKDDVCSPGGTTIEGVYRLEKLGLRVALMEAVAAGTAKSRQTGQTK | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
Sequence Length: 270
Sequence Mass (Da): 28598
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A0A0G0G6P9 | MKNRAVVASLDKRFNKQKDKIRKASLEILKILNQKSVLVEIYLASGAKMRILNRRFKGKDKPTDILSFPEPRNFPHPGLKLRNLGEIYLYLDYFRKNLVRHDYRYLLTHGILHLLGYDHKKKNDRIKMNKKEQLVIKKL | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 139
Sequence Mass (Da): 16571
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A0A2X3J117 | MVIGPCSIHDPAAAKEYAARLLTLREALKGELEIVMRVYFEKPRTTVGWKGLINDPHMDNSFRINDGLRIARKLLLDINDSGLPAAGEFLDMITPQYVADLMSWGAIGARTTESQVHRELASGLSCPVGFKNGTDGTIKVAIDAINAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPNYSAKHVAEVKIGLAKAGLPAQVMIDFSHANSSKQFKKQMEVGADVCQQIAGGERAIMGVMIESHLVEGNQSLESGEPLTYGKSVTDACIGWEDTETILRQLAEAVKPAAAKLLRASAGHKKSVEISTLFCSHQEK... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
EC: 2.... |
A0A2J0KTJ7 | MDRKEILENIQGVLGNKIKKFYEKSEKRVYIDIEPKDLIETVTFIFKKLGARFSIASAIDRPDGTEIMYHFSFDQYGMIVSFRVFMKERIGVKVDSITPIFIGAEWIEREMHELFGIDFIGHPNLKRLLLPDDWPSDKHPLRKDYKNEFR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 150
Sequence Mass (Da): 17788
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A0A1V6ECK8 | MRLFAALPFPAAAQNQIGTYCASLEESFRPARPSWVPPQNLHLTLHFFGELEAEDAEKLKVLLSDAANICPPLRITTEGLSVLPSMNRPRVLYLATRIEPFEPLTRLINRIRKIAVQLGAETDARPWKAHLTLARLKLPIAPELSSLPKLPKLNLSIDSFELLQSTLSPTGAVYSRISRFAFYTDTSTL | 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: 189
Sequence Mass (Da): 21092
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A0A377WRE1 | MPGRIIGVSKDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIASLYAVFHGPAGLKRIAGRIHRLTDILADGLQKKGLKLRHAHYFDTLCVEVADKAAVLARAEALQINLRSDIHGAVGITLDEATTREDVLNLFRAIVGDDHGLDIDTLDKDVALDSRSIPAAMLRDDAILTHPVFNRYHSENRDDALHARPGA | 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... |
A0A3Q1MCR1 | LDSQTGELLSWIVTQDFAPKGTAGAFQEYDNKYVNVKKGSLARLSTLLAAYKLFNYCHSYKEFKHKWPRKYH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
A0A3Q1LQ48 | MASPALAAALAAAAAAAGPNASGAGDGGSGRVANGSGAPWGPPPGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMAYWYFGQVWCGVYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSLYRRPDGAAYPQCGLNDETWYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTRTLSEKREPAGPDGASPTTENGLGAGENGHCVPARRPRADLEPEDSSAAAERRRRRGALRRGGRRRGAGEGAADAEGT... | Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.
Subcellular Location: Cell membrane
Sequence Length: 461
Sequence Mass (Da): 49829
Location Topology: Multi-pass membrane protein
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A0A293MCK4 | MTSQSVTQTVTKTVPKRVPMQIVWRNVILMGALHLTSIYGFYLIFTEAMWQTILAAYIMYTLSGLGITAGSHRLWAHRSYKAKLPYRIMMMILQSMAFQNDIFDWARDHRVHHKFSETPADPHDATRGFFLGKTIDLSDLLADPVVRFQRKCTWGADLSALRRFDQISAGFGICRMPNGSCLFAFFAHRLSHLHYFLHM | Subcellular Location: Membrane
Sequence Length: 199
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 22963
Location Topology: Multi-pass membrane protein
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A0A2U7NBV3 | RSLQVAAIAAKDNAVAVELAESSRAGVKASSDWVMESMSKGTDSYGVTTGFGATSHRRTKQGGALQKELIRFLNAGIFGNGTESSHTLPHTATRAAMLVRINTLLQGYSGIRFEILEALAKFLNENITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPAGEPLNAEQAFKLAGVNGGFFELQPKEGLALVNGTAVGSGLASIALFEANILAVLSEVMSAVFAEVMNGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSGYVKAAQKLHEMDPLQKPKQDRYALRTSPQWLGPQIEVIR | Pathway: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.
Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Catalyti... |
A0A3Q1MGJ6 | MLCAAVGGRRVGLCPAPVCSPAWGSGPQVTRGPPLDLLPWMQWVLCALWIGGFAEYAAANAAAGRRGEGEVWASLAPAWALPQCFHPIPSAPPLASRAAETRQSHGQEAALLVSPKWSPSFARKPPGTKGVVKTQILPPLQLAGSGLGPGIGMSSITLPPHSSTHGDSDMPAVAGRHPELRVLAEPLPVHWLPVCARPSSSPGAWGGSAAAASWAQVRGAGRPRHGSASTTTPTGSWSAPTRAAWSAARASGTSGCTATPPGATARAPSSSSRKAAGWTTSTATTGAGTPEAGSLESTRAVAGSQPSRVLRSPVMLEGLS... | Catalytic Activity: ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 793
Sequence Mass (Da): 84994
Location Topology: Single-pass type I membrane protein
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A0A486RS83 | MAAWRLTRGNFAPQTATLDVEPQTIPVGKAYDAPRWIPTDRPVKLSELLRKDQSPTVSGVWHEPLRIAFRAAPDLYLWDGETIPLQVGYRFPSESWINEDKSLLSVTLNGTFLNNLPMNKQGPLEKVWRYLGGDARQERFTIPLAPYLIYGDNQLSMYFNVVPKDDVPCSVLLNNNIKSRITDDSWIDLSKTRHFSLLPNLSYFVGASFPFSRLADYSQTTLLLPADPSETQVATLLNLAARSGNATGTALANNRVVLGMPTGGGDLQSLRERDVLAVTALDQQAFNQSLLADSPYRPVDNVLSVREPDLWQKVQRRLTG... | 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: 459
Sequence Mass (Da): 51049
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A0A9D9NDA8 | MKREVFSIRTLFSAAMAAMIVTFVLIIGSLLSTFFAHSMQEAALSSTEEIITQVNSNLDFYISDIIGVSDYARNLARTTSNLAADDIRLRLEALIDSRDDLIRIAAFDMDGRTIVSTESERLWKPEDVVMEQWFRRARDGEGDFFFTGPHTQSLSPSEDLVISYSTVINYGDINRKTSPAVLLIDLNFNAVSNLSENVNLSSSGYIYIISNDGNIVFHPRMGEIGKGNFSEDLESVEEHVYGTYISEFEGRKRLTIIQTVSQTRWRIVGVAFMDELLHPLFFFRLTLVFLMITSIIVATFVSRGISNRLTRPLRILEAEM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 587
Sequence Mass (Da): 66051
Location Topology: Multi-pass membrane protein
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A0A377XF53 | MGLGTDSLPQEAFDGPHNLMMQIFASQGVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKAHSYVIGDRATDLELADNMGITGLRYDRETLDCRPSASS | Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
EC: 3.1.3.82
Catalytic Activity: D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + pho... |
A0A293LWS0 | MLFITRVLCRLILILIHVWMHIFDKLLLIKHRVIHRLRQWPLNVTPLNSVKLEQSASFDRRLSLLKKLPRHLAVVIAEGVISYRDIANLVVWCLFVRVPYVTVYDVEGAVKKNWLQLYEEVLRSQKRHFGYSNPAEVVLHAQQKPEKNGHNGYKRRIHVRLSGPEDGRPLLADATRRICGLFKNGDLAREGLAPDLIQAHISEWPDPDVLLRLGNVHSLLGYQPWELRLTEIISLPTQKEVTLSEFLDVLQTYSSCDQRFGK | 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: 262
Sequence Mass (Da): 30372
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A0A7H9ZBI0 | MATQSEYELEAQLVEQLVGMHYERVNVTDETSMKANLRKQIEIHNRLESSPLTDGEFNRIFLHLTKGNEVIDRAKILRDRYQLLRDDGTEKWLSFINKEEWCQNEFQVASQVKQFNAEQNTRKTRFDVTLLINGLPLVQIELKRRGLGLKEAFNQIDRYHRDAFWVGSGLFQYVQIFIISNGVDTKYYANNRANHFEQTFFWTDEKNNPLKALEKFTDAFLKVCHIAKMITHYTVLNETRKCLMVMRPYQFYACEAMIHHVKDNLHKQGRPENGYIWHTTGSGKTLTSFKASQVIMEMPEVDRVIFVVDRRDLDYQTAKE... | Function: Subunit R is required for both nuclease and ATPase activities, but not for modification.
EC: 3.1.21.3
Catalytic Activity: Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Sequence Length: 672
Sequence Mass (Da): 77485
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A0A136M5B2 | MAAEVAPFAKTGGLADVTASLSKALDQRGHEVAIILPKYLMVDRGGYPTELIDLPLSFRIDNEDRTGWIHRAKFPGASITVYFVANDFYYNRNGIYHDGGRDYPDNLARFTFFCRAVIEFIRSGEFTPDIVHCHDWQTSLVPTYLKTTEKDVQSLSNLKTVFTVHNLAFQGFFPREQFPATGLPWHTFTQEGLEFFGDLNLLKAGFVYSDAITTVSERYAIEMMTPEYGCGMESIVSACRHRLTGILNGVDYEVWNPQNDPMIVSHYSPEDLSGKSRCKAALQEQFGLPVREDVPIFASISRFDDQKGLDLIYHAMEMLL... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 481
Sequence Mass (Da): 54541
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A0A3G3NHU3 | VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLXXXXXXXXXXXXXXXXXXXXXXXXYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A5C6ELY5 | MGTGPFAVPAFEALRLAGHEIALVVTKPMPPVKSRKGPPPSPVRSWAESHSLPVFDPDTINDPAAITRVADLQPWLLVVCDYGHILKPDALATATIGGINLHGSLLPAYRGAAPVQWSLLNGDAETGVSVIHMTPRLDGGPIIATSSTPIRDDETSGDLEERLSQLGVAATMDAVARLIQWDQTTPIGEIQDAARITKAPRLSKADGDIDWGRSAREIDCHIRGMQPWPVAFTHVLVDPEKPPIRLAIKEISITETDSSDRSPGEILAGEGFCVATGDRVIEIKRLQPAGKREMPAGDFLRGHSPPEGSRLFSP | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A2T4U9K3 | MPGPKTVEELPQQSALEHYTALRSMIIRSLSVFGVLFLVTLVFVHQLIPSLIVDDRLVMLGPMDVLGIYFIVAFSIALGLSVPYLAFEIWRFVRPGLTERESKVTLTYIPAVFLCFIIGITFGYMVIFPLAYQFLLGIGNIHFDMMITAREYFHFLLMSTLPIGFIFELPLVIMFLTTLGVLTPEILKKSRRYAYFMLIVISVVITPPDFVSDILLIVPLVALYEIGVVLSKRAHNKREEKELADSA | 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.
Subcellular Location: Cell membrane
Sequence Length: 247
Sequence Mass (Da): 27984
Location Topology: Multi-pass membrane protein... |
A0A921ZBL6 | MESHPTLLKVIFPLLTSIMENPCWSLVELASSVLIEKLLYTCTGIEKVFLLVRELKGLSPDQRMQQFLNNPLFQRLKDEKPKILNKLIPVNGNLSANNLGISEEDAETLIDEVSVVFHAAATVRFNDKMNVPMKVNFGDVHVSTAYAHISHLKDGVREVLYPPPATLDEVEDFITKYNDDEEMTNKYLNGRVNTYTFAKALAEHHVVKNKEHVPVIIVRPAAVTATIDAPTPGWSSNWQGVPRALYNVAMGYSRVTPGRHINVIDFIPVDYVVNLCIIAAAKSGRTNDVPVFNCSSSSVNPITWSKAYKWFTEDVVRRGK... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 442
Sequence Mass (Da): 50468
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A0A1M4TM26 | MRRRKKQTKIWTISDLVAHLRSKIDEDPQLQTLWVKGEITNFTLHERSGHMYFTLKDEQTRVKAAMFSSQNRRLRFRPQNGDSVFALARLSMYEREGQVQLYVQEMQMSGIGDLYTRFVRLKEQLEQEGYFSAPAKPLPRFPRRVGVVTSASGAVIRDIIITMRQRFPLTEILLFPVAVQGTNAANEIAEGIEILTQQGDVDVLIVGRGGGSLEELWAFNERQVADSLFRTTLPVISAVGHETDTTISDYVADHRAATPTAAAAMIVPDQIELREQLRLLQHRLIQAQRRVLDQRLQTLTNWQERLQYSGPKVKIQQYVQ... | 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... |
A0A136N2G5 | MLPVTLREIAQAAEGQLERLDGDCVVASLSTDSRTIQEGDLYWALPGENFDGHDYCREALAKGALGVVIQNNKLPGIEIPCVRVPDTLYALGELARLLRNKTSARVVGITGSVGKTSTKEFIRHAVGRVMKTKATEGNYNNLVGLPKTLMNVEPDDQWLVLELGTDRPGEMKRLVEIAQPQAGVVTAISEAHLERMGSIEGVFREKSELLKGLPPDGKAVIPQGSRFREDLAAVTEAGVITFGTEKGSEYHAVDPTLRTSGCYGFMLETPAGKGEVALQVPGLHQVYAATAAAAAAVSSGLSLESVIEGLQTFSGLPGRC... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A2N5X9Q1 | MGSRGRPRSGHHRVQPRTPDEPRTRPGRAERRRTVRRIRRRRRRGALKEIPLLIGAALLIALVLKTFLIQAFSIPSGSMEQTIRVGDRVVVDKLTPWFGAEPRRGDVVVFRDPGRWLKEQPEEDAPPGIKQLKQFFTFVGLLPSADEQDLIKRVIAVGGDTVACCDAKGRVTVNGTPLDEPYVKPGNEPSHLEFDVKVPAGRLWVMGDHRANSSDSRYHQDGPGGGTVSEDLVVGRAFAVAWPIGHWRGLGDPDPYASVADARAGATTVPDSANNHQGIIQLPTPAELPLVMGVVGLHRTRGRWQRAVRRRRGGPCGRRT... | 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: 337
Sequence Mass (Da): 37291
Location Topology: Single-pass type II membrane protein
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A0A1Q8UXH6 | MKRSVLKQRVRVSFILLISLTVITIIMLTYFLYEKFYVEKQISLLQSHGQLVAAQYGQFSNSEFIEKINWLDSVLEANVIFTSDPMLLSGGLPFEMEIEETLITFEERQVLLEGDTLVLIREHPRFAQDILAVVTPIMGSQGLEAVLFLYMPLVTVYEPFESIRYILIGFVVLTVMVVSFVTRKITNYFIRPIEEMMEITKKMANGDLTERLEINRRDELGQLAISFNRMSSSLEQAETKRREFLSNVSHELRTPISYMQGYTEAFEEKMITPEQYMQTMKKETAYIGRLVHDLLDLAQLEGDTYPITKVPLPFAQLIEE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 461
Sequence Mass (Da): 52916
Location Topology: Multi-pass membrane protein
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A0A8C4G556 | LIPHIRSLSPIRLELGKMAGSDFPSEVSKKXXXXXINGQAVKLKYCFTCKIFRPPRASHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYLFILSLSLLTLFIFAFVITHVILRKYVGVQTLDSLFLDSLTVLEVVVCFFSVWSIVGLSGFHTYLISSNQTTNEDIKGSWSTKRGKDNYNPYSYGSIITNCCAALCGPLPPRWVQDKRMTSCIEFHASFTGLERAWRDGVGNKPPPPVVAICCMCVCVCVCVCVWTYKDEAQKHTCIPRSMCAPHVKYTQ | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 280
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 31650
Location Topology: Multi-pass membrane protein
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A0A1G2EMP6 | MIILGIETSCDDTASSAVKFERKKIKVLSNVISSQVEIHKKWGGVYPSLAKREHSKNLPFVAKKALKGIKPDAIAITAGPGLDPCLWTGIEFAKDLAKERNIPLIPVNHIEAHILSCFIGQDPKLPALALVISGGHTQLILVEKIGKYKLIGETRDDAAGECFDKTARILGLPYPGGPAIAEKAEKAGKELGFSLPRPMINTKDYDFSFSGLKTAVLYDFKKRKDKGENYVRAMAKEIQQAIIDVAVKKTMRASLDYGVDTILVAGGVSANKELKKQFKENFKNVFFPLNGLSTDNAVMVAIAGYYNRKKAKKDIKADPN... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0A944ALX3 | MKFLEVSDKTVDSAIFKGLNELGLSIDEVEIEIVQQDTRGILGIGKKDAIVRLTQKPEDEVIIPDFAELAREGRRERSDDRRKSGNTDRNRNDRPCNDRRGDKRPEGREARPGAPKQDRPPKQEHRPQVQKPQPIHEISESICDTVAPTEVAVPTPAIGEKKFELTIENAANEEGAIFLKGMLTRMGIECEMLAGGDENELAIQISSPSMALIIGHRGETLDSLQYLTSLVVNKNRKEDGYRRVTVDIEGYRQKREETLVKLARRVAQQVKQTGRPRTLEPMNPYERRILHSTLQSSVYVTTHSVGDEPNRRVVVSPKRR... | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 349
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
G3MZM8 | MAAPVLLRVSVPRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSIFGLIFYILQLLLGLTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICVITYVLNFILLIINYKRLVYLNEAWKRQLQPKQD | EC: 1.17.4.4
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 176
Sequence Mass (Da): 19832
Location Topology: Multi-pass membrane protein
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A0A0D6QN20 | MGYDAVYDKLKDECGVFGIWAVGQSEEAANFTYLGLHALQHRGQESAGIVSSDGETLHTHRDMGLVADIFDAGVLSTLKGGAAIGHVRYSTTGASHLKNAQPLAVQYAGGPVALAHNGNLVNAEALRAELEAQGSIFTASTDSEVIVHLIARARASGAPGSAEQLVGAVRQALGRVSGAYSILFLTPKVMVGARDPMGFRPLVLGRLKGSWVLASETTALDLIEAEYVREVEPGELVIVDGSGLRSERLFPDERPPARLGRCVFEHIYFARPDTVLFGRSVYAVRHGFGRQLAREHAVNADLVIPVPDSGVPAAIGYAEE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
EC: 2.4... |
A0A3Q1N556 | MLRGVLGKTFRLVGYTIQYGCIAHCAFEYVGGVLVCSGPSMEPTIQNSDIVFAENLSRHFYGIQRGDIVVAKSPSDPKSNICKRVIGLEGDKILTSSPAGFFKSHSYVRMLG | Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO.
EC: 3.4.21.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 112
Se... |
A0A136MLH9 | MIVGVGVDVVAIERIRTLYEKHGERLLKRIYTQIERDYCFGFSDPLPHLAARFAAKEAVYKALPGRGPIFWKEIEVQNDPSGRPHLHIFGETWKRAEQGGVQRSWISLAHDAGVAIAQVVLEGEPEYNKTKHISIRRIAMPFTLTLGAKAPDFKLPATDGKTYSLKDFADAKALVVFFTCNHCPYVVGSDEVTRKTVEKFSPRGVAFAGINSNSRNTYAEDSFEGMVARMKENHFPWVYLRDESQDVARATGL | 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: 253
Sequence Mass (Da): 28432
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A0A136MI52 | MWLFFYNIMVHIAFVACLPWLVWKAWRTGKFKEGFGERFGHLSAGWVPSSAARRPIWIHAVSVGEAQMLPPILERLSRVYPDVPVVVSTNTVTGQAVAKSLPRVAGSFYVPLDLSWAVRKVIRLLRPRLLVIFETEIWPNLIAQNTRSDIPVIFLNGRIGDRSFQKYLKIRFFLRRILQFPRVLGMRSDEDARRILAMGAPLDRVRVLGNLKFESAFQLVHEQNLPTRQELGISDEALLIVAGSTFPGEEEMLLMVFKQLHPKNPRLRLLVAPRHPERFEEVAQLIETSGLPLHRFSTRSPGTVKPQSDTSPILLLDVMG... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A8K0PUC1 | MSPDLVFQLRGTCNNYDWGKKGSQSLAAHLCSKTSGDDFVIENDKPYSEMWFGDYPNFPARIAETGELLGDRIYNRSSMLGEGGIKKFGEHLPFLPKILSIGNPLPLQIHPNKELAAKLHQEDPDQFTDPNHKPEIAVALTEFKAFAGWRTLEVIAEVFNIAALNTFVPENVSSWSDETLRAVIRNILHAEDSTVRQALEVLERTPRNELGKSGYVLDLRPVLKEQFGSHDPAVLVAPLCMNFLVLQPGQALFIPADGIHAYVSGDILECMARSDNMLDTGFCGPRVDKSTIDTFSDSMTFKDCSRKNVELPRNKAHQGS... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer r... |
A0A2X3CZ42 | MNHSLKPWNTFGIERFAKTIVRAETEQQLLSAWQTAAAAGEPTLILGEGSNVLFLNDYAGTVILNRIMGIEVSETPEAWRLHVGAGENWHQLVQFTLQHAMPGLENLALIPGSQDLRRSRILAPTALSYSGFANMLTALSWKPGVSNVFQPRNAVLAIATVSSNMNIRTAMPSSRLAYRLAKTWQPVLSYGDLTRLDPQTVTPQQVFDAVCHMRMTKLPDPKINGNAGSFFKNPIVSAQVAKALLRSSLMHRTIRRQMAASSWPLAG | 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: 267
Sequence Mass (Da): 29404
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A0A2J0KUT2 | MLRNSMDSITLKAPAKLNLFLEVLGKRRDGYHNIITIFERINLCDDIVISIVDRGIKVFCDQKIPEKENLAYKAAKLILSRSKVNQGVFVKITKNIPIASGMGGGSSDAAYTLIGINKLFKLGYKKDGLIRLGRLLGSDVPFFILERSFAIGKGRGDSVKGLDFTPPKIWHLLMFPGVKKLTKDIYRALKLDLTKKVHNVKMLEHALKMGDFDLMKETTYNRLEGPAFDREPRLSAIKSSLIKLGIKGASLTGSGPTIFGIVKSRKEAISLSAEVLKKRTGFEKEGWRLFIAHTL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
B0PCZ7 | MLSERFEEDTGFHDRSEEVPAMIISGAQAMVNCLEAQGVSIVFGYPGAAICPFYDCLAQSGIRHILVRSEQNAGHAASGYARVAGRPGVCIATSGPGATNLLTALATAYADSIPLVAITGQVETGLLGRDVFQEVDTTGAASPFIKYSYLVEDARDIPRVFREAFYIASTGRPGPVLIDMPVDIQRAQLDFAYPETVSIRGYKPRIQGHAGQVERVARALCAARRPLLVVGGGAVGARGSVRRLCEMCGLPAVSTMMGIGTLPSKHPLYFGMLGQSGAPAANEAVGQSDLLMILGARADNRAMGRPGCLGADKTVIHIDI... | 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: 557
Sequence Mass (Da): 59084
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E0NPB2 | MYTLLVILIVLASLLMIFVVLIQESKGGGLSSNFSSSNAIMGVRKTTDFIEKTTWGLAIALVVISVACSYVVPSTVNTESVIEKSATESNTTNPNNLPGFGTGQSQQTAPAGQSNTPATPKAPASPAK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 13260
Location Topology: Multi-pass membrane protein
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D2MQN9 | MLKKRRKIKNKSLGVFGLIVTLLIVLAATTYQTIIRRINLGLDLQGGFEILYQIEPLQKGKAVDMPSVIKSISKRVNVLGVNEPQISVEGNNRVRVQLAGAKDLNTARKLIGTTAKLTFRDVNDKELADSSILQEGGASLAYQSGEPVVSFKVKDTAKFRAITREIAAKKNGQNVMVIWLDYSKGDSYQVESQKKAQGKEPKYVSAASVNQALSGDSIIQGNFTEESARTLANLINSGSLPVKLTEISSNVVSAAYGQDALSKTAFAGMIGVGVVMLFMIAVYRLPGIVASIMLVSYVWAVFGIYALMGATFTLSGIGAL... | 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: 765
Sequence Mass (Da): 84181
Location... |
A0A0R3JXS7 | MIIGIGTDIIEIDRIKIAIERSERFKEKIFTDNELSYLKNKNVESYAGYFCAKEAISKALGTGISGFSWKDIEILKINSVPNVRLHNAALQIANQKGIKTIHISISHSKDYAIAMAVAEG | 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: 120
Sequence Mass (Da): 13311
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A0A2T6AUL7 | MIYAAVGIGGILGALLRYGLSVLLFVPGGGFPLGTLAANWIGCLALGWFHARPPSSPVFRTGIGTGLIGSFTTFSTFSVETVTFLQDGRWITAGIYLLASIWGGIWLIRTGSRLGACRKEGARC | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 124
Sequence Mass (Da): 13067
Location Topology: Multi-pass membrane protein
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E1BA89 | MLSKKNNNNNMLSSGAAFSSPTAAEMVEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVSNANVIMQIPERIVVAGNNEDIPFSRPPLALKTPPRVLTLSERPLDFLDLERPAPTPQNDEIRAVGRLKGERSMSENALRQNGQLVKTDSIPVSRGGSAATTSHPHHDNVRYGISNIDAMIEGTSEDMTKLNRRLQLLKEENKEWAEREMVMYSITVAFWRLNSWLWFRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 239
Sequence Mass (Da): 27065
Location Topology: Single-pass type I... |
A0A8C3ZXV7 | AIQGEVRECAFNDQQQQFEEQHAGGEWPVSRDNNTILCSSGSRCYGLWEKTHDGDIRLVKQGECCWTHTSDQQDCHDDRCVVTTTPSLIQNGTYRFCCCSSNMCNLNFTENWVISPTSPQPPYPKTLYKEETIVIAMASVFIVAVLIVAIFFGYRMLTGDRKQGLHNMDMMEAAASEPSLDLDSLKLLELIGRGRYGSVYKGSLDERPVAVKVFSYANRQNFVNERAIYRTPLLEHDNIARFIVGDERLTSDGRMEYLLVMEYYPHGSLCRYLSVQAGDWVSCCRLAHSVTRGLAYLHTELLRGDVYKPAVSHRDLNSRN... | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 528
Sequence Mass (Da): 59802
Location Topology: Single-pass type I membrane protein
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A0A1V6E5K5 | MKNMDIPNKLVMFSEDLLTRRKKRSLRAKMKQQKRHPILDWIYAILWAACVVLVINQYFFQNYRIPSGSMEKTLLVGDMIFVDKLSYGPELLPGVLKTPGISTPKRGNVIVFENPTYLSRGPIYTIFQQLLYMVTFTLVDIDREATGEPRVHYLIKRAIGVGGDTLRVRNGEVSIKPMGSSVFLDERMLMEGLGLPVKMQRLVNSNEYTEIDNVGIASAYAELSLPLPSRVGMPSVQNANKDAFQYDMIRVTTLRDADPSNSRNAQLAQRYENGWYIADSRIFPMGDNRDNSRDARYFGPIAEKKVLGHALFVYFPLSRI... | 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: 324
Sequence Mass (Da): 36864
Location Topology: Single-pass type II membrane protein
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A0A2J0KYW7 | MKPIELFSGIEYSTLQDISKIDLDIKRITCNSQDVQEGDVFIAIKGDRFDGHNFLNAAIARGAGMAIVERMSLVQDGFIQIKVNDTRRAVSILARNFYRDPSKYIKIIGVTGTNGKTTITYLLEDIFKNANFKTGVIGTINYRVGENVMDSEQRTTPDPLTLNKLLRDMIEQSIPYCFVEVSSHGLEQGRVEDIKFAGGVFTNLTHEHLDYHKTVENYLKAKLKLFENLSQDSYAVINNDSRYRDELISRVDAKIITYGIEKESDVMAKDLRLDLNGVRCRIHAEDDVIDIKTSLIGKHNVYNILAAASVAMEEGLGPDR... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A447RVT7 | MPFYDPRDNRPLKLPMIFPGSPAVTQQQAAAIVASWFGSKAGWRGQQFPVYFNELPDRNAIVFATNDKRPDFLRDHPPVKAPTIEMIDNPNDPYVKLLVIFGRDDNDLLLAAKGIAQGNILFRGSSVTVDGIKTLQPRQPYDAPNWVRTDRSVTFAELKTYEQQLQSSGLVPDAITVALNLPPDLYLLRANGIDMDLKYRYTMPPVKDSSRMDISLNDQFLQSFSLKQLPGREQTDPAPAGAAGAAGRQIGGHHPRAASWGG | 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: 262
Sequence Mass (Da): 28987
|
A0A447S3D3 | MDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIRCSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTLVFLLATATIWPFSAWSGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASAFLPARGVEERTLADAAQLSSLADETPEGRSIVVLAKQRFNLRERDLQSLHATFVPFTAQTRMSGINIDQRMIRKGSVDAIRRHVEANGGHFPADVDKQVEEVARQGATPLVVAEGEKVLGIIALKDIVKGGIKERFAQLRKMGIKTVMITG... | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cyto... |
A9UVR8 | MIMRELGRGGQERLKAARVLIVGCGGLGCPSAMYLAGAGVGTLGLVDDDEVDVSNLHRQTLHTEARQGMPKCESIRLALMALNHHVDIQTHPSRLTPANALELVRQYDVVLDASDNAPTRYLINDACVIAGRPLVSGSALRWEGQLIVYNHKGGPCYRCLFPKPPPAHTVTNCSDGGVLGPIPGLIGCLQALEAMKVILGCPVLNEHLLLVDGYADQFRRVKMRARNTACAICGDQARDQQVGLLEDYEAFCHMSACDATQDLQLIAAEQRIDAHELDRLLRVDTAGGSPPLLVDVRSEVEFGMCSIGGSCNLPLQQLER... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of the s... |
A0A507C5G2 | MATLEAIKYRRSSLEIINQLLLPYESVFEEIKSVEDGHTAIKTMKVRGAPAIAIVAALSLAIELHVHTVHAAHSPFATPSAVVEYVLNKLEYLKTSRPTAVNLFDAARKLAAVVETSAQQAGLNVESKEASQTVVEAYISAAEAMLRHDVEDNRNIGRFGAEFVSSLYQPNAQIKLLTHCNTGSLATAGWGTALGIVRDMHQSGRLNHVFCTETRPYNQGSRLTAYELVYEKIPSTLVTDSMVGALLKKGGISAIVVGADRVTANGDTANKIGTYQLALLAHYHKVPFLVAAPSTSIDLSLASGDLITIEERGPVEVVTI... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-a... |
D5K2S8 | AELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRMNNMSFWLLPPSLLXLLSSSGVEAGAGTGWTVYPPLAGNLAHVGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPAISQYQTPLFIWSVLVTAVLLLLSLPXXAAGITMLL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A396MUM9 | MLRFLLPLRKIKSFGLIMKTKIAIVGTGGVGGFLGGLLARRYRDDPEVDIYFISRGQALENIRSRGLIVESQQGNFTARPKAATDSAAEIGEMDYILLCTKAYDIEGAVGQIRPAIGPRTVILPFLNGVDSAEKIKRMLPGHAVWDGCVYVVAFIVEPGRIAEHTNGYRYLFGSAQGPDERLEELERIFTGAEVRARLVPDITRRVWDKFAFISTVATATSYTDEPYGGVLGNPDYRAQFTALLDEFQAVAKAKGIVLSDGIAAQVVDQMERIPTDTTTSMQRDFRAHRSTELESLTGYIVREGKRLDVPTPTYDRMYAG... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 324
Sequen... |
A0A2S8GF20 | MSTTPLAFEQRRAGRMAIVADYVELTKPKIAVMLLAAVGVSGCVATWGQPDLWRLFHAIVGTALVAASSCVWNQCIERRIDLLMKRTRDRPLPSGRIAPRSAAMFGAALGSSGVAYLAATVGWQVAAIGAVTWLLYVVVYTPMKQASPWNTAVGAVAGALPLLMGWAAMGAAFDLRAAALFAILFFWQFPHFMAIAWIYRKDYAAAGMQMLPVVDPTGIRAGRQAIGAALALTLVSVVPFLNAPLDGAPWCIAAALALGFGQLLLAVRFSVRRDDRSARHLLWASLVYLPAMLGVLLAFPIL | 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 + ... |
A0A7Y3W5Q2 | MGNFDGVHKGHRALIDEAKSLADELGAPLAAVTFEPHPRRVFRPDEPPFLLTPLEAKAELLEEAGCADVFALPFTPELHRQTPEEFIRGILFGTLGLKGVATGQDFQFGAGRAGSSETLAEIAGKIGLHYKAIAPVGTGEEKFSSSQARDALRAGDPVAAAQVLGYDWFVDGEVLKGRELARTLGFPTANIAMADQIRPLYGVYAVEAVVGGKAYPGVANIGVRPTVDGKEERLEVHLFDFSGDLYGQTMRCRFRHFIREERPMNGLDALKAQIAEDSGRARELLGA | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 287
Sequence Mass (Da): 31001
|
F1MS86 | MAWQGLATEFLQVPAVTRTYTAACVLTTAAVQLELLSPFQLYFNPHLVFRKFQVWRLITNFLFFGPLGFSFFFNMLFVFRYCRMLEEGSFRGRTADFVFMFLFGGVLMTLLGLLGSLFFLGQALTAMLVYVWSRRSPGVRVNFFGLLTFQAPFLPWALMGFSMLLGNSILVDLLGIAVGHVYYFLEDVFPNQPGGKRLLLTPSFLKLLLDAPEEDPNYLPLPEEQPGPLQQ | Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome.
Subcellular Location: Endoplasmic reti... |
A0A377TZE2 | MPSLAIPPHWPHPVRWIGRLIAVSQRVVRRVCHSDRALRIGGRGDVAGGDRPDMGRGLGVLALAHGIHPWLGWLVEVWMIFTALAGRCLAQSAMAVARPLQAGDLAESRHKLSWIVGRDTSQLQPAQINRAVVETVAENTVDGIIAPLFFLLLGGAPLAMAYKAVNTLDSMVGYKHEKYRAIGMVSARLDDVANFLPARLSWLLLSLAAVLCRKMAPGRCVRAGAIAISTAVLTAPGRKRPSPARWGSALAARTITSASALKSPG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 265
Sequence Mass (Da): 28358
Location Topology: Multi-pass membrane protein
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A0A5P9KH82 | RMNNLSFWLLIPSIMLLMLSSMTGSGMGTGWTVYPPLSSTTFHSSMSVDLGIISLHIAGMSSILGAMNFITTIFYSKNISMNYNQISLFPWSVIITAILLLLSLPVLAGAITMLLTDRNLNSSFFEPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A2Z6MQF0 | MDWRFKTALRLACPTEIPLTNLTVVPIDMTPTIFDNHYYRDIMMGRGLFGIDSDISTDPRTAPFVMRFAVDQNYFFDSFKSAFVKLSSSNVLTNMQGEVRRKCNQRN | 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: 107
Sequence Mass (Da): 12395
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A0A7H1N6V5 | MVGAAAKTVPMQQTRKHPVIIGIVGDSGAGKSTMAAGLAEVLGIERTLIICMDDYIKHDRRRRAELGVTAHNPAGNHIDILEQHVGLLRDGQPILKPVYNHQGGTLEPPEYVVPRQFIILEGLLGYSTPSLRDAYDLKIFLDPREQLRLRWKFQRDTTQGGYTVEQVMASLDRLNRDSVSNVLPQRGYADLVVNFYPPDDKPDEIASPLNVRHLLRPTLPQIDLTTLLELSPPRGLEMELARDVDGRPADALHIYGEIVGADSAAIEAHLWRSVANGSRDPSQPFPRLGAFCDGRSTVQHSPSLALSQLLLTQYLLTAAL... | Pathway: Carbohydrate biosynthesis.
EC: 2.7.1.19
Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Length: 325
Sequence Mass (Da): 35828
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A0A2Z6MZA5 | MSNSYLQLLLLLVLYIISANSAQPYEGNYGEAVFTLQVPTLEETNLDNLLSFGYYHKSCPQFESTLHNKVKEWIKKDETLAASLLRLHFHDCSVRGHENITSLIEYFQSKGLTVLDLVVLSGAHTIGRTTCGSIQNRLYNYQGTGKPDPSIDAKYLNFLKRKCRWASEYVDLDATTPKTFDRMYYINLKKNMGLLSTDQWLQSDPRTSPLVSALSASPSVFEHQFAVSMSKFGVIDVLTEEDEGEIRTNCNYVNAY | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A0A1Y6CPF9 | MTACLARADRGLRIWEGFLVVLAAAAQGVIALLVLAGILSRSFPAFMVPDNVVLVRSLLLVSLAFALGEATRTGANITVDLLADRLGPRARRILELLGALAGLLLLVPLAVWLATYSLDLFHSGRTNMGLLRVPQWPTYAALCLGFATMSLRLCLIALAAIVSERALGRVRGNAA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 18588
Location Topology: Multi-pass membrane protein
|
A0A2X3CT18 | MGLIFHDTIKSLFNPVNVMYALIVGGVLLIAAEVLKPKQPRAVGIDDMTYRQAFVIGCFQCLALWPGFSARGRLSPAAC | 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: 79
Sequence Mass (Da): 8582
Location Topology: Multi-pass membrane protein
|
A0A6G2KU90 | MNVRIFEVFTSVEGEGTLCGTKTLFVRLAGCPFSCFYCDTAEALPADSGVEYTLHDAQVLIKESLQEHTYKVNFTGGDPLMQHKSVALLAEYVQRQGVHTYLESSCFDSKRFSHVLPYFDYIKIEFKTPDSEFVRSNDYGTMYESTMQCLTNSVRADKTTYIKVVVSRRTTPEYMQRLVQDIYDVAAPNEISGFVIQPTYGVEEPSLESLLRMYDVIHSRYADVRIIPQLHKYLGAP | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
L0E1W5 | MNSSEPAVSAPGKSMTDTTPERSRCADLDLPEAVLQGIRKAGFEYCTPIQALTLPIALAGHDVAGQAQTGTGKTAAFLLAAFNRLLRHPPPPDRRRDDVRMLVLAPTRELAIQIHKDALLLGAHTDLKFALAYGGTGYEQQREQLQAGADVLIGTPGRIIDYHKQRVFGLKRTEVVVLDEADRMFDLGFIKDIRYLLRRCSPPTQRQSMLFSATLSWRVMELAYEHMNNPEKVQAQAETVTADRIRQVIYYPANEQKIPLLIGLARKLQPERAIVFVNTKHWAERVCDWLNANELKAALLSGDVPQTKRSRLLSQFAEGK... | Function: DEAD-box RNA helicase involved in RNA degradation. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Cytoplasm
Sequence Length: 457
Sequence Mass (Da): 50918
|
A0A293MUX2 | MNPQQWVLWILLLTLLTAVFLYNYTTTSPFTVRPTYLKQNADQILPWYNRTSSGNSSAIPRILLWTNFYASRMLGLSPEEDTEIPNCHRRCHVTYNRNLLSSSDAVVFHSRDMNLVDMPSRRAPEQKWVFWCMEPPPYSFYGGFDFIVGMFNWTMTYRKDSNIPVPYGAFKRNDQATSADIEKSWSMKSKSVVWVVSHCKTDSWREGFVQELQQYIDVDVFGQCGPFKCPADPNNTCFDRFVKDYYFVLALENSLCRDYVTEKLFSALGHVIVPVAMGAVNYSAITPPHSVIDVSSFDSPRELADYLIQVRKDFDLYKRY... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 385
Sequence Mass (Da): 45396
Location Topology: Single-pass type II membrane protein
|
A0A293MYR9 | MAARLLAINFGNGLRRSLVPSVTHTHSTRCASSGDTSRKRELTKDAEDVLRDPAVARDIQEHQREIVIDTPMNIAPLTGVPEEHIKTRRVRIFVPARNAMQSGSHNTHAWKMEFETRERWENPLMGWCSTGDPLSNMDLNFKSKEEAMSFCEKNGWEYFVDDPPPHRPQARSYGDNFSWNRRTRVSTK | 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.
... |
A0A293MGM3 | MKIRMHFYAFLLAFFGLATITSFLYAVVSIVQKEAYMDEEFHIPQAQAYCDHNFTHWDPKITTPPGLYLTSLALTTVTNIFTSNNLCTVEDLRLTNSFLTVLNLWLSCLISIKLAYAYATVKVRVKLVFSSAVLTTLPVLYFFTFLYYTDPGTVFFLQLMYLYHLFEGYWMAAAFGAASVLFRQTSVVWVAMLAGCRLLEIVEEECFQDIKPCDVVKSVIQKWAVVVQKIFLDCLGYIVVGVLFLTFLFFFVIHAHPRSSVPASSKCGEGLLWKCGATLLVLRFTGCTLDSRGQTV | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A2Z6PU06 | MSFFCQPKRLGALNKFKSGDCNILLCTDVASRGLDIPAVDMVINYDIPTNSKVRCAMTARAERSGVAISLVNQYELEWYIQIEKLIGKKLPEYPAQEEEVLLLEERVSEARRLAATAN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 118
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 13251
|
A0A1F7J488 | MVSTERLDKTAPEKREVPSSINIIFEGYRGTGKSTIATLVAERLGRQLISTDVEVERREGRKISDMVAEFGWNHFRDRESEICHEASLMEGVVIDLGGGAVLREENRRDLKRNAVVILLTASNETIAERISMNDDRPSLTGSKSAVEEIADVMGIRGPIYNEMADHTISTDEHDIEESVQLVIDAVTRASKKLYRKVPELLRIFQADLQHVTKERNLPFQMRLATVDDIPALVPLICAAYLYENEGEMAFKQRERVRADAESVVEAMREGLVLVATKQGDEGEQIIGCMQYKEISSTEGSASGQETSAYFGLFAVDQRLQ... | 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... |
A0A4P1TPQ7 | LYMVLGAWSSAVGTSMSVIIRSELSSPGSLIGSDQIYNVLVTAHAFIMIFFMVMPLMIGGFGNWLVPLMLGSPDMAFPRMNNMSFWLLPPSLMFLLLSGLVESGVGTGWTVYPPLSGSLGHSGVSVDLAIFSLHLAGVSSILGAVNFISTVVNMRSTGLYWDQVPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPGEGGDPVLYQHL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A5N7AEN9 | MNILFWFAGNACFFSPANFILARPGPYINAEVSGGGFPGWVQRIEGSVRTTDPSFLNAIENYISTIGGLISKAQITNGGPVILFQPENEYSVCEGAPSDEDLNFCLEKNYMAAIKQQFRDAGVVVPFVNNDAVALGNWAPGTGKGAVDIYGFDNYPFGWGNGCESRELDTDYRPLTQYNFTQHQSMSFGTPFSLIELQGGAPDQWGDTGVDVCAEMVSNIFARVFYKINYGFRITIFNLYMMLGGTNWGNLGYSSGYTSYDVGAPIMEDRQITRVPISTSYKWQVNTSQGNITVPQLGGFLTLHGRDSRFHVTGYDLGVV... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
EC: 3.2.1.23
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Length: 563
Sequence Mass (Da): 62232
|
A0A4P0XU82 | MTHQLKSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAIGFLITAWVCRC | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell inner membrane
Sequence Length: 57
Sequence Mass (Da): 6222
Location Topology: Multi-pass membrane protein
|
A0A2S8R8N4 | MKQKATVLLAIIMCMTILVMPNVQARTVTSNEIGTHGGYDFEFWVDSGSGSMTLKDGGAFSCQWSNINNILFRKGRKFDQTKTHQQLGNIVVEYAADYRPNGNSYLCIYGWTVDPLVEYYIIESWGNWRPPGAQSKGMITVDGGTYDCQW | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 150
Sequence Mass (Da): 16880
|
A9V7I5 | MTPVQAACIPLFLDHCDVAADAVTGSGKTLAFVVPLLELLLRTPLPSPTSVGAIVLSPTRELAQQTYDVVKTFLQHGVDLSACLITGAHDVQVDVNQLKEGCNVIVATPGRLLDLLNKSGSLMKSVKHLEMLVLDEADRLLDMGFEQAITQIFTFLPKQRRTGLFSATQTNEVQALARAGLRNPVQVAVKVEHRQEGAGSVQQATPSTLINTYLFLSAEEKFNQLVAFLRLMRQQQAKAIVYMATCACVNYFVSLLENMPGLRRAKILALHSKVSSKARTSVFSTFCNTEGAILVSTDIAARGLDVPDVAWVLQYDPPQD... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 575
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 64816
|
A0A6J3CDE7 | MYNNSVYPWTESMLGPGCTLFALCVIIYTPVRFCHSFISISLKNNAWTCPYCHVXYPSEKFPAPDSAKKMKKIYQNCSQYQTLLLLLISLVCLSKIRAHWRTCEKCIEKYGPVQELGDAVTR | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 122
Sequence Mass (Da): 14020
|
A0A6J3DF86 | MAMALRKVLFGDTSRIFSRDWAQAHFRFREPHSDLAYALEADKGGTRAILMAVQGNIIKYLLFVRNTEYTHLERLCKISQKEQGEALAAALADSLWAAGEGQEATVCLISAATHFVPTTDYKADNFTERIQLFNFFEKAAAQKFIFDHINCFKSEGSKGLILFLYSLLFSRTLESYMPTLILMRRSNSQRNSDMMYDAPVTDLDITAIFCVWLHRVQNDLGGTTPHLLESSCGNVICTQVGSVLKTPKFPIWLCSINGMHSVLFSTNRLLLSDWKMEHVFHLYFYNGQRGQTRTAHLTVDTHSHHWEEGRRKDTSSPGKR... | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting... |
A0A378BMN8 | MQMTMRWFGPEEDKISLEHIRQVPGVEGVVGALYDVAVGEVWPVDKIERLVGQAHAAGLKMEVIESVNIHDDIKIGLPTRDRYIANYQQTIRNLARFGVKVICYNFMPVFDWMKTDMNYVLPDGSLTMAFEKKDIDKRLEDVVKEVLENSNGFALPGWEPERLAEVQTLFAKYSAVDDQKLRENLVYFLQAVIPVCEEVGVKMAIHPDDPPYSILACRGWSKTATIWTGSAGPSIHPPTALRSAPARLPKILIMTCTPSWPNLRGVSEFILPTSAI | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 276
Sequence Mass (Da): 30999
|
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