ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A507C615 | MPTWSDVSDDDLSSGPVDNRYKDARKVLTYGKRATRVYVKPSVKVWDVSPVSSIGSVATPDSSRFLRNETVGTPNHHHHKDWFSATPERERRSSSENDRNSIGSILSLHSNSPERHRSPLSDGSQKENTPTPALSDIKQPVQRLSSLSVNVASEKSRQSTGSSKIPLPGNCPASPLANKSVISSTQSVRSVSPPQSPSKLPVRCRTSYGSVASASSVESIANDGGVEDDVSMARFSSGSPVAASPTAKLRRMIGRILLNTDQTPSPISRVSIGSVTSYRAPPLHVATPKSQVPPSSPLWHHRPHYPSQVSSSSLTPLEEL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 669
Sequence Mass (Da): 74696
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A0A507C088 | MDIPDALLDIATFSLVLFYILVEESFHLQATHDIMLYGPINMTLYDHFTFPGAVPKSFMPSLLLSFLASPSLLAYKQSWISKFDIQIVVRVVLGGLTVLSLASIRDAVKARFGKDVAAWYSIIGMTEFHLLYYGSRTLPNTFAFVATNYALACWILGDVDEDGQSSSGIKDAPGSSSAATGSKDGSKSSNSSSEKKQPKQETPKSNSKPKQLTEGLTQMIQIFCFTAAVLRAEISVFAASIILVEWILHPSIISQSIIVGYQAAAMSVAMTVSVDMYFWNELWMWPEAKSFIYNVVYGKSSNWGVEPWHAYFSMHLPKLM... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 566
Sequence Mass (Da): 63449
Location Topology: Multi-pass membrane protein
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A0A7H1N4Z5 | MNSLLASAPLAFFATSPQPCPYLPDRYERRLVTDLSRRDAVPVHDALSQAGFRRSHTLAYTPICSGCAACVPVRVDVRGFQPDRAHRRVLAHNSDLLLQHLPPAATKEQYALFTAYQHRRHHHGDMAKMGYHDYQLLIEQTPVRTSILEVRDPTQILRAVCIVDHICDGLSAVYSFFDPTLRRRSLGTFIILSLIDRSHRADLNYLYLGFWIAQTTKMSYKARFRPLQGFTNTGWQRIDPAEWNDAGTAAADAEQTF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
A0A061D687 | MIGVNHVCEIFVEFAGGLSAFTVDKRRRLKIEIQTESVTVSQLVAYLRKAAFAAKRDLFAYPPKLEAIRCSEVEVRGDLPGVFNMGETSDVIPGVIVLIDDTDLELLGGSGHKLKGKRDVSFISSLHGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of the MOCS3/UBA4 homolog, then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3/UBA4 homolog.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function... |
T1YYY8 | LSNIQTHSGGSVDMAIFSLHCAGASSIMGAINFITTIFNMRTPGISMDKLPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPVLYQHLF | 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... |
A0A2S8G2I4 | MTKQVYDSIAMRHLLTRRFVIAMAVLCFASVISVAAVFTQLRKVERDARLINVSGRQRMLSQRIALLSTLVNEEQGNARQATTRSLEECISIMADAHAELSADSGKSKVRRQLFQGPDGLDQMVPQYLAAAKQVVANHSSENVIAVVKTMATQGALLGKLDAVVAAYEAENEYRKMGWFVALELLLLVVSFLTIVAVAWFVFRPIVKLVSSTLGALENSNEELTEFSYRISHDLRAPVVSCLGIVEVVKDALSENEVDAAITANQHIQTSLTRLSATIDSIVDVVRQRMTDVAPETFKLTSVVSESVDALRHMPDFACID... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 445
Sequence Mass (Da): 49294
Location Topology: Multi-pass membrane protein
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A0A319CCV8 | MVDGYQECLHCQYTHPSFSVYYPPTSYAVHNHQNFSQHIADPKKPDDGLFLYFFPNCTLNVYGGGMSSFRVCPTEDPHVTRMEFDYYHMESGEKFEQYYKFVRQVAMEDYELCEKAQDNLARGIYSEGILNPEKENGVSFYQGRVFELVCEQYAADQAEQAGSKKAIGHKEGAEMTMAVVA | Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (monooxygenase route): step 1/1.
Function: Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
EC: 1.14.15.7
Catalytic Activity: choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin... |
A0A7Y3W508 | MMRAVSDYAPRPGPPPTLIGIGGIAWSGDPSVCYSTLLGSCIAVCLWDPMACKGGITHFLLAEAPSDKADDTRYGTVALPLLAMNLAAVGCDRQRFRAIVAGGSDLLSNMKPIGTENSEYALEWLRQERIQIVQKDFGGSNARRVRFHPSTGVCEITTIANAPQSPS | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 167
Sequence Mass (Da): 17837
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A0A293MM42 | MMTYLVSQQSCSTRRDTVTSVHHVRPPGLFKELHQNQVCHHRQLHVPPSLQGIRRDTLKSYIKTKYVIIDNFMCRLHYKASVGILVAFSILVTGKQYIGDPIDCISKDAIPHDLLDTYCWIHKTFSVPSAWEKKVGDEAAYPGVAPRPPTENVVYHTYPTENVVYHTYYQWVCLQALFFYVPRYIWKTWEGKRVQNLTEQLTEPMKDGATVTKASEMLVDYLDQNRGYHGGYFFGFVPDRTADGAHEGRSDSNESKRNVG | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 260
Sequence Mass (Da): 29922
Location Topology: Multi-pass membrane protein
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A0A851CZL5 | YVYSRPPPWSDTLPTIFVITPTYTRPVQKAELTRLANTFLHVQNLHWVVVEDSPRRTNLVSNLLEKAGLNFTHLNVETPKSLKLGLSRIPSHTPRGTLQRNLGLHWLRDSFSNTAQPEGVVYFADDDNTYSLELFEEIRYTRTVSVWPVAFVGGLRYESPKVSPAGKVVGWKTVFDPNRPFAIDMAGFAVNIKLILEKPHASFKLEGVKGGYQETSLLKDLVTMDGLEPKAANCTKVLVWHTRTERPTLVNEGKRGFTDPRVEV | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular ... |
A0A293LJQ6 | MVLQNSGRYKSDKFDKKKNDDGKTYQKEDTSERRLQDSLFRDEIDRKFGFERHKLPTERVGWLVNIKQTEILNEDKRLISAVDYYFIEEDGGRFKVSLPYEPYFYVAAKPGTEQEVISYLTRKYQGTLTRVEIIPKEDLDLPNHLVGLKRKYLKLLFVSVSDLMKVRKELLPAIHKNQERQKISATSGTDTREMQDSNSGPRKMTEQTDNIVDIREYDVPYHVRVSIDLKIFVGLWYSVRGRGNDAPDIRKREDLLQTPD | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 260
Sequence Mass (Da): 30544
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A0A2Z6MJW2 | MKDKTVIITTLNDAWAEPGDNFTNEAFFMTPTYLHMMWRRIEFLGAVLHLGYNFVFTDTDIMWLRDPFKLFYKDADFQIACDYFNGNSYDLHNLPNGGFTYVKSNARTIWFYKFWYNSRELYPTMHDQDVLNKIKMHPLITTKKLKIRFLSTGYFGGFCESSKDFAKVATMHANCCVGLENKVNDLKILLKDWKKYMALNDDKRKNSHPSWSVPKSCR | EC: 2.4.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 218
Sequence Mass (Da): 25720
Location Topology: Single-pass type II membrane protein
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A0A7S0C1E1 | MIKGGDLVTSLSSNDVVRSNDINHVSSYKTQGMRPYQEDEMLIQGPNSHDANSSYFLGVFDGHGGHAVSRYLKQNLFAAYLLCRRRSRESSALLLKKVDGNSKNMQGSEELGNYFTPSIDEPGASVENLQNGNNFFDDDGLVRISINALQMAFEKVDQEVQRVSHWSFQGSTAVVVLLLKLQNQRIIVSANVGDSRAVVCQRYCPSKLNEGCNTVITAVDLTVDHKPNVLSERIRIEKLGGCITKPTSSGGVHRINGNLAVSRAIGDRSEKPWVSSQVDIKIHATSISTDVIDEFIIMASDGLWDVMSSAEAVSLCREYV... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 385
Sequence Mass (Da): 42982
Location Topology: Peripheral membrane protein
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A0A378F4C4 | MFLLLVVLPACLWRKGKTSGCVQQLHDICLDCDGDAVLLLVVQKGEACHTSRRSCFYNAIKGDELTVLVLNNKVDLISEAQKEKLVAILHSLNPRARIVVSQFGQVPLSNILNTGLFDFEQAAQAPGWLKELRGEHTPETEEYGITSFVFRARRPFHPTRFWQVMDGVVRSKGYFWLASRPEFAGSWSQAGGIARQALGGVWWASVPKERWPEDAESLKFIMSHWIDGIGDARQELVFIGMDMNESKLRNRLDSALLTDAEMAEGPQNWRHYPDPVEPWFEE | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A1G2IE94 | MESGSIFEQLGIHWQLLLSQAVNFFILLIILRVFAYKPLLAVIKKRNEKIKEGLQKAEEAEARLKEVDIIAKKHLQKADQEAMEIIKATQKKAETLQQSLQKETEDRQKELMAQAELAYLRQQEQAKQLVFSQAMELVKKTIMKTVELKPEIIDEALIKKAVLQVKDEI | 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: 169
Sequence Mass (Da): 19525
Location Topology: Single-pass membrane protein
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A0A1U9VXT9 | MINQNKHRQLQIGLASPEQIRAWSERILPNGERVGEVTNPYAFDIETNKPERDGLFRERIFGPKKTGVCACGKPKVIENEEGSQFCKHCGVELVDSRIRRYRMGYIKLACPVVHIWYFKRRPSYIANLLDLTRKDLEGLVYCDEEEAPDWEEYMIRRRKDFLVRRMKLTKHFIQTNIQPEWMVLCLLPVLPPEPRPMFQLDEGDIITSDINELYRKLILRNRILTKFLAKLFTPLPDSVNGQKRLIQESVDALLDNGIGGQPVTDRHDRPYKSFSDLIQGKEGRFRENLLGKRVDYSGRSVIVVGPFLSLYQCGLPLEIA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Plastid
Sequenc... |
A0A6J3EAX1 | MRCPQPPRALLLLPALLSLALLGVRVQRRLSGEPLDGPQGPDGPGAPNAPDGPGGPNGVLGRPGSQGRPGGPGRLGSHGRPDGPGAINMAAFQWRASSSSSSSSSSSVKATAKPPPPSRHPLQPPYPYPYRFLLNEPHKCRERAPFLVLLVATEPADTAGRAAIRQTWGNESSVPGVSILRLFLTGVHPVFGAPLRRVLEEESALHRDILQQDFLDTYNNLTLKTLMGMEWVSRHCPGAAYVLKADRDVFLNLAFLVGRLLQPQLPPKRDFMTGYIYRDTGPLRSKAYKWYVPRQVYPNDTYPPYCGGPAYVLSGDLAAK... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 399
Sequence Mass (Da): 43544
Location Topology: Single-pass type II membrane protein
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A0A377TL36 | MAAYSYMALVPLIQPPIMKALTTDKERKIRMVQLRTVSKREKILFPAVLLATGGAPAAGRRAAAGDVLLRQPDARRAVWWSG | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9018
Location Topology: Multi-pass membrane protein
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A0A377U1N9 | MKLSFATIAPPPGSIVLRGSRPDASVEFGMRSDELVANALLNLEYTPSPSLLPVQSQLKVYLNDELMGVLPVTKEQLGKKIRAQLPIDRCTSPTSTAYGWSLSPLPRRLRKPGQQHAVAGRRTRKLSGSHLPVAEGK | 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: 137
Sequence Mass (Da): 14911
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A0A507C6A4 | MHWRISILLALAISLVGNLPAVHASKTLQLADIVFTINKGGDNQKITENLKYPAKLPSTLPTIKNTDTVKLSFTASFSDGSALPGLHQAVLSLQSTDPVSRVATQIATKLDVAYACDKGRGASYSVSTDFGTQDTIDAFLAHSGSYDAILYIAHSESSTPLAYPMGSIRINFPINAQVSIKPSMPESFRPEKEIHHIFRLPDKQAPKWLSGLFTILVVVPWVFLLAAWGILGANISNAFEPSTIVPAIAFFASLGGWVYLMYMYWLKLNMFQFLYYGGLLGLATFVVGRRALVDRAQLRLKKGY | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A2X3EJ31 | MLTEQLDWEKTDGMMPAIVQHAVSGEVLMHGYMNKEALEKTEATGKVTFYSRTKQRLWTKGETSGHVLNVVSITPDCDNDTLLVLVNPIGPTCHKGTTSCFGETGHQWLFLYQLEQLLAERKHADPGELLHGEAVCQRHQAYCAESGGRRRGDRAGRHGERPLRAEE | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A7G5XDJ8 | MRYFITGFMGSGKTYWGKQWSEKFGLKFYDLDEEIEKREGKAVTAIFEEKGEEAFRKMEKETLCTYMKLDNFILSCGGGTPCFHNNMKRMNAQGVTIYIKSPVELLVKRLHTEKETRPLIAGMNDEVLAQFITGKLTEREHFYNQAMYHLPAEFMSLDNFQKIIRRNG | 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... |
A0A293LVU6 | MSWYISIVSGRIYQFYLSSPMRDILSCDSYSPWSSFWNTSVVTVFGARSGWGTRRGQSCLAEQKFLTRFCCACWCFCESRIWGRQTIFVFSCEEELLLQDFSRNVSTKSSALFYGNAFIVSSIPIWLFWRIHQMDLYQSAIIFAVMTLVSTWLIALAYKNVKFVLKHKVAQKREDAVNREIMKKLSDDKKMSKKEKDERILWKKNEVADYEATTSDYEATTFSIFSPSSTTTPCSSPSSSSLPSTCSGLSVRVSTTYSPLSSPSSSSLPSTCSGLSVRVCILYSERYDTNVSDRNSFRERCTLIGAFGECCPSGPRWGFS... | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 350
Sequence Mass (Da): 39835
Location Topology: Multi-pass membrane protein
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A0A2Z6NVC1 | EWWKSDVEAVVNQATNSGMPPNISDAHTINGHPGPALGCISQGYTLHVESGKTYLLRIINAALNDELFFKIADHKLTVVEADASYLKPFETDTIFLSPGQTTNVLLTANKLVGKYLIATTPFMDAPIGFDNLSSIATLRYKGTPPYTKTILTNIPPLNATPITKTFSDSLRSINSNTYPTKVSSTIDHTLLFAITVGLNPCDTCLTGVWFLHCHLEVHTTWGLKMAFIVDNGRGPNESILPPPKDLPKC | Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
EC: 1.10.3.2
Subcellular Location: Secreted
Sequence Length: 249
Sequence Mass (Da): 27183
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A0A507BUF3 | MKRHIHLHVGPTNSGKTHEALSRLSTATTATYLGPLRLLAHEIYERLNKNGVACSLITGEERREVEGSKVTSCTVEMAPLFQKLDVAVIDEGQMMSDDSRGFAWTNSILGLQAKEIHICGEESIVDRVQAMCDVTGDSMTVRHYKRLTSLSMSPHSLNGRLDKIQKGDCVVTFSRMDIFGLKREIETATGLRCAVIYGGLPPEIRSEQARLFNDPASGFDVLVASDAIGMGLNLNIRRIIFERVEKYNGVDQQVLTVSQIKQIAGRAGRFNTIYSAGEVTTLEKPPDHSIVARALKSPVVPIRTAGLHPLLEQIEAFKSR... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Mitochondrion matrix
Sequence Length: 491
Sequence Mass (Da): 55174
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A0A061D9F6 | MADPSAEDDRKVLVKEFLDLDELKEREAKSRAVVLEILGDIPDADVAPPKNVLFVCKLNPVTEQDDLKLIFSRFGPVRSCDVIRDYKTGDSLQYAFVEFETEEACNDAYFKMQNVLVDDRRIHVDFCQSVSGFWKRFKENGTFTREVKGGPSQAETTRQGQWRRDYDRYRRQRGPVRDVRRQEYRNRGAGRDMDIEAMAEIDQCTVGAAATVADQAVLCPALQVTDLVCVVEGTLGISLGTDHKTATGIVIARDIVTGHNALHIDGTASVIFHEATHRTAPQVAVGPMGAANKRRKTTFTVLPYIGLPDTPNLMTFTMRT... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Nucleus
Sequence Length: 328
Sequence Mass (D... |
A0A507C697 | MRACIKLRKSLNVTACLKLQQTLIRRTYAAASTSQTINQLPAYPGADIKYTPTLTSKSSYPTIETFRILNPEGEIEPGATDPNLSRETCLKIYQSMVLTEIMDSLLYESNRHGRIGFYMSSSGEEAVAVASAAALKKDDHIISSAREQGSLVYLGFELKRIVGQAFANEADLGKGRQMPVHYTSKDLHFHPVSSPMGSQPPHGAGVGYALKRSKKDACCICFFGDGAASQGDFHAAVNMAAVHGSRTIFLCRNNGFSISTRTTEQYIGDGVAARGIALGVETMRVDGNDPLAVYSVVSKARKLTVSENRPILVEAMTYRL... | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A507CAN6 | MVAALGESTGSFMLSRMRDRMLLDSTGRKILQLQPIINTSTLPDNLSTLPPGTFGHEYLAFCTTHNVSADTRTPIKYISDPELAYVMTRYRQVHDFWHTLLGLGITVQDELAIKWFEMVQTGLPVAALSSFVGPARLSKAERDILFDVYVPWAVQTGARAKFLMNIMYEEEFERPLEDVRKDIGVWPAPI | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Subcellular Location: Mitochondrion inne... |
A0A2X3IRP5 | MDGENNTLVAMDPEVKPNTAGGPRTSTMQVNQYTIDSEQKAAQKFDPGTIRLLSNTSKENRMGNPVSYQIIPYAGGTHPAATGAKFAPDEWIYHRLSFMDKQLWVTRYHPTERYPEGKYPNRSAHDTGLGQYAKDDESLTNHDDVVWITTGTTHVARAEEWPIMPTEWAHALLKPWNFFDETPTLGEKKK | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 190
Sequence Mass (Da): 21509
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A0A061D197 | MDSLVGSIPCMTRLYITTSLCLMVLCSLDIISPLNLYMSWTLILQGEVWRLLTCFIYFGSFGMNFFWNIYVLIHYCSSLESVSMHNRPADFFWMLICSAVMLLGLSQIFHHNMFYGGTMINVLTYIWGRKNPYSRVGVVFISVPAPYLPWIMMLLSYFAGYLLTENLIGIAVGHTYYFFSDVFPRMPISRGIEIFGAPRFV | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 201
Sequence Mass (Da): 23186
Location Topology: Multi-pass membrane protein
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A0A0Q6GNX0 | MHPKTVGVPMHARDALNYYFESSRTSASVVHCYAFDVAGVTSPLRTHADALEFGEKILGLDPVFRRRLQKVPGHLAFPHWVTVDVDVARHVFVHTPAPDRSREFLVSKIVEFSTVPLDWDLPPWQFHFILDVVGVEGVPHGGTVAIFRSHHSAIDGMGVVEMLNRILSDEPVARGESDRAVAVPGVWSALRALPRDVGALVSAVARRRSATKAASKRGSTPSSAPHRTPYPATRFNYDARVHQDGPDEMTYAFLSVDFARVRAMKNAYPGVTVNDVMLTVVSLALSSYLDAIGEIPDRSLGTTIPVSTRAMADSTNANRI... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 490
Sequence Mass (Da): 52897
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A0A371SJ18 | MEGTQPLLGKTILNTRGKSAAAEFSKKILAAGGTPIEIPLLTFQKPNDTTLIEDTIKNLHMYEWLIFTSKNGVDFFFDFYDQVVEIVTKNIPMPKIAVVGTKTEKALLAKGYRPEIVPDEFIAEGLFESLRPHVMKGVRFLLARGNLSRSYLVDEITRHGAVATDLIVYETTGDSREKEHLITLLKEKQIDIITFTSPSTVKQFYNLVEQTDWEELTKDVLFACIGPETKKAADHLHIPIHICPKNYTTDHLLTEIINFLQAQGGE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A377XQP8 | MKLRGSENRDEITKAGFQSNHAGGILGGISSGQQIVANIALKPTSSITVPGHTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHFMRQRAQNGDVTTTIPRW | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 110
Sequence Mass (Da): 11921
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A0A447S6Z7 | MNSENFVAFNLSERIQLIGGTWYGGEMKKGLFSVMNYLLPQKGIASMHCSANRGEAGDVALFFGLSGTGKTTLSTDPHRQLIGDDEHGWDDDGVFNFEGGCYAKTINLDPQAEPEIYGAIRRNALLENVVVRADGSVDYADAAKPKTPASPIRCRISTISSSRCPARAIRRR | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.49
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Length: 172
Sequence Mass (Da): 18758
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A0A2Z6MV44 | MENLCLYGFPNEEWKVNLPVEKIPPELPEPALGINFARDGMQKVDWLSLVAAHSDAWLSGIAFYYGGEFGFNKSDRERLFNMINELPSILEVVTDAAKKQVEEKSSVSNHSGSKSNSSLILQARSPHVKETRALEPEVVEEAMEEDDEDVLCNILCGGYAFYC | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 163
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 18246... |
A9V4A9 | MAHAVFTYDVGDLEHEEGFADEVEHTVIILGREFKFKYTDQGSRDEIRSRASAFLWFTYRNSEYAIGDSPRHKTDRGWGCTLRVGQMIVGEALQRCHCPRDYDKLSYPSEAARMSILKEFEDRPDRVLSVHAMAMQSKFVGKRAGQWHTPTDVAHVLRLAVNEQEAMGLQVHVAMDSMVVLDDLRKLFRADRATLLFVPLRLGIDIVQAEMIPAVKRFFHSPSALGIMGGRPGAAHYFIGYMDHNLLLLDPHTTQDPLRAGSQDALVSCRCSRPMLLDLDKVDPTMCLAFLLTDEESLQRFADDYNASVEETGVRLFSML... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
A9VCH8 | MLLLTVNLLIASSAAWAWGALAASPQDMAVNEETWFLLSNLLAPVTPQNFVDSYYRRDLLHVPAAASSWSQLAAADPWLKGLRNVDAFLLETYAQLRTIPQAVNYKTPTGADRPAPPAATWSEEAARFHDSGESLVLRREATTAPLSKLELALQAAFQTNRVTAHAYISSGGAQALPFHTDRCAYDSGCDINCAPCPECVFGCAGTCASVNCEPGMYFIPDDENVSSATCQATDKPPENLMSVWQLHFFYLFYLFYLFYLFYLFYLFYLFYLFYLFYFIDFIDLFILFILFILLNFLNFLNFLNIFNIFILLNFLNFLNF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 608
Sequence Mass (Da): 69315
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A0A377TSZ4 | MKEIKRRNAWIAFSLALVVFLAGVFVINWQLWHSDQATHVAAARQAAKKISAILDEAHAATATALNVSRSGCSGQGQFQLGTEAALQPHLRTILLIKDGQVWCSSLPGNRVLTLHPESLPDEKLQLLPARMMVNKRPVLIYHTRSAQVRVIVSISDIHLRDALYSDEDNAGLALSVNHQMIARYGDVGPLKASPHQDIFSSPDYPFRIIYPESPFFSPSRLFQNGFGLLIFIFSVSLLFYFLLRKYLNVYTSEEENLRYAIAQGYIVPFYQPVVNGKTGEIYGVEILARWKNATTQRRSPAEFIPLAERTGLIIPLTRSL... | Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
EC: 3.1.4.52
Subcellular Location: Membrane
Sequence Length: 327
Sequence Mass (Da): 36648
Location Topology: Multi-pass membrane protein
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A0A378A8N3 | MPTISRKEYASLFGPTVGDKIRLGETDLYIEIEKDLRGYGDESVYGGGKSLRDGMGSNNTLTRDNGVLDLVITNVTILDAKLGVIKADVGIKDGLIVGIGKSGNPAIMDGVTQNMIVGLSTDAISGEHLILTAAGIDSHIHLISPQQAYSALSNGVATFFGGGIGPTDGTNGTTVTPGPGIFARCCAQWKGYRSTSDCWVRVTRLGVLRWLNRLLPGWRA | Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 23281
|
A9V3Z2 | MGNTPSFDPVREMCVQVAPATENSSYTVRHRNFKDRLIELPFEDEPDINTVWKLWKRGSVKFAKNDCMGIRSYLPNGKRGEFEFETYEEIHAQVEQLGGALDKLGVKAEDAIGIFSINRPEWMKSFMATMRQGAICVPLYDTLGPSAVTFILGDAGVETVFVSKENFDTLIENATEAKCVKTIIVFDPVTDEMRKKGEDAGFTIFSMDEFAKTCDKPGEPAERTTEDLVYYMYTSGTTGNPKGVRLSNKSVLSNVGAIIGIGIRLNEDDVYLSYLPLAHCLEALLQLTGLGFGASVGFYQGNIRLLTDDIMTLRPTIFAG... | Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.
EC: 6.2.1.3
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Length: 668
Sequence Mass ... |
A0A4S4L1P0 | MYTAAILSTLVLSAFSFVNGHGYVQEVVADGVSYTGYLPYSDPYYNPVPERIIRAIPGNGPVTDITLIDLQCNGDSADGIIGTSPAPIYGTGPMITYMAAAPEGTNVTAWMPGIEAVWFKVAEAGKTAAGLWASTDILTENDSIYTFTVPTSLKPGQYIIRHEIIALQSAYVYPGAQFYPSCIQLEITGSGSAFPTSFVSFPGAYTPDTPGIAFDVYTNTSSFNFADFSDSDVWPSRAQLDRHLKRPRAYVLRKTCTAAACMTSSENSKVEFELWTLDSVSYGTAVVLAVAVLARRKGCSRDRNESNQETATKVREASVG... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
A0A061D2N6 | MSPRYRLIYMFSQASSGCRGALRFAARRCSSTTRCNVCANRRRLVEHELLDRSSALWTFLLDSAATDLPPNDCSSMSFVVGSRVCSLWRCVGSSRAVRLPAGVSSSTVWLHVRRLSTTKGELPIESAPVDSTASTRELDRKPAGGESELTLPRDGTPLRCTEDQWLYKPTSSEVDLFRNSTLLPPRPIDVEGSVIVRLVDLHSGVTSPVGQSVLYSEYGIRRGELLRFMLFGSFLISVFCSLGYWQLRRRAWKVDILNRRREALSQPLVKVESFAQLEKALGASDDPNSLIEYRCVECTGVLDTSCSMLVGPRPSLYESY... | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 549
Sequence Mass (Da): 61197
Location Topology: Multi-pass membrane protein
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G9MSF3 | MEPIVHKASLHATQPAAVKTDPSMSTEPKETIKGDGESSLPERNKGQPLNSANPVAMDDLEATPNAYEQADTPPDQETDYESSDSSVGQGFNNIRLPYVGMGGGFDIYRAAIRLGTDKVTKFTTRQIGTDNQKQFIPINGRELLLYQSEKRVGVDLQAFVCLNRMKSPTQGSWRLEMRLLFDARSDSILLLNANKHMPVSRQDIFVNELTASPAKPPIAVELHQSLALRAVSHRIVWLGEHIFDIDVFPRRYLSLRTPNYEPVKTGAKRAFEPSSSSPRAGPSTAKRARAETSDGLTARTTIYTMPPTSEFCAESCDTAE... | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
A0A7S0BVS2 | IETVKAEGHHFSELNWKTIGVVIFNAKSAKKYHEFLDSIPLRVVKILYWREAHYPSITPDIQAKFDIIMGTQFTDAVSNPCHYPYGFREDNILPVVDVPFVKRTHLAVHISSRCYGKDGFRNNFVERLGELMDVEFYGKCYTNEYDLRVPDMHASREKMKKFYSNFKYYIAVENTGTNDYVSEKIFNGLGSGAIPVYLGANNIDKFPKLDGHSKWFIN | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 218
Sequence Mass (Da): 25239
Location Topology: Single-pass type II membrane protein
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A0A3D8GS89 | MTKCTPDMLGICLPFMLTRMVLLHIPTFDRLTIDQLKKEKLAVIVHANPDNFGNIPDRYQTDGKPGPDEATLKTGDAGDRQACGVILSTDEDNK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 94
Sequence Mass (Da): 10386
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A0A3G9IZ18 | MLMNNIKLATDQRDNEIAQIQNLIRNMGKLDIPVLCYNFMAHFNWIRTSLAVPSRGGALVTGYDHTLMKEAPLTEAGVVTEEQLWERLEYFLKKVVPVAEEAKVKLSLHPCDPPLSPIRGISRIITSAAAMKRAINLVPSEYSGVTFCQGTFATAGEDIPALIRELGGLGKIFFLHFRDVRGTPEKFVETFHDDGQTNMFEAIRAYKEVGFDGPVRVDHVPTMEGEYNLDPGYASIGRLYALGYLKGLLEGAGYQY | 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: 256
Sequence Mass (Da): 28532
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A0A2N3NCZ1 | MAEKDDWSTDANEALSISLWQPTNDGPELVGRPFHPRFTYPIFGDEQQIFGYKGLEINLKYCSSDMRPFLEMKYKDKFQAIGDTEPCDVLGELKKHLPPVAFGTEPDFIESTLQLAVSDSWKPAGELYTTIQDATGTYEVWKGNLKDPAIMQLVKRVQILVLLYIDGGSKIIELDAETGDDRWTVWTLYKKQDDDYIFIGYSTVYHFYYFDKRITPVRDPSAQLELPNGNFDLAQLDRRARLSQFIILPPYQSAGHGQRLYKTIFAHHYNDPQTKQFAVEDPSEAFDDLRDLCDLDFLRSLPEFRDLTYQPGVKIPKEGA... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subc... |
A9USP7 | MSEFSSDAAAPWATTEGSSESWADSPFPALEDQQQASATTDSGAKKTAQADKEAGENKGLDKLAADLGDALDTDKESKSAEAAETAKDAPPAAAPSFSSKLLIDVEGVDLDIQRSDKSSPLYSALTFEDVGKQPDTLPIREQVLINCYAKGFKQPSKIQSAALPILLRNSPELGRPENLIFQSQAGTGKTAAFSLNLLTRCDPSIKLPQAIYTAPTFLLCQQTLKTIDELAQDTGATRLNTFNGTTAPNFTKGKITQQIVVGTLGRLANQAVGAPRNRQFDFKNIKYFVIDEADDLLAKPNSRADIDKIMGKLDKNVQVI... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 538
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): 59032
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G9MF82 | MYRAALRTASRPAVSGLRTSLVRTAPRRFASTAPADKARSWKSSAVRWGLAVAGVYYYNTSSVFADEAEAHALPVPAPYTDNDLPTVDALIEKKRKEVSPKPVEVVATKAETPKTDAPKTDAKSEAPAQSAAGFGGPEALEEEASQEGAFNPETGEINWDCPCLGGMAHGPCGEEFKTAFSCFVYSTEEPKGMDCIEKFQGMQECFRKYPEIYGSELEEADNAEAEGSDEAASAAPAAAVAAPEAPEAPVEDRQQLREDSPAKSRNSDGAETDNLPGVKLVENSAPRVTEDATEQKKN | Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondri... |
A0A8J2YTN5 | MIPTSTWPKGGAPLWRVALEAPDEFSAEGFAQVLEALGGAISAFETEPQGPWKVETFVQGKPDLAVVEGGLALVALQFGVVQPAVTLEQLPDVDWVRQNQESFPPLHIGRYFVYGSHIVEPPPAGTIGLEIDAASAFGTGEHATTAGCLLALDRLAKRGPRRRVLDMGSGTGILAIAAAKTWHVSVLACDIDRNSVRVAAENVVTNGVQHLVVSRESDGYRAAAVSAAGPYDLIFANILARPLAKMAPDLAHHLAPGGIAILSGLLARQETYVAAAHRNAGLTFKGRIPRAGWHTLVFEKAWP | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 303
Sequence Mass (Da): 32138
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A0A7H1N029 | MTADAIGDASDFWVFGYGSLMWDPCFTVAESSWGIVRGYHRALCILSVRNRGTWEQPGLALGLERGGSCRGRIFRIPPDAVATARAALWAREMPNEAYVPRLLSVRLDDGRRLPALVFVARPGHPQHVSHLPPSAAAIMVAEGRGQYGTALDYLRNVVAHLDGFGIADGPLHRILSLAEAIAGDAATG | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 188
Sequence Mass (Da): 20230
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A0A507BWF2 | MRGAFKLNSAILKRGIIINNIVPFNSTTSRLPLPPSTTINHRIHSLPCNAINPTTRRLDSINRRDFTSSRSALTATTALNPVGAGTSAVDHPLSPKLTFDERQVFLNLNLPQGSVNFVITKTKPVSDLYANIAEEYPLAKSISIFKFPSEAQWAKSTPSEDILSQALLDRGLILQINNERIKVNVPTAEQRTAHLKTDLLTLEKELTVLETRRSDLDRLAERTSQVFVWLFLAGMCAQWGLMLRLTFVEYSWDIMEPITYFLSYFWVIASYAFWMVFRRDQTNDAMSNIAFTRRQMSLYKRHAFDVAHLESIRNKRDKIK... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A2Z6PDM3 | MALQHCFSHESKTIPNSMSEAENSNGCFDCNICLDFAHEPSDDSLGVDEHPQCPVCKDDISHTTMIPLYGRGGHAPPSAKSSHILYI | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
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
Subcellul... |
A0A7S0BYV5 | TKSIRLCLRAEQIMDDLNDKEKSHLHRMEGCHWVPEYGGWMIEATPNRPYTGFTNDLLRVERNMRLRRRRLVSVLRDNEIAPTVSTFPLLGALGDDGSVPATSVGGNITESAYIGDGIINSHPRFGALTANIRKRRGEKVTIRVPLYKDLETPEYKKMRTDEKGCDCESGSLQLWRYGKGDISRKRHGDNLLVVGCSSSEFPMGPSLNEEDTGEPITLEKWQVNVEIEGCLGLYYRSSPNIIVSDADWPRNGEFVTGIEVPDIPGGWVRLQNGYYLPIQSENGKIKFLHKVTPANTVSPSIVRNNSITSSTMPLVGGGGT... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 360
Sequence Mass (Da): 39803
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A0A1H8NYK2 | MRRSPGSPAHWPRHVIMIVVCFLMLVPFYWVIKTSLTGENIYAWPPRIIPVDPHLFNYVDVWYMIPFARYLLNSVIVTAMAIAGSLLFNVAAGYALTRHFPGRRWIVVLLLSCMLIPFQATIIPAYLVTSWLGVLDTWLGVALPLLSTIICIFIFKASFEAVPPSLIDAARVDGLGEWRIVTRILLPLSKSAIATNVILTFIWSWNSFLWPLIAIRSPDMQTLPLGLARFLSVMEDTTGALFAFVVLVLIPGLAIFLMAQKEFIRGLTSGATKG | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 274
Sequence Mass (Da): 30618
Location Topology: Multi-pass membrane protein... |
A0A1J5BJ96 | MAAAPDDPRAGLPAHRAAGFDRLLGIVAAATLFFIMALTCADVAGRYFFGAPIPGGFEITELAMGALIFTGLPLATLRGQQVTVDLFDAAVPRALRAGRDFAIHLLAAACLGALAWRLWVKAGQMVASGDTTATLHIPVPPLVYYMSMQAAVTAVVLLALALVRETPRQA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 170
Sequence Mass (Da): 17800
Location Topology: Multi-pass membrane protein
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A0A159V830 | ILIRAELGHPGALIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLASSLIENGAGTGWTVYPPLSSGIAHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSIGITFDRMPLFVWAVVITAVLLLLSLPVLAGAIT | 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... |
A0A089LCV0 | MNIIPTMGNVDTIESHNTLVENLMNSSTQIVRCCVSKASYDEHVEAVNYVRNEFKKHTNKDLQLMLDIAWPKDKKRIWIESEQQITGGETVYICISENEISNDKKIIVDFDCSLFNVGEEIYLGNAEIILTVTQIGDNYLQCVANNDGLLKSGLGIASKQGFIKPSAVDIKEKCVKLIDVLRPECIVLSYIETSDDVIEFKELLLKHINYNPIIMSKIECYSAIKNIDAIIDVSDEIMIARGCLAVNVGLENLLFAQDLTLSKCIEKNKRCCIASNILKSLSSSYAPNRADICDLAHMVKEGVDNIVITDSISRSSRYKN... | 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: 333
Sequence Mass (Da): 37459
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A0A377ZLY2 | MPVKAIWADPKELHDAGGVTLDTRWKALADALNMPLDQLATRINTNPRMRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNFAGTAKDTMRNRAITDVFEPGSTVKPMVVMTALQRGIVNENTVLNTVPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alani... |
A0A293LVF2 | MTVQKGKQGTKGQKQIVEENKQTIKFYAVMAAGATGFYVIAMATIFSNSFTTFYWVMAAFALLVYGGCLQAMRHMAKSCYSESGQLLDGGIDLNMEAGIADCCSSYFSDLQLLLVFMATCSRSSRLPPVGEYPWPVVFPATCT | Function: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 143
Sequence Mass (Da): 15622
Location Topology: Multi-pass membrane protein
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A0A2A3XEH4 | MNNILFVHASPHGKYALGYRLAEKILAEEMLINSRVSLIERDLLTAPLSPLTHRYASALVSYNIGDSPNADLTESEQMISELEQSDRLLIAMPMHNFSVPAALKLWIDHVVRINRTFIASVEGKQGLLQDRPTTILVSAGGILQGGNPQPDFLTPYLTLILNTIGIQDIRFVYLQGLAFGEPAITQAWHQAQAALVEVGVLTNPLP | Cofactor: Binds 1 FMN per subunit.
Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
EC: 1.6.5.-
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Length: 206
Sequence Mass (Da):... |
K5XJ85 | MTPQTLMNDLTSENCDVMDIVLLIVDEAHRATGDYAYNQIVRHMMAKNPHFRLIALTATPGKDTEGVQNLVDGLHISRIEIRNEESIDLRGYMHDQNVEQHCIRMPEGIAAIRDALEQLMETFMKPLQSMGIIWPNQQAVKLHPYAARAKISTLAPHQRGFVHQLSMLGNLAQVMAYLLEATVGMAY | Function: ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at ... |
A0A2N3NJC2 | MTTDDEGSRRILNARIRRIDLACKLLGPFVIASIDDFSTIVAIWTTLILTLLSVAPEYICIAQTYYAVPALGYRSAGQLQSEPDESEETPLLHNGLPTPNATKSEHPVFSWVRFLLSSIFPISSIRFYSQHRAFLPSLAYVFLHLTVLSFSGRMIVFLLSIGYSSLAVGIARTICTFVELSATWTTPKLIERAGNVMAGFYSISLQALCLTFGVACFIVDWNGALQTHDGAMLGAGGLILGVIFSRIGLWGVDLTTQIIVQDEVEEEYRGAFSTAEASSQNLFEMMSYVSTIVYYRPEQFQWPMYLTLASVYAGWLTYAI... | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 333
Sequence Mass (Da): 36986
Location Topology: Multi-pass membrane protein
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A0A1V5QLC2 | MRSLILPLLLALPLAAQTAPKAKAKARPQAAPKAAPAPAPEPPPAPEPAPAPKAKPRVKLETSYGPVVIELEPDLAPLTVENFLRYVKEGHYAGTLFHRVIPGFMIQGGGMLEDMSEKPTRAPIPNEAPATFAAGLKNLRGTVAMARTDDPNSATAQFFINTADNASLDHRSPNAEGMGYCVFGRVVEGMEAVDRIEKVRTGWRKGHQNVPEYPVRLKGAEILPAP | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 226
Sequence Mass (Da): 24219
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A0A559QN81 | MPTGTSLHNCATKCLAVLFVFLLIPQAYAQFGLSSSTDFYTIDTGAGLVFKVRRTDNGVSTQSAGDIASLTYNGTEYQNQSRGSQINSGFDWLYDGVSAVSVSAITVGSDYIKVTVNAGNLTHYYMARRGYPHIYMGTWFSAEPSVHGQVRYIMRLDEGLLPYSPEPSDLRGVVSTIESGDIFALANGETRSKHYSGERLKDWQFFGANSGYVGMWFVRDNQEGGSGGPFYRSLKMQTTDSNQELTYIVNYAQAQTEAYRTGILNSYTFVVTNGSEPGTIDTTWFENMNLLGYVGDSGRGRVAGVGINNRDSNYEYTVGF... | Catalytic Activity: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end... |
A0A293ME06 | MVERGHFEDLSKLFGLINVVPPEGEKRRRQNFVFSATLTLVHDLPKRLKNKPRKQKLTEKDKLEQLMRKIGVSAKPKVVDITRKLGTAEALSESRIMCPSPEEKDSRLYYFLLAHPGRTIVFCNSIDCVRRLRSVLEHLNCRPLPLHASMAQRQRLKNLDQFRTNPVGLLLATDVAARGLDIPGIEHVVHFQVPRTAEVYVHRSGRTARAQNVGLSVMLVEPKELPMYRKICHTLNREEALPEFPLDIDILKSARERVMLARKLESEEHKIRRRNYDNNWFQRAAEEMDMEVDEILLDKRGEKEAADDRRKLTVMQAQLA... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 405
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): 46841
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A0A507CBB5 | MSNQHDEAVLLFTQFASIPSYSAASVITNSNGSGITISLTSTIRDIERKVKRKFQTVLSATLSADGKLENATSGYPVDVENVSLESTSTSGLLCCARSIVEKDSKKKRFIEIFNKTSMLHQIDVTDRHGEFYNDGEMRIYKSNALPFLTSENLETFGALSWSPDEHHIAYVAEKNRSTDGFQKFAYEPDFGEGYTKKAPPVIVVITLPSCEVQVRLSPCAVGQPLFLDNDKLLYLQVPTQPINYGIRFCTNRIMNLATISISSQEIETLSTPSGFNARYPRITPDRKHLIYISNRVGGPHNSTCRIMKSNLVDGKVGSAQ... | Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
EC: 3.4.21.-
Subcellular Location: Cytoplasm
Sequence Length: 648
Sequence Mass (Da): 70938
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A0A507C919 | MFFLLRYSRALEEGSFRNRTADYVWMLLLGAISIVIITPFTTPRASIPFLSSPLTFFLVYVWSRRNPAVNMSFLGLFTFTAPYLPWVLLAFTVLLHNVWPSGDLIGMAVGHAYYFLEDVFPRMEGHLDHRPLATPWILKRVFGDLMRDRADPTLPEANGGVGVVGLPAVDGGAGNDEPEQQ | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 181
Sequence Mass (Da): 20305
Location Topology: Multi-pass membrane protein
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A0A2Z6LV87 | MAEQPVVTLPESVENLIKIICEKQNQPPPDHFPRQQLAMIGEQRALELLTIISNTTIQRSFNGYIVYLIKNGISPPKPSPPSSSEASPLPLHPPEHFPPSSLSESSMSSSLSQFPLHPPPYCVLTALGELEFRKSFLLLSYAGEKNIENVVTAAYIETLKHLTMRDFENEIWEAVGKYNVKCVDRQLYLDRDSGRTHIYQCYVSPSGSLRFKGPILQYTRTHLQKSLGDDNVLVVKFADVGANSKNISAQEAAKLYGKFGKEGIRVGHRLYRFFVFKDGGKEEKKKEDQTTSSKSYNSSVKCYFVRTESRCSVDQMQDYI... | Function: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 983
Sequence Mass (Da): 111617
|
A0A6J3DT29 | MLQVPLPLDRDGILLRLPFTRLAVGTVCCPLFGFLFCVTWSLLFHFQETTATHCGVPNYLPSISAAIGGETPQRYVWRLCIGLHSAPRFLVAVAYWNHYQSCHCSHPRYPRLCHFNLLLNLLENFALLVLTYVSSSENYAIHENAFIVFITSALGHMLLTCILWRMTKKHTVSPEERKSYKWKQLLFFFTFITFAFAVCVYFHHNWYCGPGVYTIFAFLEYLVVLSNMAFHMTAFWDFSNKELVAGGTLSGDPWPTSPTRAHGPEGAAKLRGAPTPRLSGRTPRTERSERGRAGHRLQRLGLIQAPRCCCGAKLPRAELE... | Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface.
Subcellular Location: Membrane
Sequence Length: 333
Sequence Mass (Da): 37700
Location Topology: Multi-pass membrane protein
|
A0A354DG36 | MVAAFFTAFYMFRLFFLTFTGPEKVPQDVQVHESPKVMTYPMIVLAILAVVAGFINTPWKPALGDWMTQGMSFAHGGHESAPFWVTILAVGISLLGIFLSWLMYGKRSISNGNTARAFGPLYTLSYRKYFIDEIYHAIVVVPLRALGKVADLFDRYIIDGLVRLVASFTYGVGAAGSRVQNGQVQGYGAMMLVGLVILLITALVAGGLFVS | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 211
Sequence Mass (Da): 23088
Location Topology: Multi-pass membrane protein
|
A0A0B4UZ05 | LYWLSKSGNAYPVLNVTMPNNDNFDKLYIWGVHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGQSGRISIYWTVVKPGDVLVINSNGNLIAPRGYFKIRIGKSSIMRSDAPIDTCVSECITPNGSIPNDKPFQNANKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAKAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIY... | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... |
A0A2Z6NGF4 | MPQFGCSIEKLISVTPDDYRCPISLEIMLDPVTVSTGQTYNRASIQKWFEAGNMTCPKTGERLISTEFFPNLALKNLIQQFCYDNGISILTNKSHSITATTVSPGSLAAAHAIQFASWSLARRLVFGTDEQKNKAAYEIRLLAKSNVFNTACLVENGTVPPLLDLVLTSTMQENAISALLKLSKHSNGREVIMESRGLKPIVKVLNRGYSLEARRVAAGIIFYLTSVKEYRKLIGENSEAVSGLVKLIKEGTIRGKKSAVDAIFGLLLLAKNHSKVLASGVVPVIINVLASSDKRYVVNDCLAVLVALAESVEGSRAVLE... | 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: 420
Sequence Mass (Da): 45805
|
A0A919HSM5 | MAPVGAVVTAAVILDPAKPIVGLNDSKKLSEKRRLALFDEIKEKALCWSLGRAEPHEIDELNILHATMLAMQRAVAGLSIVPEFVLIDGNRCPSLPMPSQAVVKGDSRVAEISAASILAKVTRDAEMATLDLAFPHYGFAQHKGYPTAVHLQKLQEHGATEHHRRSFGPVKRARPGVQLSHRDLKMAEPRFVHLRVHSDYSMIDGLAKTGPLVKKAASLGMPALAITDFTNLCGLVKFYGRDTARGLSRSSAPTFTCSATCSATNLPS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A319D789 | MWNAYDKKVLLVTGGTGFLGTTLLYRLLTEATPARVYVVCRGGRKRAFERWLEHLPMTIFQPVFQTANSIAVLDGDITQPRMGLSESDWKNLENSVHIVVHAASSINLMSRLPAMSKSIIIPTVSLAGLALDFVNLERFVYISSAYSNSHLWKPQAPATDVAVREKMYPLGGDTEDWAQSTLKAWEEIQARASSTEYESQDLFPWAYGYAKHLTERLLVHRFSEAGASDKLLIIRPSIMGPACEFPFPGFCVPSSTPFFTVTAMIIPDPGREIVFNSRLQDPYHQATLDEVPIDVVADRLWAHLALGTTEFVHAVSGKSH... | 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: 428
Sequence Mass (Da): 48451
|
A9UTB9 | MAQRPHGLKLSRGQRRAEPHGGVGGPPLTVRDQEPILIVDEDEDGGDDAGSAGGLGGSTAMARARAKRPAAMQAARRGPGVSEPPPQRSRSAPSSQSAHGSLPRPTPVQAATSLTHIPTPSSGTAATITTTPLRRRRASVAEMLRSKERPGRLPACPSCGVHMHLTALHRHLDACLSKHATPPRPATPPPSATPINWAPQTILYSPDTCARLTRQRPPLAACLTPQRLDFATEDREPATTPDSSASQEIRQPPASPSELAERASACFLCGEPTHFARVCPQGPYYVYYFCREVSAVLQHSYFCTLFTPAERAQLEAICAL... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A2Z6MTS1 | MIDVAEKIKIFAKQNEFVWIAGAIGSLYEAEIGQEQKDLILQGDYDIINLGGLFTAPKNGNPMTGQLSITIAAAGIGRVYGGAVLGPLIAQSVVQIITAFIWNSVEDGSEEQDNDI | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 116
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 12382
|
A0A7L7LFE1 | MTPRQKELIKATVPILKEHGVALTSHFYKRMFTHHPELKHVFNMGNQQSGKQQTALAMAVLNYADNIENLSVLRSSVTQIAHKHTSLDIRPEHYAIVGKHLLASIGEVLGEGATPELLEAWGVAYGQLADIMTGIETGLYKGATAKEGGWTGWRPFLVKQKERESAEITSFYFYPADGGRVADFQPGQYVSVRLFLPELNLFQPRQYSLSNAPNGEYYRISVKKEAGANLRPNGLISNRLHDHIEEGDIVEISAPAGDFILNTSKSGPVVLISGGVGQTPLLSMLDYLISTNSPREIVWVHGSRHPNVHAFKDRIEALHG... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate
Sequence Length: 403
Domain: Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Sequence Mass (Da):... |
A0A4Q2LLF5 | MAIALIAAVDRNNLIGDHNNSLPWKIPEDLAYFKEITSGNVVIMGSRTFNSIGRPLPNRVNIILTRETNTASNKYPECHVVNSIEQAISLCQKSFHNKKVFVIGGADIYKQFLPFADYLYLTHINHSFKGDKFFPDYDHDDYEISSYQAIYKEDTKSYDLIFGVYKRVKK | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A293MZL9 | MTKKVAMPAEVREPLMVAATELSIDESGLQRVLPRCLRFLFADVDAERLYQEYYSHEKRLDLKAWLCTALCVDAALLTAYAISGQGPLPLSLLAAHALVVVLLLALALRDLLPAGPLTAPPALALAAAQLAADAFLYESREAAEALPWLLVHSFAAYALLPLRVVGCWLAATALCGVYVALSLPSGSVLMAALLLCIAAHLLGLASFLFTERLQRRAFLETRRSLEVKLVVEEESQEQERLLLSVLPKHVAAELKQDLDAVVTGPFKKIYMSRHENVSILFADIVGFTAFSSTCPAPELVRTLNELFARFDKLSDKYHQL... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 478
Sequence Mass (Da): 52103
Location Topology: Multi-pass membrane protein
|
A0A1Q8UQ51 | MAVVPAVNLPLRALKNGDLIILYDDLKTNMANLIGLAEHVSPEKVNFMTKIGQGLTYVCITEEKAEQLLLSKMIERDQLEETKSFTISIDFKDTTTGISSIERSDTISAMTRMEYQPSDFKRPGHVFPLIGKRNGLLDRIGVTEALIDLTKMITSTHVGYMTEILNSTGEIASYEEIEQISSAYDIPILSISELIIMKQDEFIQLLEGTVVDGRKIGRKIGFPTANIELIGNNIALPRGVYGVKVFHQNREYLGVMNVGKRPTFTRNSNELHYEVHILNFNEMIYGQALDVKVCFYLREEIAFPSFNDLIAQINRDIDSV... | 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.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Length: 330
Se... |
A0A851CC93 | GVGLSIHGHFRVATEKTLFAMPETAIGKLSGKIGYYLGLTGYRLKGRDVLKAGIATHFVESDKV | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.
Catalytic Activity: 3-hydro... |
A0A097ZI16 | PMTTTPTKSHFAHLRGTETRGKLCPKCLNCTDLDVALGRPKCTGKIPSARVSILHEVRPVTSGCFPIMHDRTKIRQLPNLLRGYEHIRLSTHNVINAENAPGGPYKIGTSGSCPNITNGNGFFATMAWAVPKNDKNKTATNPLTIEVPYICTEGEDQITVWGFHSDNETQNGKALWGLKAPEVHLICQRSDHTLRFTDWWLPKS | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by med... |
L0DV48 | MRYRIKICGLTDLSQALNAAASGADAIGLVFYSRSRRAVTLEQARAIVSVLPPFVASVALFVDPANADVEAVLKTVHPDFLQFHGDEPARFCESFGVPYLKAVAMAEHADPRPVMDAHPRARGFLLDSHGNGKIGGSGERFDWASIPAALERPWLLAGGLDAGNVGAALAQTDPYGVDVSSGVESAPGQKDAARVREFVQSVRQVERERNETGD | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 214
Sequence Mass (Da): 22870
|
G9MFC1 | MSFSTPTATLANGQPSANPGSVQQVRQGQTNGGLVLLSDTQTIEVLAHFARERIPERSVHAKAAGAFGEFEVLDDISDLTDADFLTGIGKKTKLLTRISTVGGEKGSSDTVRDVRGWATKFYTEEGIQDFVFNDLPVFFIRDPIKFPSMNRSHKRHPQTNVPDNSMFWDFHKNNPEGIHALMHLFGPRGIPASLRNINGFSVHTYTLNKSDGSYVYVKWHFKPEDGIKNMDPKVAVRLAGEDPDYHVKDLFKAIERGDYPTWTVNIQVMKPEEVKTAPIDIFDCTYTWPYEKYPLRRVGRLTLNKNPNNYFQDIEQACFS... | Pathway: Alkaloid biosynthesis.
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
EC: 1.11.1.6
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Length: 488
Sequence Mass (Da): 55208
|
A0A328SLS2 | LSGQQDNHIIESVERIVDNWGGDFQVEYDKNYMRVIRQHKENGFEVIHLTMYGKQVCDVIPDIRDNGRDKLVIVGGAKVPTEVYEESDWNLSVTNQP | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.206
Subcellular Location: Cytoplasm
Sequence Length: 97
Seq... |
A0A2Z3H0U8 | MEPTQSLGPTSPPEKGPGNEVPGAAPTRRHNFPKEEHLCRKKLIDELFGKQSSSFGVYPLRIVWLPSEGPTGAPPQVLISVSKRGFKRAVDRNRLKRLIREAYRLNKYQLLEHPGGHPVGVLGIIYTGKEKSALPLVEKKLISAFHRLLGTAVSRPASPPAA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A507BXP7 | MRYSWPDENTRKEMQVKETFHHSANAVTYMHDKIGLHRIANLTDKPAISLHLYTPAFDTCATFEEGTGKKRQCGKCTFYTINGEKVERTYSTTSSNDEAGIISTVTDITTL | Cofactor: Binds 1 Fe cation per subunit.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 111
Sequence Mass (Da): 12568
|
A0A2X1QGU1 | MYLVGFLFGLGFDTATEIGVLGISAAGASSGISVWSIMGLSGRCSPAVWRWWIRLIMC | Function: Efflux system for nickel and cobalt.
Subcellular Location: Cell membrane
Sequence Length: 58
Sequence Mass (Da): 6212
Location Topology: Multi-pass membrane protein
|
R2PUS5 | MSILLIGFMGAGKSTVGRLLAEQLAKPFRDLDQLVEEMTQKTIPQLFEEGEAVFREAETKALMAALGKDQVIACGGGIILKEANQALLQAHPQVVYLKGQPDALFRRIQKDEANVRPLATEKTVAEMQEILSPRLPLYQSAASIEVETTGKAPQEIVQEIVERLEL | 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... |
A0A372BZ04 | MQRVLILLFGIVAYLVFLPTFLYFIAFVGNLQTTALVEHIPALAWLVPYSVSFGRETGPVGLAVVINLSLIALFGVQHSVMARSGFKGWLKQMLPASAERSVYVLISSLLLILLFWQWRPMGPVIWSVESGTGQAVLWTLFAVGFGITFVSTYLIDHFDLFGLKQIWSQFRGRKAQPPRFVTPLFYRVVRHPLYLGFLLAFWTVPHVTLGHVLFAGGMTVYILIGVQLEERDLVRYLGEDYQRYQKQVPQLVPVPGRTWRDDETPEGSGASGRA | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 30906
Location Topology: Mult... |
A0A845XW21 | DVGSGRPGEVVKIAKTIGPIIQTGKGMLLLQQVQLAGKRAQSAWDFANGMRLEVGEVLGNG | 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... |
A0A6I2GVM2 | MRTTPVPMALPLTAMLGPLRAARTRTEVLGAVEEVVCQLVGCEEFALLELDAASGALVVAHQVGLKVGSGSPWPTARGLIHQAARAGVPYIAGRSFGGEASSDEWNLSGCVPVRDGTRICGVLALFRLLPHKRQLTQADADLLSLLAQEAGRALKVLEPAGAPQPLAAAAPVRPPLAALPRAAAGTFVGTAHTLVPAAEPTPSLVYLHPGELYSAAAASGAVEVSTILGSCVAVCLWDSRLRVGGVNHYLLPTSPGGPDAAPHRYGDGAIPALVDALQALGSRRSQLQAKVFGGASVGAGPGAAEAANGVGARNVQQALR... | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 360
Sequence Mass (Da): 36516
|
D9SKH4 | MSEKNENAKKGGFSKILIGLLLAIVLVGAAFATAYFYFTKSAEKVTQKTVHPLAHQVTYSLDEFKLNLSEPKTYIQTKISLGYDGGEESEEFAKELETKKTIIRDAVITLIRTKTNTDFTKEGTETLKIQIINTVNPLLEKGEINHVYFDSIIIQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 17392
Location Topology: Single-pass membrane protein
|
A0A559QKU4 | MKIVVDENIPLADELFASFGEIVKLPGREISVQDVRHADALLVRSVTKVNRDLLDASKIRFVGTCTIGTDHLDKNYLDSAGIKYASAPGCNAWGVVQYDIAAMDYLGLFNTSLKVGIVGCGNVGGRLYRTLKALGFKCCCYDPFLTAEQIPDLTDWQALFECDIVCVHTPLTYDGPHPTYHMIDKEFLGVLKPGAVLLNAGRGEVVDNLALKKYLQSNNAKSLRVVLDVWENEPAIDAGLAELVDLATPHIAGYSFEGKTNGSLMIYEALAEFLGVEQLQCDATVRDVKQRTYGTPELLQVGTLSDAIRGSYDIVSDDKR... | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phos... |
A0A2N3N9E0 | MDGDYEYNDTNRAFLQALMGRGFVTFRDAQEIIAGLRLAAGTEDVKLEHITQHDVDYYINSASDAVSQFDYQVRSAVHQANATRVWALVNTTSDPSTQLATTFTPDELSFVKRVFDAIFDTYNTPRMEKMCVTMQEAISLSRPPRNANNPNTSINDGDESQAVSTDKGLRHSDVNRVIEELVEGGWLEKSPEGFYSPAPRALMELRTWLLDTYNDPDVPADEWQRIKTCEACRDIVTYGYRCNDRDCLVRLHDSCEERFWRARRSKTCPKCGKAWEGNRFVGERAVTTTKTYRQARGRGRKSNTLASDIFNDAQGGGLGN... | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Catalytic Activity: S-... |
A0A377WC43 | MFIKPKYGTENLMSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLTGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAAEQIDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFHAVDKAAVLAKFGVADVNGPVSLVIWTTTPWTLPANRAISLSPEFDYALVQVDGQALILAKDLVESVMKRVGATDYTILAAVQGSELELMRFKH... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A9V469 | MLDVVEHLVGYARQPVTVGTAWHQLWEPSTFQWQHGQTPLSHIVVVVAALVAYVVISFGLRAWMRSRTPFGGPIFKAFVVLHNATLSGGSAIMVVGCAYATYEQYRLGQYDDLVEGALCDSKHITEQNNAVTNTHRWWLYVFYLSKFYEMIDTFILALKKKDLTFLQMYHHAIIVLLCWSWIDAKFFLAWYAMVVNATVHTFMYYYFGCQALGVRVWWKKWLTTGQLVQFGTVFMLLVVYMRVGFVQVEYGSAYPFLRVQNRCQGEAWAPIFSQLINVTFLYLFGELFVRLYHHKPTSKPGRAKKD | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 306
Sequence Mass (Da): 35466
Location Topology: Multi-pass membrane protein
|
A0A2Z6M3C9 | MGIVAAIGVLSPFPFYYYLWNWPQSWVDLCGKGRDPSKIMAYVAHLLKIIQFISLFFVSSFHWPPPFYFWPLFAFGQFLNFRVYQLLGEAGTYYGVRFGKTIPWVTEFPFGVISDPQYVGSIMSLLGCLSWVPYQYILLWIIGRENEEATICSFLVDASLVLSQFPFYYYVWNWPQSWVDLCGKGRDPSKIMAYVGHVLKIIQFISLFSVSSFHWPPPFYFWPLFAFGQFLNFRVYQLLGEAGTYYGVRFGKTIPWVTEFPFGVISDPQYIGSIMSLLACLPWVPFQYILLWILGYVFMIRVESKEDESTRAKPLN | Pathway: Lipid metabolism.
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Catalytic Activity: 1,2-diacy... |
A0A2N3NIL3 | MRSSRYSVAISLDGYIGPHDHSTAWITDDASIDFAELYSQFDIFIMGRTTYEVMRAQGDANPFRTRPKESIFVVSQSMRPSEYPEVTVLGANFLSEIKKLKEQEGKDIWLFGGGQLLGSCLDAGLVDTIEAAIMPTLLRGGIKMVSDAAANPGTLGTKLELVEVRRLESSGILMTTYKVRYH | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
EC: 1.1.1.302
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrim... |
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