ids
stringlengths 6
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stringlengths 16
1.02k
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stringlengths 117
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A0A7R8W9K0 | MNLAQIICFSSICSRVKKRFPTSDHLVEAGIMTSAEQKILENIEPKNVCKYWVPIVWASAVVECGRRENRIKSAYAHEALIRRITDFRTGLGTLLGYNTMSLPLLYSQTVTIGVYSYFVASGIGNQWLDPAMKYPFNEIDMVFPFFTFLQFLFYIGWLRAAEVMINPFGEDDDDFEINTLIDRNLTISYTIVDEMHHQHPELVRDAFWDVAPEIPHTIASEQIPEVTNLFVGSAENVEVHPNEAIYGRLTSASSMSSVNSGKEEPIYGSLSNFRTSIRSLTKRIRGSKRSSSRRQRSVKSQSPQTPDTDNDVGGAPLPVLQENEDLETSADMAVLESQKKPNDDDQKCDDKDVV | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 39948
Location Topology: Multi-pass membrane protein
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A0A0N4UX02 | MPHCGRRLRSSSVTEDTVPSKQLKVESQGAGRQENVKDEEVSSDLCSICYEDFNFKTTLPDCGHSFCFLCIKGVALRVGSCPLCRNPVQPSLFERPSFCSSDHASSSAQVREQNPQPRTLAGGESTNYEGEVKWLYRSRGRGWWRFEPRQERDLEAAYSAGERIFELIIAGFPYVIDFDIMREYRKDLPRSTLWERAIKRIVEDGSSKGKHVYVVGVAGVKQKRDVEG | PTM: Ubiquitinated; autoubiquitinated.
Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
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: 228
Domain: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Sequence Mass (Da): 25849
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A0A951E0W8 | MPDLYRFCGPLLRMLSPESAHRLTFAALALGLAGASRAPDAPELRQRLWGLDFPNPIGIAAGFDKDARAPEALLRLGFGFVEVGTVTPHPQPGNPKPRVFRLKADGALINRMGFNSSGLDLVVDRMRRRDRGTGIVGINIGKNRDSADAGLDYVEGARRGSSLADYLVINVSSPNTPGLRDLQARATLEALLNKVLSARNISDARPPLLVKIAPDLTAAERADIAAVALETGIDGIIASNTTIARSPELLSAQAKEAGGLSGRPLFAPSTALLGEMYRLTRGRLPLIGVGGVASAEDAYAKVRAGASLVQLYTALVFTGPSLLDDIKTGLAALLRRDGFASVAEAVGADHAKVAEISIGRGSVP | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
EC: 1.3.5.2
Subcellular Location: Cell membrane
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Sequence Length: 364
Sequence Mass (Da): 38194
Location Topology: Peripheral membrane protein
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M1C508 | MQTSASSLQSLFWGKNLSYAPYTFSRTLDFIPAMTSPPLGPQRLSVQCGVGFRPCIDIHKGKVKQIVGSTLRDSKEADTSLVTNFESDKSAAEYAKLYRDDGLVGGHVIMLGADPLSIAAATEALHAYPGGLQVGGGIKTENALSYIEEGASHVIVTSYVFNNGQMDLERLKELSSLVGRKRLVLDLSCRKKEGEYVIVTDRWQKFSDVHLNEKVLNFLAEYADEFLVHGVDVEGKKLGIDEELVALLGKYSPIPVTYAGGVTVMADLEKIKVAGMGHVDVTVGSALDIFGGNLAYKDVVAWHSLQDSIAV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
EC: 5.3.1.16
Subcellular Location: Plastid
Sequence Length: 311
Sequence Mass (Da): 33687
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A0A5A8E0Y4 | MSGRKESRSVCGCCSYKEPEAEKDPAPPLSPKEGDRRCTDILCLLLFIIFFAGMIGLAGLALQNGDYKRVLNGVDYRGCICGTPSKLMNDGSCTEVEKGSAGSFVPGGSSMFGVPLAVPSSPDLSASTVVVCAPACPAAPVSSGPFEGVQLACYDNSSQTVFGTGATYSEQLDSLDSCPGTIFATTAPARSIAGYCLPKSAVNSNMTGLQMAVDKAVGAGTWASAVASLSQAWPAMLGLGFGALLISFVYLYFVQFCAGILTAVAIIGFGASLIAGGAFFILKANAIADSYDNVADSYSQDTNWQMSFYGGIALEVVAALYICIIVFMWRRIFLAVGLIQHAGKALRDVWGVVFLPVFFVPLTLAIAALWCATTVLLFSLGEIKSVDVPGVPSGTLRTFVVDDTIRYTLFVHLFGLFWATQFVQAFSELVIAFATTHWFFSPTVDGKRQIIPNTTLFACRTVLRYHVGTAAFGSAIIAIIRTLRAIFVYIYDKIRRGNKDSTFLRAVGCLCWCCFWCLDCCMRYVNRNAYVMVALSKQSFCPSTVMAFSYIARNFLRVGALTGMSTVFLFIGKLFVAGITTAIGFAVFTMVPMYADETSADYVASPFWPCLVIFGVSYTIGSLFMSVYAIAIDAMLMCYLYNEDWGFVDSESSAAIADLNSKASKEGSSSGAEYRDRGSDEVGERVPVAASDGRPTYS | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 698
Sequence Mass (Da): 74924
Location Topology: Multi-pass membrane protein
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A0A356L601 | MLVKSEYASPIGKLTLVASDNALVGLWIAGQRYHGDVSDIPFGDNAILQRASRWLDDYFAGGRPTVDFELSPRGTAFQCAVWRALREIPYGARASYSDIARRVGCASARAVGGAVGRNPISIIVPCHRVVGAHGTMTGYAGGIATKEKLLNWEQGVIRAK | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 160
Sequence Mass (Da): 17189
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A0A1A8V4M0 | MEDQNQESSDPVVALSLCDSTPLLWRAQDLRTVRSQSVVGALLGSLPRAPRQNLKLGRPLLLLPEEERLLRERHAAAFPPRNQDVERAEFQQQYEEEQQRSFEEQSVFALEDRKSALQRAMTSSQSGSGSGTSSDEALQRRLLDLDQNFTFPRSALAIQLSTTRAGLNYCPEARAFLQLDWPIRDQGNAQFDTRYLVFRDLWGRGFFLTSAGKFGGDFLVYPGDPLRFHAHFIAICLSLDEPVSLLDILAAARLGCNVKKTVLLCSPAPNGPVHYTSVQWSGMV | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
EC: 4.6.1.16
Subcellular Location: Nucleus
Sequence Length: 284
Sequence Mass (Da): 31811
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A0A0R3R2E0 | MASSLDYTTSLRWALGFIIVLSAAHFIFRTTLKKYFDEQMKSLYILFFNDDIISNCSARAIVEHHLHNYIDRYYSPEVINEYIERMKPLDGPIKKSDDSTHHSDQFGQEVFTNLMHKSKINIQSQPHIERKTAIICTIGPACGSVDNLKEMISSGMNIARLNFSHGSHEYHATTIKNIREAVQSFHQKPIVGIALDTKGPEIRTGLIDGSATAEIELKKGAKIKLTIDKAMASKCNANILYVDYENMPKILNPGAHVFIDDGLISVVVDSIQGKDIMCTIENGGKLGSKKGVNLPGTKCDLPAVSDKDTKDLKFGVEQGVDMIFASFIRNAEGVRTIRRILGEKGRFIKIIAKIENQEGIENKMWLIVLLINEGENVVMAFSADEIIREADGLMIARGDLGIEIPTEKVFAAQKMLIARCNLMGKPVVCATQMLESMTKKPRPTRAEGQLTIRDSIIQWLYFARFLLPKDFAKNSSNLLHY | 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: 481
Sequence Mass (Da): 53856
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A0A024LPT9 | MAHIELASPDTLGMWSLFMQANWVVKAVMIGLILASVWSWAIIIDKIFTYRKIRYDIKQFEQTFWSGKSLEELYVTYQNQHTNSICVVFIAAMTEWKKSLTKGVQPSLNLQSRIEKAMDLALGRESAKIESKLGFLATLGSAAPFIGLFGTVVGIMNSFLSISASQNTSLAVVAPGIAEALLATAIGLLAAIPAVIAYNKLMHESTQIITHIEGFADEFSTIMSRQIDEKITSNSLQ | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell inner membrane
Sequence Length: 237
Sequence Mass (Da): 26082
Location Topology: Multi-pass membrane protein
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A0A7R8W4J3 | MPLSTLNSSLLELYNETGVSASRQNLIWYPPHFPLEDEFDNVASFLWMQENWTLSIWISVIYVCTIFLGRRIMKNRPAFDLKQPMEIWNCVLAVYSILGCMKSVPYLLTVIQKEGLQSLCTHHHEIELFRPAVVWGWLFAYSKVVELGDTLFIVLRKRPLLFLHWYHHVTVLIYCWFSMRDYTPSGLWFSSMNYFVHAFMYTYYSLRSMDIKVPRKAAQFLTLTQILQMIVGCYVSFISFKLKYADPSCLVTWPNIFASFVMYLSYWMLFMHFFYQAYVSKARRSAASSKGGEKLE | 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: 296
Sequence Mass (Da): 34924
Location Topology: Multi-pass membrane protein
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A0A950D3P5 | MAPVLTLSKGRFEAFSDGVFAIAITLLVLEFHLPALAATPGVPLSVEQFHALVGIWPQYIVYVASFATIGIMWMNRHSLPRYIEKITYGIVLSLIAVGYNTLMWQVQASHPSIPRRPVLWVVIGLTAYPLATLIAYFAPVAGIALFFALMIFYLLPGNVASVAFKPE | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 18350
Location Topology: Multi-pass membrane protein
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A0A4U9FF14 | GPDIAIGLLRLLVNQSVLIRLKSHNSIQIFHQPLNMSYKVTIKTPNQDYTFNCGSDEYILDVAESNGIKLPYSCRTGVYSSCAGKLVSGTIQQDDQDFLDSDQVEAGYVLLCIAYPTSDCIIKANAEDEL | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Location: Plastid
Sequence Length: 130
Sequence Mass (Da): 14322
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A0A0N4UWY5 | MPTIGIRKAVIEKHLGHPINVVSAEEEFDELCFDYGLELDEVTSEKCAVEKEKGEKAAEGLCEEEVYKIELPANRYDLLSIEGLARALKIFHSRIEQPNYKVLPVEKRERIVVLPEVASVRPVIVAALLRNITLDSDSYASFIDLQDKLHQNICRKRTLVAIGTHDYDSIQGPFTYGAERPSEIRFRPLNQTQEYTADELMRIYSVDSHLKPYLPIIADKERYPVIRDKNGIVCSLPPIINGMFYMVLFSEHSKIRMDTKNIFIECTATDLQKAIIVLDTIVALFSQYSKQQFTVEPVDVQQIDGTVVSYPKLEYRTEHVSVKNINTKIGLELKGNEMAKLLSRMSLSTKVLDEDTLEVTIPPTRHDVLHECDIAEDVGIAFGYNNIQQKLPEIQTVAEPYCLNKLSDLLREEMAFAGWTETLNFALCSSADISTKIKRENGLLDAVKISNPKTSEFQVARTTLLPGLLRTLACNRDMPLPLRLFELQDVVIKDLRAETGARNERHLAAVYCGKTAGFEIIHGCFDRLMQVVDIKWSADNSGYHIKEYDDPTFFDGRCARVVGPGGFEFGTFGVIHPEVLAAFGLTLPVSAIEITVEQAMYADTLLIIFIAVCTALLGELLTYVLVYRSDQYKRLKSEMERKTKKLERKKEMTTEADRMKKKKIEREEERLKATNRDMSMFKMKSMFAIGFAFTALLSTFSSIFDGRTVAKLPFTPISFIQGLSHRNLVGEDYTDCSFIFLYILCTMTIRQNLQKLLGFAPSRAMNRQVPPSFFSTPSSGLSNNFSYLR | EC: 6.1.1.20
Subcellular Location: Membrane
Sequence Length: 789
Sequence Mass (Da): 89464
Location Topology: Multi-pass membrane protein
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A0A061HCT3 | MSKTRMPANSYRRGGKQAYSGVKVNSSRGNYEPLSSNEKRESVRLADSIDEAHGFTRYESGKKKVGWLVNIKSTTIEDENLPDGRAAVDCYFIEEDGGTFKTSLKYDPYFLVAVKRGYENEAEEWLKRSPGDGVLKSLRKVEKEDLQMPNHLLGYRRTFFELRFNNVTDLLAARKDIMPIAARNKTSMDAMEIYAEVARYFLFIQA | 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: 206
Sequence Mass (Da): 23591
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A0A0A7LFU6 | MFVMMLLIVFLFYFGMKNLKGYQEMNSKALYSTYECGYQEMTYNNMLYSSQFFVLALSFMLFDLEIVFFLPYFIFYFYSYMIVYMLMFFLMLLLLGLYYELFQKIV | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 106
Sequence Mass (Da): 13080
Location Topology: Multi-pass membrane protein
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A0A7R8ZNY1 | MSATPIILSGSVEGSFPYLTLKDRKPVILTRIVDYLSRHKGLLAERYGEESMEEIKLLTESIAQLKYELVTDKPMKPLVNDVLGDMKLWNQVLEEGTEEKTFFSVQWLLADALWGNQFDLSLSSGSVSSEKMSDQQCHAHRRDDIVINELDAAVRFVKTFRECPSPGIIRYVLDNAGLELFWDLVLADYLLTQGFCSQVIFYPKAIPWFVSDVLKEDIDWLLDHGSLRDLGKRWKRNFQEGRFKVCVNKFFTLPHAFMDMKTVAPELYNELASSAMIVFKGDLNYRKLLGDCSWDPPTVPFACALRGFNPAPFLVLRTCKAPLIAGIGSMSLYRELKEADPNWLVKDTIFGKFLFLKKMK | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism. Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Possibly methylates PCNA, suggesting it is involved in the DNA damage response.
EC: 2.1.1.-
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 360
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence Mass (Da): 41147
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A0A7R8W484 | MEVSSPIASTDDFMTQRFTSATAEETAPSVTPPQRSTTSQHRTHSKHSCEYQGFPLINLEFKKGSWKERAFNLFWVLRTHFLYYFISYGVHVLRFFTTGCASLFFTLMAIVIYDYQRPHFYLLLVYHVLNITVNWYHVITVSAKVQAKDCPAHSNKFCYTCLFYRPPRVHHCSFCDACIWRRDHHCFFFGTCIGGQNHGYFITTLFQQIVAVCSSTYFGFQYLEDRYRYEGLEWSDIIVYPYLYQKLFYQRYRLWVMSCLMLKYGLVVIAVVIFGLFAFNIFSTIRDITQQELQYRVLKGPSPYKSYKVVFGQYPFLRLFLPVHFPDPKMMEYLKDPYGVHDNCRYGHRCHLEETGGETPAYLTGDQSGDLQGNVQVERGDGGQFARRGRQNQPAHRRGGRYAALQVMRVQLLLRQTGLAGLGATDGGNTD | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 431
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 50133
Location Topology: Multi-pass membrane protein
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F7PF16 | MGWWDSERGGSDDSDGESDFERQRDELIEQLRGRERVSDRALAALAAVPRHEFVPENKRRYAYADRPLPIGEGQTISAPHMVAIMVDRLELEAGQTVLEIGTGCGYHAAVTAEIVGAANVYSVEYHSSLAERARSRLAELGYGDISITVGDGHEGWPEHAPYDRAYLTAAASSVPDALLEQLRPDGIFLGPIGDRRQTLVRVRKRPDGETERETFGGVRFVRMQGGR | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 25077
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Q57TR6 | MKAITTTIGTLWILSAHWTKADTNAADNEPDFTVLCSVLDVATGKPALNDIPTKWRNLRQQLTDINISLSTGDWTKHLLDTDGNVQEWTKAQQAGKLPEDWATEWPAWAAAAKRSAKGGETHDKLQASGIPSLDAEQRKEAAQLIKHLLNSTQPLMDALQGVETAEAATTAAALAATLDQSVYGDKPEAHPGKQASAAVRRTATRGICASGAKIGTSQALADALLCLCWTDTGSPPQGQGSVCRKNLGNTLTSTWDTASATVNAAYAQIKGACKLQTGHTITAANIAEALAAVKHKIAQHKEGGYLGKYEGDFSCDGKNANGVCIKYADFSDKGNKAFEEIEWVKKLRSVETALRKREAAVARVDTLTTALETQTAAAWLIPQRAKSSQQKREGVSPKQHTSTGNGNKQQADQCEAIKKATECKEKQPNCEWQGKNDEDGPHCKVNKTHITKEAAQTGTNRGNEETTTDKCSQAKTSDECAAVKGDIPKDKKSVCGWIEGKCQNSRFPVNKKLTLMVSAFVSIAAF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 526
Sequence Mass (Da): 56473
Location Topology: Lipid-anchor
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A0A949ZAE8 | MMALFWICTAILILTAIGVVASRHPVHSVIALIVNFSALAVMFLMLNAEFLAMIQIIIYAGAILVLFLFVITLLTIGTGPVESGPSRLAFQAVPSIVSGIVALALLASGVRTASAAAPPEAPADFGLVGSFGMQLLTTHLFAFEVTGFVLLIAVLGVVLMAARKELRF | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 17625
Location Topology: Multi-pass membrane protein
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F7HH31 | MAAAGLAHIPDVDIDSDGVFKYVLIRIHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKVSGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHSISTEKIKAKYPDYEVTWANDGY | Function: Exhibits phosphohistidine phosphatase activity.
EC: 3.9.1.3
Catalytic Activity: H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate
Sequence Length: 125
Sequence Mass (Da): 13800
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A0A2G5CWZ1 | MSLGGCTIISGSMGMKPMPCGPVTQKTTLTRFSRVFTKAAYPSIRSSWGTFQGQTRWPYTGWRPDLSIPSKSVLNGEHGSMSQRIPMLPYRHNKMRMFEPPRASKDVPTSFRYPPMTKKPKWYWRVLACLPYLMPFHETWMYAETAYHLHSFLERFEYLTYPFLGVIGRLPSWFLMAYFFTAYLGVVRRKEWPHFFRFHVVMGMLLEIGLQVVGSVSRWLPMGVYWGKVGMHFWTAFAFGYMFTVIECIRCSLTGMYADVPFVCDAAYIQIPYD | Function: Involved in protein precursor import into chloroplasts.
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 31940
Location Topology: Multi-pass membrane protein
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A0A6L7XDF5 | SFWIMLVGFNLTFGPMHILGLQGMSRRIDTYARGYGFEFWNMAATVGSLLIAVSVVIFIWNVVKSKRDAPHLPPPGPDPWDGRTLEWSIPSPVPVHNFDTVPQVHGRDEWWHTKYAENDEGKVVRVATVEEAAQTGEATDVHLPSPSFWPLAVAVGLPLIGYGLIFNLWLALIGALLTIASLYSWALEPVDDPDAAHDHHDDHSDDEAEATDPGAADDSTEGDQQ | Function: Part of cytochrome c oxidase, its function is unknown.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 225
Sequence Mass (Da): 24775
Location Topology: Multi-pass membrane protein
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A0A7R8WPD8 | MTRLAHWLLGLIVASLIWLTWLSTLASISVHALLVPAYFVIAFGIYCIVILSYRVATFNECPEAATQMRQDIEEARADLLRRGYVF | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 86
Sequence Mass (Da): 9774
Location Topology: Multi-pass membrane protein
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Q583L5 | MHHFQLQLPYVEILLMVATQPIATNKDSTTVKAACHEVAFNDKLAAAFKQKIDGLAAKKSQLLKEAEALDAAACLATDHKTKKATRMLASIGSSRAAATEANADAVKQLKASIETLKRRNAQLMAAIAFNTKGDLTISHDASAQKSDLIGGAGAKSCSVTITQPPKNEHGCQSSLVNDPAINDDVNNVQNLDSYQAIHDKAFQLTDIAADIGNKGDYGSATPATHNKKIACVDTGDRSNKLGSVAKGIILTNFARKADWNTPTKNTIKSKGDGTDCEDDQDSDKKAFVTAKAAGYAICNGRRQTVTEPETLSQLTMDALKEQKDVQEAAMLITAGPTAELPDTDKQKEAVVALVGEGKTTVHDKFLKDMEANKLDFKIGDKHVNKGIVSISGTEDYARAIGFCLGDQYRKEKAQKKVESVTAAAPENNKECKGETDEGKCNEKVGCEFKDGKCEAKVTETTGTNGKITNTTESNSFVINKAPILLEFLAL | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 490
Sequence Mass (Da): 52441
Location Topology: Lipid-anchor
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A0A358HZG0 | MRLFVGVEIPADIAADLYPLARGIKGLDAQTPENMHITLKFIGNVDPGLAVEIDQALAKIAFEPFDLCVQGLNVFASTRKIRIFWAGVKDQPLMRQLAARVENALLALEECPDMDMRNFTPHITLGRNRNAARATIEQAVADHGDVSSRTFTIDRFCLYESHSTADGPEFRVVAAYDGTDGQNGTGDTQNFRDDQAFLEREMLGEIE | 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: 207
Sequence Mass (Da): 22930
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A0A7R8W426 | MSQVEEGESRLKNGRMLRACRGQAVDRIPVWIMRQAGRYLPEFRDLRSKHDFFTLCRTPALACEVTLQPLKRFDLDAAIIFSDILIVPQALGMEVEMRAGVGPVFPNPLSTEDELERLEEVCQTSIEQRLDYLFEAIRVTQRELDGLVPLIGFAGAPWTLMSYMIEGGGSKTLAKAKRWLYERPELSERLLRLLTKCVVTCLLGQARAGAQILQVFESHAEFLNAELFRTFCLPYLKEIRSCVQREFPHIPMVLFAKGGHYALQVLSQESGYDVLGVDWTISPETAIKSVFGEGSVGSVKALQGNLDPCALYSNFTRGRCAAYVRFKALLLVFSCDEMHSVAEERYNTRRLKPIPSRSNSKRVAFSVPGDKVSVAAKICSKPVHSSNGMKSAVERKESDQRLRRRAGSVQPVVLDRCGKKRVSLWKTANSNVEKSAQEFNPDFSFSEPTLNSIKKIVEKLDTLRVEANDQEKNIVQCSSVQKEALKQATRSILKFETEAKLFKEVIPSVVDLGAKTQKAVSAKESSWQKKMERVRSKLTLDPRDPEIAPSDFRDLTWHREVDPKLELKRVSISNSAKSSIDTKFNMDSVIQRETFSNTDSDLSDYPSKTYSPAAQTHRYSYPFSLPDWWNPSDEECRRAFENEARLFCLSY | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
EC: 4.1.1.37
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Length: 651
Sequence Mass (Da): 73765
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A0A1B8J6S5 | MLAKYACKARFWVVLDFWNCVLKIFKILRIRQNLAGICTQAGANQRLTRIFMWLNRQVSKDFHTEFSVEEKLLDVRSEHILEVFKSKEFGQIALFDERDILFEKFIYIQSELLAHVGACSLPIASTNSAGAGAISADAGVGAESSVESKGANADSSAESIAGAESSALLLGGFNLEIAHELAKHRMQIDFLQSDEKVLDSLISFLPHFQEVRASRAFALYSKAIDLPLKKYDLIIHQSIPNAHEIDGLQRMLSAQGILIARLPHPYLQEEAFAQILGAFGKFFGIVMPFFAPLALFSDQGFVFASKATHPLADFCLHKCDMLKDLRFYNADIHQAVFALPSLLAQNLKGVIKN | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Length: 353
Sequence Mass (Da): 39283
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A0Q8G3 | MVVTDILFYTFASLAIISALVLVLANNPVNSVIAMIFTFIFTAAVWIILQQVYLALLLIVVYVGAVLVMFLFVVFMLDLHVEEQGRVGRFFYALAAVVVCAIFATVISYAATNVFAGAMMQGGVGGLKIIGLTMFSNANLYVFELVDFILLAAMTAAITLTLRAKRKGNKTVNPAQQVKVRAKDRLTMVKMPSNNEGAKDE | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 21898
Location Topology: Multi-pass membrane protein
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A0A2Y9MQL8 | MGLTSTWRYGRGRGIGTVTMVSWGRFVGLVVVTMATLSLARPSFNLVEDTTVEPEEPSTKYQISQPEVYVAAPRESLELRCLLRDAAMISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTAARNVDSETVYFMVNVTDAISSGDDEDDTDGSEDFVSEHSNSKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENDYGSINHTYHLDVVERSPHRPILQAGLPANASAVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYVCKVSNYIGQANQSAWLTVLPKQQAPVGEKEITASPEYLEIAIYCIGVFLIACMVVGVIVCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKEKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDITRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHRNGSVKT | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 841
Sequence Mass (Da): 94062
Location Topology: Single-pass type I membrane protein
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Q57W35 | MTKGGKVAVTKGSAQSDGAGEGGMSKAKSSTTFVATGGGSLPAWALKAVSTVVSAVILIYSVHRAYDIRLTSVRLYGELIHEFDPWFNYRATQYLSDNGWRAFFQWYDYMSWYPLGRPVGTTIFPGMQLTGVAIHRVLEMLGRGMSINNICVYIPAWFGSIATVLAALIAYESSNSLSVMAFTAYFFSIVPAHLMRSMAGEFDNECVAMAAMLLTFYMWVRSLRSSSSWPIGALAGVAYGYMVSTWGGYIFVLNMVAFHASVCVLLDWARGTYSVSLLRAYSLFFVIGTALAICVPPVEWTPFRSLEQLTALFVFVFMWALHYSEYLRERARAPIHSSKALQIRARIFMGTLSLLLIVAIYLFSTGYFRPFSSRVRALFVKHTRTGNPLVDSVAEHHPASNDDFFGYLHVCYNGWIIGFFFMSVSCFFHCTPGMSFLLLYSILAYYFSLKMSRLLLLSAPVASILTGYVVGSIVDLAADCFAASGTEHADSKEHQGKARGKGQKEQITVECGCHNPFYKLWCNSFSSRLVVGKFFVVVVLSICGPTFLGSNFRIYSEQFADSMSSPQIIMRATVGGRRVILDDYYVSYLWLRNNTPEDARILSWWDYGYQITGIGNRTTLADGNTWNHEHIATIGKMLTSPVKESHALIRHLADYVLIWAGYDGSDLLKSPHMARIGNSVYRDICSEDDPLCTQFGFYSGDFSKPTPMMQRSLLYNLHRFGTDGGKTQLDKNMFQLAYVSKYGLVKIYKVMNVSEESKAWVADPKNRKCDAPGSWICTGQYPPAKEIQDMLAKRIDYEQLEDFNRRNRSDAYYRAYMRQMG | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Location: Membrane
Sequence Length: 821
Sequence Mass (Da): 92233
Location Topology: Multi-pass membrane protein
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A0A3B9YPN7 | MGFASAATPWCMALAGTLLIAGLYGALFAAPADYQQGDSARIMYVHVPAAWLAMAGYSGIVIASAIGLIFKHPLADTAAKSMALPGAVFTALALITGSLWGKPTWGTFWVWDARLTSVLVLLFLYVGYMAIWEAIEEPTRAARAAAILALVGAVNVPIIHYSVEWWSTLHQGTSVLRKDGPSMPWSMLWPLLSMAFAYQALFAGIVLVRMRSEILERRLRTRRLSLGEEAP | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 231
Sequence Mass (Da): 25085
Location Topology: Multi-pass membrane protein
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V5VHN7 | MTQERKVALVTGASRGIGAAIAQQLIQDGYFVVGTATSESGAQKLTDSFGEQGAGLALDVRNLDEIEAVVSHIEQNYGPVLVLVNNAGITKDNLLLRMSEDDWDDILNIHLKAVYRLSKRVLKGMTKARFGRIINISSVVAHFANPGQANYSAAKAGIEAFSRSLAKEMGSRQITVNSVAPGFIATEMTDALSEDIRKKMSDQVALNRLGEPQDIANAVSFLASDKAGYITGTVLHVNGGLYMA | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Length: 244
Sequence Mass (Da): 26099
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A0A949Y5V1 | MVVRSSWRIGQIAGIEIAIHPSWLVIFALFSYAAMTSAQMLANQMGVALSTRSSIVLGILAALLLFGCVVAHELSHALVARRLGIPIGNITLFLFGGVASILREPGTPADEIKMAAAGPLASLALAALFGGIAYLAKDAPWILTLSLILASSNFVLALFNLLPAFPSDGGRILRAIIWTFVKSQARATAAASTVSAVIAALLVVAGVTMALNRMYNGIWLVFIALFLLQAAIASGRQARVSLALERMRVGDCMARTLIPVSEDAPLTTFVSTVQEAKTTAYPVVENGAFVGLVSPRDTGAVPPTLWAHTPVRAIMTPAAGLPSLTVDTPASDALAALAKSGVKSLPVFENGELAGVVSEETIFSKLRDQGATAA | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 374
Sequence Mass (Da): 38985
Location Topology: Multi-pass membrane protein
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A0A7R8W5F0 | SGNHKINFNQPDGFGHLESEGQEFYGFDRVRSVMDGVVLTIAYPSLRLLYLIDEVEGPSVTLNVLGHQWYWEYSLANIEVSSVSGMPWQHLVSLGTDTLTDHPTGRPLLPNLLVSSGTDASIEHPTPSPLWIFEKQLVLRKRNSKAGDVIHSWALPELGVKVDAVPGRLNQVQRPYDRRARGDPKEGNLGTGLYEQPTRVQDGGQVDRISGSQRIPLEPQKEVHPTL | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 25262
Location Topology: Multi-pass membrane protein
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A0A3C2A4K1 | MTKLSWSSGYQKINPWLLGLLSALFLCLCWPPLGAVVLLPLVFVPLLVAEDRWYQKGKPAALFLLLCFLVFFVWNAYAANWLYKTQARAAFIIFAVNALMMALPMWSYALVKRRMGIAWGLLCWVCGYGLYEWLTQSWELGYPLLSLSSALAPAPFVIQWIELTGWLGATVWVLTLNGLLFLALRSRGRSIGWSHRQRWALLGVLLLPLGYSLVRWFSYPTAEKSMNILVLHTALDAYTVKYQLSNEDLLNRYFGLMEEHMTPEVDLVVWPESALPNGGWLEDLRINTDWDNIRSRMAQHPRAGLAMGAIFTELLQTTQLGPLSKYEHLLTLTDVGQPYFQYNAGVVLQPGDYRMAYRTKDRRVPIEETLPYPGVLGPLQGFIGSLAGYKIAHRHTNQEVMPGPQGTFLSYVICYESLFGSINRELVAEGAEMLVVGLNESWYENRNASMQFRWASQLRAIENRRAVVRSANEGFSSYISPMGQVKQELQTAEDAAFLAQVPIQDSFTMYTLWGNYVGWILMALLVFIFIYPVYVKIKHK | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 540
Sequence Mass (Da): 61495
Location Topology: Multi-pass membrane protein
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F7IEU5 | MAGYLRVARALCRASGSGPAWAPAALTPPTSREQPRRHYADKRIKVAKPVVEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDKSISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNPDLIRFAQTLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
EC: 1.1.1.42
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Length: 452
Sequence Mass (Da): 50758
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A0A0M3FFV0 | MKLLHLDSSALGEFSATREIGQAVVQELKKHGPLEVTYRDLHVEPLPHFSKHFDSLSEEAQVDERILQQFEETDIFVLGAPMYNLSIPTTLKAWIDRILIAGRTFRYTENGPQGLVSAKKVIIVSARGSAYGDQFPMDHQESYLKDIFNFLGVQEVFVVRAEGMAFPTRSQSISQAINSIPQMFAMPAQN | 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: 190
Sequence Mass (Da): 21370
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A0A8C7GY69 | MKSGAEREALKRRWTVQQTQQNKESGLVYTEEEWEREWNELLKLASSEPRTHSSKNNNNTVGVDNSEDPVYESLEEFHVFVLAHVLRRPIIVVADTMLRDSGGEAFAPIPFGGLYLPLEVPPNLCHCSPLVLAYDQAHFSALVSMEQKDQHQEQAVIPLTDSEHKLLSLHFATDPGKDWEWSRDHNDNIKLANLILSLEAKLNLLHNYMNVTWIRIPSETRAPLAQPESPTASHGGDDVQSLADSMDSDRDSVCSNSNVNNGKVSAKDKDPKEKTERQQQRKDKDKTRTDSVANKLGSFSKTLGIKLKKNMGGLGGLVHGKINRSNSGGNGRNNGGVGGGNGGGGGGGNGGGTENNVEKKKEKREGKARKDGGGGEKEGQSASTSFSSDKTTSPSPTERPPGVPSPPGERDRDRGGLLARLVGDKALSEHWKYSTDVKLSLNILRAAMQGERKFIFAGLLLTSHRHQFHEEMISFYLTSAQERFSAEQETRRKEGEKKPAANSTTTTTTTNGPSNALKKPEQESAPHREREREKEREREKERERERERERERERERERERERERERERDTRTPPPPPSCPPPPTPLPQDFISSPGRHHHSHTPHTPPQIALKMQGRHSPSPNSSPSNGATRRPGSVPPVPRPVPTTVPVSAHYSHTPPIQRSSIIHLRDVNLQALQAPSFQPDDPQPSYKPPLVGTLKTCATYPQQNRSLSSQSYSPARLSGVRLGTGVNHTHPGVPGTTEPYNMPGEHKSHTYTNGFNTSHIQDCLEFADADVPQTWGSSRVTRTGSGSDKVKSQIGSTGGGCLVYCLQQRRCKREKCSFYGRPETDNYCSYCFKEDLKHKEREAKALSRPG | 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 signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 853
Sequence Mass (Da): 94645
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A0A9D9JDZ0 | MASVVVLLPLIIAGVWWPPTTALLAGVATSLAIGELFAIFRHGGYQPRLAEGLAVGWLICAATFFQPLTTIDLLLAVMFVAIIGTLIAEIARRDRQTSLLSWALTLAGAYYVGGLLSSYLLLRQLEQPLQDGWLAFAQIPPGAAWVFFTLATTWLQDTGAFFVGRAFGRTKMAPILSPKKSWEGFAGGMAAAIATALFCVPLLGLPITLVEAVILGMAAGIFGPLGDLAESLIKRQVGVKDSGFIIPGHGGILDRIDSILFTGPVIYYLVVIFLQ | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 275
Sequence Mass (Da): 29303
Location Topology: Multi-pass membrane protein
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B5X124 | MSARNPGMPLDLQWVSKVRVNTQAVLKRAQQIQGHNKNKKQWQAAWLLRAVTCIDLTTLAGDDTPGNVHRLCMKATQPVRSDLLKSMDMQDKGVTTAAVCVYPSRVADAVKALKAANSSLPVASVATGFPAGQTSLKTRLEEVRMAVEDGAMEIDIVINRTLALTGQWEAMYDEVCQFREACGEAHMKSILAIGELGTYTNVYKASLVAMMAGSDFIKTSTGKESVNATYPVAIVMVRAIRDYFLKTGHKVGFKPAGGIRTAKESLVWLTLMKEELGDEWLSPHLFRLGASSLLADIERQIYHYVTGRYAAYHQMPMA | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
EC: 4.1.2.4
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Length: 318
Sequence Mass (Da): 34985
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A0A1A8V7W8 | MKKSRSVLSVTGEEGNDLEVTDVVEKAESSRYSRSYTSGATLGAELRRGRSRRLSPSLQVPCWLRPRDRTRSPDILSNTSRPTSLPLRIPPRISITQADADSYEAENGVPQGYTPVGSQSPSLTLNTSFPQGQRRESFLYRSDSDYDMSPKTVPRNSSLASEGHTAEDFIVTPFAQVLASLRSVRRHFTILANVSTPTVKRSPLGGVCVSPRATLSDQQYQQLALDTLEELDWCLDQLETIQTHRSVSEMASNKFKRMLNRELSHLSEMSRSGNQVSEYISSTFLDKHNEVEIPSPTLKDKPMSHIIGVRKLSHSSSLSSASMPRFGVNTDYEEELAKELEDLDKWSFNIFRVAEFSNNRPLSCIMYAIFQERELLKTFRIPADTFVTYVMTLEDHYHGNVAYHNSLHAADVTQSTHVLLSTPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLHQENCDIFQNLTKRQRQSLRKLVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDHYTERIQVLKNMVHCADLSNPTKPLPLYRQWTERIMEEFFRQGDKERERGMEISAMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQELLDTLEENREWYLNTMPQSPSPPPDRHLQQDRFQFELTLENLEHNNHNHICLKSGRSSRSNQKAICDDSSHGDPTETSEGEQNYSGAEKDDKENHNSEQNGVQGEKEHEDTEGKEGEAGEEEEVHKDEHVGEEINGAQDEETREEDEEEDKMEEEVDKEREEDEVEGEEGAQQEELDGESKGEELETEENLAEKQEDVEEEGETKEKGEEEETEKEDKDQEVEQEDNEEEEASEGVREDEAKEEES | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.-
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+)
Sequence Length: 884
Sequence Mass (Da): 100541
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A0A1A8UKC3 | MASTGMQIFGFVLALLGILGATVATLLPNWKVRADVGSNIITVISQMQGLWMDCNWYSTGMFSCTLKYSVLSLPAYLQTARTTMVLCCVLAAMGLCLASLGLKCTRWGGGRRSKRHATIASGGCFVAAGFLCLVPASWFTNEVITNFLDSSVPESNKFEPGGAVYVAFVSAGFLFVGGSIFCMSCSGKRHGPQDLILLPHPDKLLLQQQQQQLLQQQQELQHQYCSLSPLDNKTGYSLQDYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 242
Sequence Mass (Da): 26284
Location Topology: Multi-pass membrane protein
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A0A7R8WH36 | MSRNCDHTKSSSLGRFVPEKLQYSNELKCAWCPKKGPNLWLCLHEDCFELSCGKKAGDHSGVHYRDNITHCLQMNISTKRIWCHSCTMEVFLEQSSTMESIPSGKSSSTDTTSTFDDSEEKPIVRRGLAGLQNLGNTCYMNGALQALSNTPPLRQFFLDCGSSIAEEERPALAFQFQILMREMWGSHQVSCISPTSLFHRVKMINPAFRGFQQQDTQEFLRCFLDALHEELKERTRIVDGQKNRNAVDSGEGAGGDGGGSECSDDGSSDDETESNQDLISLDDQEDLGGFETADSGVSGDEDGVHPHPMLSEPPQGNRPRRKRKRRQGDGDQLRQNRLSSPRTVKPHQPSKKRHQSNAEQKEHSNKKKENFKSIISEVFDGKILSTVQCLTCQQVSTTREIFQDLSLPIPSRDQVALIRSQTQAAIAGQLASQSTHVPSCSDGQRGSWFYWLLEWLKPWTWFWGHSVSLMDCLSAFFSADELKGDNMYSCEKCHKLRNGVKLCRMLELPEVLCIHLKRFRHDFVLSSKILTPVSFPLEGLDLSSFCDRDCPSRVTTYDLIGVICHHGGVGGGHYTAFCYNDVSRTWFEYDDRFVTEVSPELVATSEAYVLFYRYNFKESFDVLLMFGRLLNLIRRKSNSSMIRHRSRVMDLAEREEIEQEPFLKFYISRRWLNRFNTFAEPGPIDNSDFLCPHGGLSEKTVPARNMILEVSQTVWEYLHSTFGGGPPCNRLFDCQICDEELRRLKERRDTEYDEYHKRYKELQNADGGTVALYAISLPWFKSWENFLRGKEPEPPGPIDNTSIVTVRNAQNTLRAGSDYCQIPASVWEYLLETYGGGPPLLVRPGSRPLGAAYVERIPATISLAGGGRMEGGEAAAGGGRMEGGEAAAGGGRMEGGEAAAGGGRMEGGEAAAGGGRMDEEEAAVRMEEAEPMETQEDEEFQEDDFDEDKNMEEGSDREGEQDESPPFQENTLILNVPPPVDLPDTNCPPCLEKIEELHS | 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 signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 999
Sequence Mass (Da): 112119
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A0A7R8WPG3 | MWFRSAAEKMDIQLMVSQVLRYFQVCFISAVFFAILLLFYNSSISEIRPFPSLPSQDWVPSRRHLQQIPPVNQSAPTTSSTSTQTSANKKAAKTLADLFEPGFQIPGDDICGEDQGKGVLVLILVTSAPGSSEKRRAIRETWGHYSLRRDVTIAFVVGNTTESSYQAVINEESKTFGDIIQERNVDSYQNLTLKTQSLLDWTMAYCPNAQFLLKTDDDMYINIKNLLNF | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 229
Sequence Mass (Da): 25865
Location Topology: Single-pass type II membrane protein
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A0A2A5GWL2 | MYMIDETNKLLREISPEFNFNNPPIDPIQFAKDIAESLMNTSGVGLAANQVGLPHRCFVIRSNPILVMYNPIIVDYSKKEVYMDEGCLSFPNLIIKIKRPEHIRMRFTLPNGEVKTEKYTGMTSRIIQHEYDHLNGIIYTDRATRYHREMAQKKCLKLRKTIW | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 163
Sequence Mass (Da): 19092
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A0A7S4E7N9 | MRRTAVEEEAPMLEMTPVVAPGEDAKDEEAGEPGAPGTQTPTPDEGLAGEFAVGAGVPRTWDDPHEGCPDDCGPDGPCVKYGRRNVARFCKCLGARRLGYMAVLRWKNVKGKPAPMPGGAVRRTKLLCIVGPFWPFTCCVTFPLIFLISGAIGIAVLPDRALVTKIVWALSVLCLVTALSCVAFRDPGILRRHPEKPEANWRWNDQARTFRPPGACYDEDLGLVVEGFDHVCPWTGTGIGQRNMGAFHCFVTLLCVCIVLDVLIVMRVLP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 270
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 29356
Location Topology: Multi-pass membrane protein
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A0A182GG42 | MIFRVVDAAKIIGTRQNLVPYLTLCHQVNHRIGILALRKLSVLSNSRISNKFVVNVRKADKKQPSIQRLSYGTQSTTPPKEDKKDAAGAGKESQEKTLEINTKSGKLLVTTTTTADAKLQEVIIEKPINLMKSAADATAAKEALQHSTAVPGDDDPKRKLEAAEQKEKLAEKNRQLAKKRIQVDFSRSSLERNFITPVRAMSDFLLKPSDLEGLPKTKRRSPYEQEPPITVYWRKDVEAKAIEVWGSRENLLKECLKREIEKKRHQQNIFTVKRRLRDYRREIGSRTNVVDSEPGLFGKSGKVVLTAIAINATNCLFKFGAWLYTGSHSMFAETIHSLADTINQLILAYGIHKSTQSADSDHPYGYANMKYVSSLISGVGIFCVGTGLSFYHGIMGLVDPHPLDDLYWAFFILGGSLVSEGATLVVAINSCRSGAKALGMTFKDYGK | Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Subcellular Location: Endoplasmic reticulum
Sequence Length: 447
Sequence Mass (Da): 49715
Location Topology: Multi-pass membrane protein
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A0A813ETM8 | MAEVDLRHYKPPSGFKACVRGILQALSAKWELRGPLRPYCHGSIVVGQVIPNLVTTAWMIAIPAAAGIHYYVGPLLGTKPLHHDLLGISAVLQLVLILVLVLFVALRNPGLIQKGHGLPEGLLPEDLDAQGWPRARSICVRNVWVRQEFCRTCMLWRPLRSKHLRDSGWCVEGFDHYCQLLGTVVGRRNYLAFIALVHFLALFTLEALVVLGVGVLPHRRRASRGGRWLETLLDSPDICCAFAYALLWLCFALRILHLHWFLIARNMTTNEYVKSHWGLGNDPQRGEVPGSYANQNPFDKGCTSNFFDVCVSGVAAA | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 317
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 35363
Location Topology: Multi-pass membrane protein
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L2FHD2 | MADKSKKFPDVEGGGSLILAWQIKGKKVLVVGGGEVAAGRILNCLNADANVTVVCPASGFNPEVAHRVARGEVTHVDRLFEPTDLDGADMVLVAIDDPAASTTIWKLCKERRIPANIADVPPECDFYFGSVHRDGPLQIMVSTNGKGPRLAAIIRRFVAKQLPKNAGNAIEAIGTLRGKLRKIAPTPEESPKRMGWMTKVSNAYDWGEMCDLTDEDMENLLRFYSSNTVPTIDDLMSMREEPGFQADLFDGSFGFCVGA | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 259
Sequence Mass (Da): 28128
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A0A3D1G694 | MTDGPVSPDLDDIRRGLIWRWIPDWCVPFIILARLERPIGWWLLVLPGWQAIILGGLGAGASLKTVLWLMALFWLGAVVMRGAGCVVNDSWDRDIDGDVERTRNRPLASGAVSLRAAMVFLFLLGVIGLLVLINLPMAAIITGFASLPLIVIYPLAKRVIGFPQVVLSLTFSWGALLGWAAHGQWPGIPAGILYLATAFWVFAYDTIYAIQDMEDDRQVGIRSSALTLGRGLRPVVAGCQIMMVVLLILLGMMMALPAIWYGGVALVAFHLIWQMSRVDIEAPHRAGAIFRSNRDTGLILTVTALIIFVLSA | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate
EC: 2.5.1.39
Subcellular Location: Cell inner membrane
Sequence Length: 312
Sequence Mass (Da): 34139
Location Topology: Multi-pass membrane protein
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Q57U08 | MSFVPPPASSTTHAQREVELTLLRFLEKYRPEVCDLWGTHSNIYLHADSNEKEEEMCTIDNEEGIVHSLNRESHEKYLKSRLVKLPEYAQRLYNAQPWMVYWTLQAAEMLGITEKLYEQISQDALGEFILSCLQEQPVEDEQKGCWGSEEGGKHGKGSMPQQCGNVYDFLRRCDADHTCAIGFSGGNYGQIPHLATSYAGVCSLCILECPEYLQALPRSAIKRWLLSLRCADGSFRMHIGGEADIRASYCVAVITTLLQLQDVDASSGDILREQEAQFVASCQTHEGGFACGRFASEAHGAYTQCGLAALILMKRPELCNYTALRGWLAARQLRFEGGFNGRTNKLVDSCYAHWVGASHVLLRVGESLAKITTCGETKRSLTSREMLLLDHAQLVDISNLHPESFEAWSQHEEEKQERASRVEAYLSATPLAASWSSSGVPNVLDDDAGDFYFNQRRLQLYILACCQNREEGGLMDKPNYPNDFYHTCYSLSGMSSAQNLQGMQVNRDGRDLSGNSFYAAAVSRGYIPGRRDSYGIVLPSDERSGVSSELHLSKNCLRPTNPIFNINQSKVLFALRTWGAKTFMC | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
EC: 2.5.1.58
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]
Sequence Length: 585
Sequence Mass (Da): 65419
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A0A7R8W8S9 | MKTLIPLGSIDLVTTFRQNPPPTLRWGVFFLVTLASFGTRLYRVEAPAHVCWDETHFGKMASWYINRTFFFDVHPPLGKMMIAASGYLTGYDGKFGFVKPGDRYDDVNYLGMRVVCAILGACLVPFVFETVWEVTKSLPAATLAGSMILLDFGVLTLTQYILLDPYMLFFIAGATMCLAKFNGCSERPFSVLWFFWLFSVGTCLAGAIGVKFVGLFIVLYVGFQTIRDLWVVLGDLSRPLLYTLQHFIARAVCLILWPFLLYVLFFYIHLRVLSKTGTGDGHFSSAFQSTLEGNPLYNASMPAALVNFPSRSQATEKMEQVTQMTCGVSMLRISKKVTRSILYELCSKFIIISQDALCTRTGKPYQSVPNVSIEIYKPSFISRFIEAHAVMFQGNADLKPKAGENFARPWQWPIDFRGQWFSASDSMYIYLLGNPVIWWGNLLLLLVFLSCQFWNIVKERRGTQEAPAIKKTPEITPEGPGILPVVSKTKFFKKFWHIDYCR | 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 Location: Endoplasmic reticulum membrane
Sequence Length: 502
Sequence Mass (Da): 56908
Location Topology: Multi-pass membrane protein
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A0A7R8WL36 | MQNLIGILQVDIAYDEDNPLDGQPPITMELQLGYRNRGDKEWDWKLLANSTEVRKLECDIEEVFIFFTLNDSDNSNKKAEYLYNCSMIPVFELGSLHHDFYLLNVKLPVTNRINQHLGKITDLWLVTINQNGGFTKVWLSMKTVFFPIVIGVMVWFWKRIKLLPRPPALLERSLMALGTALSLLNLPVEYLSLFVDMPFNLLLSDMRQGIFYAVLLGFWLVFAGEHLMVRSLRWGILKNKISGEKRIARNSTEEARSIQ | Function: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 259
Sequence Mass (Da): 29982
Location Topology: Multi-pass membrane protein
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A0A950BDH3 | MTASAAPMRCGRISYTNDLPVYAAFDLGVLEFPGNLVAAVPSELNRALLAGELDVSPVSSFFYAQHGELTTLPGLCIGSRREAKSIQCISRVHPRELAGKRIATTTDSATGRALFDVICRAGYGFTPDLAPSDDPYGEHQRDGTPCVLIGDVAIDAALAEPHNAHDIGKLWYGLSGTDMVYAVWAMRRDRLKALMRDPQGKEWVGGLVFDLHRAIDFGRANMARVIELAQKQCLRPAGFYEEYYKALNYDLDTQAMLGFAAFCKMAQQCGVLDRDVAVPAAPEDTVHVPND | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.2.1.151
Catalytic Activity: chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O
Sequence Length: 291
Sequence Mass (Da): 31728
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A0A329SV74 | MICVIHVAGILVSATALLTFDLSEATNAQQGMISKLAAPDVVHSTDALASDKRYLRSHDYDEDDEEERAGGANAFDKAKLQKMLDNINYAYKKFAKWSTRGWSSGDVHDSVPKQLYNQYYNYRKDAGHASNLVPQLQPRHGQHYPLLLSYMREAIPQEPLGKQQIHVMVKSFFGTLITTT | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 180
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 20246
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A0A358R602 | MNSTKKKYKKGAVLGAGSFGTALSAVLASNGVEVTLWAREPEIIDGIQSNRRNPVYIPTLELPSSVVAQAELSKALEGAEFILIAVPSHAMREISSDIAPMLRGDEVVVHVAKGLEEGTFLRMTQVLEETLKGVIPNDHLVVLSGPSHAEDVAEGLPTTVVVSCRSNEVATRVQHTFTNERFRLYVNPDVVGVEIAGAVKNIMAIAGGVSAGLGLGDNAMAALMTRGLHEITRMGMAMGGQQDTFAGLAGMGDLIVTCSSEHSRNRRVGWRMAHGERLEEIIESMNMVAEGVKTTRAVHQWAQENGLEMPITAVVYGMLFEELDPRAAMDSLMTREPKNEINM | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 343
Sequence Mass (Da): 36946
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A0A7R8ZVY2 | MHVQYAVVTSVTRDDLLDGGASFFAETIERIRELSPQTLVEVLIPDLQGNWEALAFILAARPAVLNHNMETVPRLYPTVRPQAGYELSLSLLAECKRRDPAMVTKSGIMVGLGEGRREIETVMDDLLEVGCDILTIGQYLQPSKNHLPVVDFVAPEVFVELEGVARKKGFPGVASSPMVRSSYEAGEIYRQVTESRGQA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Mitochondrion
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 199
Sequence Mass (Da): 21930
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Q57X48 | METAVPVRYFLGTLIEAPARDTLIFAPRSLVCVGADGCITAVLQPNDIKNESGVSGGGGSGCGGKSDNETYEQTLKEARRSGALTVLKDHQYLLPGLIDLHVHAPQWPQLGKALDRPLEIWLHEYTFPLEAKYADLDFAATSYNSLVSTLLAHGTTTAVYFATIHVDASLLLARVCLEKGQRAVVGRVAMDLASQCPAYYRDASPQESIERSEIFIQAVRKLPGNDNSSPLVLPAVVPRFIPTSSDEALQGLGRLVAKYGCHVQSHVSESDWEHHHVLERCGKPDAFALDDAGLLTRRTVLAHGNFLSDADMKLLCSRGSAVAHCPLSNFYFSGAVFPLRRALDFGLRVGLGTDISGGPSPAIWDAARDALMAARALESGVDPTTSKEERGGRRHANPEQSKAEDSNGKKGENPRVGGSAAESRDSTSCRINSVEAFWLATTRGGEALDLKVGRLAAGFHFDAVVVDVSVPTGGVHIFQGLDGPRDIFDKIVYGASAANVVQTYVAGRLVHGRVEL | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
EC: 3.5.4.3
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Length: 516
Sequence Mass (Da): 55322
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A0A7R8WJ13 | MKKKHLLQRGGSKKKGSSSRPGRVSKATKRREKRRKKREQKKQPPDARPAGNPVSQKVNQEVATVLDEPVQEDPALATIPTTSLHPTQTKLSPWDRLEPSLLPELRSAVSCFPAMTPVQGAAIPLFLTNKDVVAQAATGSGKTLAFLLPLVQILLRTKRKWKKHEVGAIVVAPTRELTNQIASVLCDLIRELPLTHLLLVGGTDIGQDIRRFEEDGANVLVATPGRLCELLSNQQQLRKSVTDFSLASHVKSLEVLVLDEADKLLELGFSVHIDAILSVLPKQRRTGLFSATQTQELEDLIRAGMRNPVRVIIKGDSITPETLENYYRIEEDDKKMEFLLNFLEKRGRGQKILVFLATCACVDYFGSALKEILAGKSANPETLSEKSPIPVLALHGKMKTKREKVFESFRGMANGVMVCTDVMARGIDVPDIDWVVQFHPPSTSKAFVHRCGRTARSGSEGKALLLLSPHEEPYLEFLRLNQGVKLLPFTDEGASMEVDKVDSTKHEVPTAVEAAEKLESCTEAMDLKDKSDKVTTVLRALQLKDHGLFDKAIRAFVSYIQFYRKHECGLIFHLKECNLGRLANGFGLLKLPKMPEVKWAGDWSAFDAPGDVEVNGIPYRDQQKEKRRKEDLKAFEATGKWPLKRAALKKREKFLEKREAEAEARKERQERLKRLKASKQKKKRSRKSAFDLENFEELDKDWKLIKKFNKRKLTKEQFDEEFLADEAAGDR | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 731
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): 82384
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A0A950D527 | MALFVAIEIDDVARGALVRAMGDLAAAGPQLRLERPEKLHVTVAYLGKVDTQRLDAFEDALARAADACPPFAIEFDCLGPFGDSRKPRIIALRCSRPQPGFAACAAAVRAQYEALGVVFEHEALAHVTVARARNGLGTLARIETELPCILAVRELALFESVPAGPTTRYERRSTAPLQTTRSRR | 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: 184
Sequence Mass (Da): 19937
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A0A7R8WGL8 | MVDVMHNQKLFISVSSFLGAILIYGHVLNKVLPTEEEQKISFSLIVLVALSFSVPVSFFLKDVPEVVHEITRPAFLGLMLVNAWTLLRFGGPLWTPFSVYALFLVLFHYSEYFFHCLIQPPRKDHLDSYLLNHSKAYGIALVVGWVEYGLEVYFMPSLKSMYLPVILGVCLCTIGEILRKSAMVTAGRSFHHVVQTVKQPEHVLITWGVFSFCRHPSYLGWFLWSLGSQVILFNPVCMVIYPIVSWQFFSSRIYHEEYTLLKFFGEGYSEYQNRVPTGLPFIAGFKQTDLRQLQHRKSN | Function: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 299
Sequence Mass (Da): 34446
Location Topology: Multi-pass membrane protein
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A0A7R8W0U5 | MDIHPPPLIITLSGKRKCGKDFISDIIMNSSFGDHGAKLTLSAPIKEHWAATKGLSYEELCTSSEYKENHRKEMVAWGEEQRRKDPAVFIRAVAKAAPTKVKFWLVSDVRRWSDMEVFDTLQGTAVKRIKVTASPDTRKRRNFVFTPGVDDAGTECDLDPYEKWDLVIHNDGTEENLHQQLEPTLSEIIEHDEWCKEHNVRLEAKRKAIERWKEDRKMEKLQERRAASLDELRRSSVPGSSVSGTSSYNRRNEHLQRQLEEYRLQKADMEAAAAAREAEEARAQAIRRRNANREIAKTRCQMRLQWQLMKKHQEQKKREKQAAAEAANALRMKNFESRKNASRLFAPTQAHLRRIAAAKPASTLPSSPVMSVRTLDRKGVPAWRQVRSSSIS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
EC: 2.7.4.2
Subcellular Location: Cytoplasm
Sequence Length: 392
Sequence Mass (Da): 45062
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K8Z302 | MLSPIAESPLKEQAAEQDEEGETKNVNHSRDVEHVVEEDEENLLSADALRRRIQESTRCGKPFRGTPMEMESGCEALRTPSPWLSSAPYISLGTTSMPSSAPAGHLGATHSPLPSRSASSSRTNPWRRPLDLLISTRNIVGQILSFSRGGMECPLPVLYDEDHPDPFVTARHHYLIYLSPPPPSSSLGPSLPSSSCPPPPGGRLYTVGPHWAGVVFTVFLVCLASFLFISHVCVPLGPFFVLVAGVYTGLTLLTLLRTACLDPGLITRSVPPSLPRRKYCSICRLYTGPTARHCEDCGVCIEGMDHHCPWMGHCVGSGNMGAFLCFNCVWLTYVLFVLACLAAQSGVFGNATRVEN | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 356
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 38633
Location Topology: Multi-pass membrane protein
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A0A9D5JAX1 | MRWYQPLRRPREIAYVRRRGRSFGRPTLVGYAAVAQPGSPTCIVVSVGKAVGGAVVRNRVRRRIKGALDHRPPLAVPARIVLVARPGAAAREYARLADDVTAVLTRLACPVGT | 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 the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 113
Sequence Mass (Da): 12294
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A0A7R8W3R3 | MFHGLFCKVSVVCFPVWVTSAVRLTSRCSSGHFVCIALNKSKPAFRVINRLHEYEEEAEDVQENEGEDLDFGISINLPEAKGTFTCLNCVNEQCDYLFEISECHHAVKCYEYSQFEPDGTWYRSRGCIHNLQSSHLHCRSSSAKIKQDLEFSVFCCDGSLCNNGSMETHHSMLIKANTQGSDDSSKAWILLPVVLGVAFTIAIILFIIVTLRWYEARRRRECEDTQDGDSIRLDDLACSPMIPKLTRGDDGSAGMATLELTSGSGSGLPLLLQSTLAKQISLQEIIGKGRYGEVWRGVWRGQSVAIKSFFSKDEASWGRETEIYTTTLLRHENILGYIGSDVTSNNSFTQLWVVMDYHPLGSLYDFLNMRTLSEQQFLVMAHSAANGIVHLHTEIFGSNAKPAIAHRDIKSKNILVKNDLRCCIADLGLAVTHKNSSDELHVPQNSRVGTRRYMAPEVLDFTLNTNNFESFRRADMYAFALVLWEMCRRLEGRPGEENILPLDYQPPFFDHVSPDPSFDVMRRVVSVEGIRPVFPLGWNDCPTRHSVALMIQETWHQKPEVRLTSLRMTKNLIKLITHSDPQLSQTLFLT | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 590
Sequence Mass (Da): 66739
Location Topology: Single-pass type I membrane protein
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A0A0N4V6C1 | MGQIVVGDILKVEQNKDFPADLLLLSSSETNGLCYVETSKINGETNLTMCRGFECTSHLKEEGKIKLFSCEIECEKPNENLNEFTGTLITENENEKMRKKIESEFSFLLNCAEFFLLYCNLVPISLLHTLKIIRYIQAYYINNDSEMYDEYSNTPAKANTSALTDELGQVDLVICDKTGTLTNNAMKAKAFSVGGENYDFNASLTSKNKQGDPECFEKFFRVLTLCNDVFPQEQDRGQICYSGESPDEVALVRGAKLLGFKLCERNFNQITVKEVFLLFGAFDIWLTYFASLSVYSNSGLGSVSYGDLLKRDKDKKYEMLNTLEFTSDRKRMSVIVRCPDKSVLVCTKGAESVIYPLLHKDSKYLDKCKEHLVDYAKKGYRTMCFAYRKLQMHDYDDWNEKYQSALKYTDKGERNKSVESIFGEIEKDLYLAGGSAVEDNLQEDVPKTINFLMKAGIRVWMVTGDRLETARKIAVSCGICLKQNVLLHLTLQNGVDLFASIKQLQEKAECLQQKGQEFFLATSGSDLQLGFKNSCREKLMKLLLSCRSVICYGTSAIQKAGVVEMAQDNGKNVVLAIGDGANDVPMIQRADVGIGICGQEGLEAASMSDYSIGQFRFLERLLFIHGAWSFQRNTKAILVFFYKNVCFFLAGLWIALFSAFSGLEFFDSLSLTLFNLLITVIEALMLGIFFKPCSDERLLKQPMKYRTLREGAFTGNAFVKDIILAFFHSATSNCFSFLFMSHSVLWSNGRSSGWSMFRNSCNTVWQHTPFGADVCGISGIMSESPCFWLACFIIPVATLLIKPFSKLVLYTMHLSTPKFLFLNECNGDQSSPIDLDEFDVRQHLVDDHAVDNGEEDSIHNDNIIFESLKSSASRKLLQNSERKCQNEM | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 888
Sequence Mass (Da): 100253
Location Topology: Multi-pass membrane protein
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A0A099TWB4 | MNYLAQTRSNDETYKTFSDAILDPNAKLGGLYTFNNIKPFSDFTWLKKASYVDICNKVFSQLGIIDINSNNISSYIQIALKSYDSFRHKEICPLVNISPNLYCLELYHGPTFAFKDMALQPFSKLLDSLASSQKQKYLILSATSGDTGPATLQGFADSTNIRAICIYPKGGTSEVQRLQMTTQDAKNLKVFGIQGDFDMAQNSLKLLLRKQSFRENLTNMGYALSAANSVNIGRIAFQIIYYFVIARDLYLQGIQEFSIIVPSGNFGNALAGFFAKQLGLQITKLCIASNPNDILSEFFNTGIYDLRNKILKQSYSPAMDILKSSNIERLLFALFGANRTRQCMESLDKDLIFSLTKEELKTLQTLFEAHSFDDSSCLIGIKKAFNQGYVIDPHTSNAYLFAKLRESSINGQTQVILSTAYFAKFAKTTLKALKGDSDRIKSIGDLEALKEIQKEIRNNINPNFTLESNITSLFNKSEIHTHTYHIEDLEQEILNFCKD | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
EC: 4.2.3.1
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Length: 499
Sequence Mass (Da): 56160
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A0A1S8D646 | MNILSIQSWVAYGHVGNASAVFPLQRLGAEVWALNTVQFSNHTGYGAWRGQVFGAELIRELVTGIEERGVLGTCDAVLSGYMGDAAIGEAILEAVARVRAANPQAVYCCDPVIGDVGRGVFVRPGIPEFMRDRAMPAADIATPNQFELEWLTGRAVGTLAEAKAAVRALQESGPRCVLVTSLRVEDTPADAIEMLAAEGGQFWRVRTPLLPISVNGAGDAIAALFLFHRLRWGDVRVAVSSAASSIHGLLRRTAEAGSREILTVAAQDEFVRPSQTFVAEPC | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1.
Function: Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
EC: 2.7.1.35
Catalytic Activity: ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
Sequence Length: 282
Sequence Mass (Da): 30143
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A0A949Z964 | MFFRNLKWNIIGQRNYWFALSAAIIIAGIIALVAHHGLALGLSFTGGSTIDVKLSQSVTETQVRNALKAIDLSGIGPEFRSQYAAIQSGDEGIQLAFKQGDAAPNDRVIIQTQSAINDPGPVYKALDNAGIPVDRGQSQITSVGPSLSKEYLSRSLWALVIALVLQLLYIAFRFGNQLRYGIVADIALVHDVLVMVGIYAIANRKADDAFLAALLTVIGYSVMDSIVIFDRIRENGRIMPDVPYDEMVNTSLLQTMTRSVNTLATVLITLFALYFFGGDTLKNFAFALLVGVTSGAYSSIFIASPLLVLWKHADQRKRQAIRTAATARDVSSAQSTSPASAETVPRTPPKRKAKVTPPPRYRKRRVTPAGPGESSRPTGILGLLEELGESDEGDAADGQLADRPVPDDQLPGHQEL | 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: 416
Sequence Mass (Da): 45021
Location Topology: Multi-pass membrane protein
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A0A7S4A0H2 | MAWRQALPRLAAATTAPAASLALCEAQRKTDYDLARHQHGKTRVRVLKVRREGGVHAISEYKVETTLFSPAYDRVFTKGDNTDLVATDTQKNTVYIVAKRTDASTPEAFGVALCEHLLKEYPILSGCRADVESVEWARACVDGRNGAQPHVHGFLRSEPERQVASVSMTRGQGPKVESSIEGLVVLKTTQSGFEGYLKDKYTLLPDTQERCMATEMTASWNYAQLPQDFGAARNNVRRQILKGFFGEPATGVYSASLQESIYDAGCLVLDAVPEVKQIEIDTPNLHYLPAKLLDAVGEKFEDDVFIPTSEPSGSINCIVARGAGGRPTTTAPTSGPKLSVETKPVSLNVADAQARAAEEIRGAIITPKANSCPMAVRLAWHASGTFDKNDGSGGSDGATMRFAPEREDGANAGLGIERDILQPVKRAVPEVSTADIWTLAGAQAVEVCGGPRINHAMGRKDATSGAQCPPVGRLPDASQGADHLRDVFYRMGFDDREIVALSGAHTLGRCHKVRSGFDGPWTSNPLKFDGEYFRNLMTKDWVPRDWDGPLQYTDKESHSLTMLPSDLALKEDPAFAVYASKYAADESLFFEDFKKAFEKLISLGTTAAPASTDLDDAAAKVREECMHGSLEHAQTAWRPGVDANSYDAGSRRTALHKAACVPASLFELWSVDIGRQRSVCYTGSGATRTSFLGSSTTSAPPSTRRTRPATPRYMMRRASATPTSCPSCSPAAPRRTRATPPARPREKWPRRTGTRPRSAASSRSRRLPPQAVHVIPCPPSPPTN | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
EC: 1.7.3.3
Subcellular Location: Peroxisome
Sequence Length: 784
Sequence Mass (Da): 85047
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Q582W1 | MLRCIQCNAAVYRIVQPENEVVEKCGTCGRRCDRYYEFSNCQKWISITLLEKPAWIHVLFNKKDIRATLFCTALLSRLIEAYVVRTSLVYGALRMLRSKGPVSNVSSVATLQLFRNVNPKIEPLMAYQDTLPNIFICACGEYLLCLLVTVIFALHSWRRGGSALWDVVLTWMTCVNLAYSAKLCFVVFLIWRIPIALVSLVDLISLLWAARGFSLVENRYPPLFTSVVVLICTAATRYLFRSVTQWSPQLLV | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 252
Sequence Mass (Da): 28745
Location Topology: Multi-pass membrane protein
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A0A2N5CT75 | MTKKKAENGETGRDVLVLLGGAGDLALRMLLPSLYFLEVDRLLPRDLRIFGVARGDLDGAGYRKLVREHLGKRANVEEAAWERLAARLDYLSVDITKEEGAKALADKIGGHDSLTVFFAVSPSLYPAACQALQSAGLTGPSTRLVLEKPIGRDLESSKATNAAVGAVVDESQIFRIDHYLGKETVQNLTALRFANVLFEPLWDNKSIDHVQITIAETEKVGDRWPYYDEYGALRDMLQNHLLQLLCLVAMEAPSGFDPDAVRDEKVKVLRSLRPFTKDNVAHDTVRGQYVAGVVEGTARAGYLEEVGQPSKTETFVAMKVAIDNWRWAGVPFFLRTGKNLPDRRTQIVVQFKPVPHNIFGQVTQGEMQANRLVIDLQPEEDISLSVMTKRPGLSEEGMRLQSLPLSLNMAAPGARRRIAYEKLLLDAFRGDRTLFVRRDEVEAAWRFVDGVAKAWADAGIEPATYAAGTWGPPSAASLIAPQGRGWKS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Length: 488
Sequence Mass (Da): 53907
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A0A7R8ZME2 | MAAAAPEASGMAGEICRRNPKEVYKLMQRLGCGTYGSVYKGMRIETGELAAIKVCRFESAAEMVPLQQEIAMMKGCHHENIVTYYGSYYWNKKFWICMEFCGGGSLHDIYNVTGPLQERQIAFCCREVTRGLAYLHGQGMMHRDIKGANILLTDGGNVKLADFGVSQYISSREAKRKTLIGTPFWMAPEMALADHGGGYNQLCDIWAVGITSIELAELQPPWYDLHPQRVLTLLASSKLKPPPGLKDKTKWSPDFHNFIKVTLTKNPKKRPTAEKLLKHDFLRGHLTKALTLELLDRARNPLRSPDSSDLDEDEALERISVPLRIPSKPSKERTKSELNMESVNFDPPLVTALSAEPPPARYPDPSSDWGSILEKLDDVKFDFDTAWTSEEDRKGGEDDPEANYCRDPTLPLPSDEGEVVAKGSSWGRDGAQEDGTLKQESTATPTVPPRRRDRRRPTPPRIQSNGLPPTPKVHMGAGFTKIFNGCPLTIHCSASWVHPATRNQHILIGSDEGIFSLNLKDLADDCMELIYRRRTTWMFVMKDVLMSISGKTPHVYSHDLVALHARKQGGLTTKLSVTLHMNRIPDRLVPKRFAPSTRLSETKGMLRCCVRRNPLNGYKYLCGASTERVFLMQWYDPLHKFMTLKTFDCNLPPRLRTFEMVFVPDAEYPRVCVDVRVPHPESAQLCLEMLDLNSDAACLTPGLDAGGQQDEQALAGHVNLKHVSQLDRHTLLVCHDNVVQFVDLDGKLKTTPGREGPAELAADFEIEGLVCLTDSILMFHRHGLQGRSIKEFAITQNIFDESRTFRLLGSERTVVLESRSATLDYSNPESGVNLYILTGHENSY | Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 844
Sequence Mass (Da): 94621
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A0A7S3EBF8 | MDEELFELKNYFYLGNFAAAVQEGTTLSVDDMDVKIDKDAYLFRVEVAKGNLDTVISKVGDEAPLALRAVKLYATYLKDRSNSVVVIETIKELMQDAAHASNSTFLLMSAMIYAQEKDFDNALRLANKGITMEHKALKVQILIAMDRVDNAKVELEIMRREDEYATLTQLCSCWVNLASGGSAVQEALYTYQELLERHGSTEPLLNGVALCQIALNKYDDAERTLQEALGKNPNHPDTLANCIVCSMHKKKRQELVDRYKAQLETVGGEDHAWLNAEKQFRTMFDSAVASAIADV | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Location: Cytoplasm
Sequence Length: 295
Sequence Mass (Da): 33014
Location Topology: Peripheral membrane protein
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A0A2D9WQI6 | MKVRVNNIKTYSYHGCLDEEGVIGSDYRVDVEVDVKNKLAQQTDNLSQTVDYSDVTKIVVEEMGIRSKLIETVSARIIRRIHNECEHVSSVIVSVTKINPPIDGDVETVCVVLNSSDI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 118
Sequence Mass (Da): 13178
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A0A0A2Z437 | MIFNRYDRYPLWRIIVDDIFQANKTVMLLLIALLISAVSTIWVTHLTRLAISEKNQLQTEYQALQSEALNLRLEDSALSDRTRIEGIAKQLGMQSTQDDQEVLIIE | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 106
Sequence Mass (Da): 12263
Location Topology: Single-pass type II membrane protein
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A0A078BJF6 | MTSVALARKWRPKSFASLVGQDHVVRALTHALDHDRLHHAYLFTGTRGVGKTTVSRILAKALNCTGPDGQGGVTSQPCGVCPACTEIDAGRFVDYIELDAASNRGVEDMTTLLEQAVYKPTAGRFKVYMIDEVHMLSNHAFNAMLKTLEEPPDYVKFVLATTDPQKVPVTVLSRCLQFNLKQMMPGAIVGHLQQVLQAENVPADDAALRLIARAAHGSMRDALSLTDQALAYCAGRVETEAVQQMLGTVDRSDLLLILQALASQDGVALIHQADALEARGLSFGAALEELAALLQTIALLQLVPQAADADDPQHEALVALAAQLSPELVQLAYTTVLHGRNELSLAPDDRTGFTMTLLRLLAFAPVIAGSVPSLPPGGLALPKAAAPASPPSQSAAAQVAAQREQPATKSAPPVQTAAKAMPRTAATLSAPLAPAAPVLAAEEAPATNYAAKPEPQTQPQPTPPRPADIKPPLQITPHIASDTDWPTLVQRLDVPAGLPRALAQQSELVAMQGTEWLLRVPNEQLTRAGSLDKLQTAVRQALGQDIVLRAEAGEVTDSVMQRDARAKAQAQADAEAAIRNDPLVLQLMHDLGAQIVPGSLKPMPPSAQPTPA | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 612
Sequence Mass (Da): 64795
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Q5MA12 | MLSHRQRLGKHGRATCRETCTCGSGRGPRYTVLICVGSRNSSEIVMAQKQIWSGIPLFPVLVMFFISRLAETNRAPFDLPEAEAESVAGYNVEYARDAILNSSLLAEANVPGSRGLILTETRGGSLPTSKYSILGKPKKVSA | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Cell membrane
Sequence Length: 142
Sequence Mass (Da): 15385
Location Topology: Multi-pass membrane protein
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A0A3B8ICC9 | MAADNPGILISFILYLLLMLGVGWYFYLRTKNLSDYVLGGRGLNTWVTSLSAQASDMSGWLLLGLPGAAYNSGYEVSWLAVGLALGTYANWKLVARRIRVYTEIAQDSITLPDFFENRFHDKSRVLRVVAALFILLFFMIYTSSGFVAGAKLFVTVFGWEYHTSLIIGVLVIISYTFLGGFSAVSWTDFFQGMLMFFAVILVPAIGLGMTGGWAGLKGEMSAANPNMLDAFTDTTGQRLSWIAIVSSMAWGLGYCGQPHILARFMAINKAENVRKSRLIAMIWVVIALGAAVLIGMVGLGFDANQVLTGGDAETVFMGLVNTIVHPAVAGVLLAAILAAVMSTADSQLLITSSSLTEDIYKAFINPKATDKQLVLLSRLAVVIVALIAVVIAWNPDSSVLSLVAYAWAGFGATFGPLVIMSLYWKRMNFTGALAGILVGGVTTVVWKEVLSEYGGIFQLYEIFPGFVLSLLAIYVGSILTKPPVVEIENEFVKFSEELNNPK | Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 502
Sequence Mass (Da): 54409
Location Topology: Multi-pass membrane protein
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A0A1B8J865 | MSSGAGLLVLFGRFLARFGAGCALWAICALCLLDAKSAPNALESKSTPKIALESKKVPESKKASESKKAKNAESSAHSADSAASTQATINKFATIKSKLDSSAQNAKIYASLQGAKNQGKKSAIDFGANADPGAPMEFSLDEGPILESESILGAESILQESFLGESILDEPILGAESDFLASNLPESKISESKIPESNPQKSIFSPESSQPKPNHINANQPKPFPLESFLPRQSAPDSSPAFLVPPPKPKIPTNPKSRYIQLTNNLPVYILPAYYSFSTPYSTRDIPVEMKFQVSFRVVFLERLFCKYCGFDFAYTQTHWFQIYNTQDSKPMRDINFSPSINFNYARQIPLFGGYITWLRFGYLHISNGERENNLDVGLADKRNNGLSPQDAGWFSRSKSLDRFVVQADWQRGRFGLSLRAWMPLSQYILSDRGDNADIASYIGYGDIVLSYVYKRHRFELYLNNIFNNYFSADFWDWKGRAELGYTYGLSRRVGLYFQLVHGYGDSLYEFNYRVTRAGAGLRLNF | Cofactor: Binds 1 Ca(2+) ion per monomer.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Cell outer membrane
Sequence Length: 526
Sequence Mass (Da): 58758
Location Topology: Multi-pass membrane protein
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A0A7R8ZMS9 | MQEVVSFLSRRTPGFLLNGGQVRVLRTPTEFYEFLMFRMASARKRVGVASLYLGTGSMESHLASFYQTPSLRGIWWKYLPQRYNEVIGLQHMKILVFDECVLMTGANLSEDYFTKRQDRYIVFDNAVHLSNFFYGLIETVSQFSYTLTEDNELEVKDGWGVNPIHSPYSDFVRKAGNAVRNFLNNEMMKQRELLERSASDASIAASSFDGKSGLAALFGRQTKGDTRVYPMVQMGELNIHDDFLATQKIFHGAEPGSLLKIATGYFNLVTDYKQILLDRSRANVQLLMAHPTCNGFLGAKGPAGGIPYGYTMLAKTFFDSVKKSGEGLKRISLWEYQRPKWSFHAKGLWYYPKGEYLPSVTLIGSPNFGYRSVYRDLEVQLCLVTVNEELRRALNEEQKLLFEPHSSIATGETFSAVDRRPPLWVCRVLLLLWVEMDPALLRQRDAFKAKAMDTPTIENKRSSGPSRKSLGNEAFLREVSKRRSLASSSSSGSSSTPKSIDIVNYKTLQGSSAHKFSVLAKCVQHLKTRHLEGNFECCTVEQLLDETCQLDIPLKTRQWLSSEALPNNPKVEVVDGVKFLFKPPYRIRDKKSLLSLLKKHDLKGLGGIFLDDIRESLPRADKCIKVLGDEVILIQRPVDKKIVVFYNDRSCQIELDDEIVKLWRSVAVDSIDDKKIAEYLSNQGIRSMADHGVKQMRPLKRKGGGGKRKGFKKPKDNEHISDVLQHYEDGT | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 731
Sequence Mass (Da): 82909
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A0A369ASE8 | MNDILATFFLVFCRISSFMVISPGFSLKQAPNLLKGLLSLSFSVTVLSSLQKIVVFQNLFIFSLQSFKEILVGMALGFIVQLVFSAIEMAGQIIDFQVGFSMGSVYDPGVGIQGSNYGRLYYWLALAVFFFTDMHHLVIDNLIQSFSIIPITEMSMHGNTVEGMMILFVEVFKISILLAAPVVLVALVTDCVLGIISRSVPQINVLMLGMPMKILISFFFVLLFMPNLIESIQKVLPDISRYLNEFMESLVR | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 28155
Location Topology: Multi-pass membrane protein
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A8B498 | MLNNKFTANQITEYNLTNLKKLVEQGLKGVDKNHPHFNRVKICCTLGPSSFNVEVIAGMIRAGADIIRINFSHGNTDDHTQIFHKVQQAMQLTGKTVAIMGDIQGPKLRIAGFSNPDNCIELKEGQEFTLDHNNVNGDESRVYLPHKEFFAVCEPNDDIILNDGYIRLVATSVDRQAMRIVTRVKTGGKLGARKGITIPTRILPLSGLSPKDLGDIRNACRLGMDWIALSFVQTKADVIEARDYIAKLHAENPASFCPRVCSKIEKPTAVLDIDDIALLSDMLMVARGDLAIETCLSKVCSIQKYICERARYHGCQAMVATQMVESLIENTVPTRAEVTDVASVCFDGANSVLVTAETAAGHDPVNVVKVLRSILTTTEQSEAFIKQVLTDNYINQRTSKEHKRPDSIALGACLLARELGAKLIIVFSKSGNSTGRVLRQLPHCPVLCITSEQRSYQWLHMCWGCRPVLHPGNIDSMKTLISVADTHALESGQAERGDAVVLVFGTPFSDVNRKGCNNIMAHVVGGGSFNNSTDVEYGVTPQLAELTPVVGDS | 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: 553
Sequence Mass (Da): 60525
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W5XJR4 | LGAWAGMVGTALSLLIRAELAQPGSFLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNIAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 218
Sequence Mass (Da): 23288
Location Topology: Multi-pass membrane protein
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A0A7R8ZTD4 | MPAAKRKVSASTSQKSVGKPGASARATRAQKRRELKDEQECSTSAQNGFCSRDRESRTPSPASVVSVQDGEPSPKEKKQEVPDPCNGSDFSSNIVESHVGSPGKPLSNKSRALLRCFRGTASADKSRRKILSNESNSPATASPCDSHLITEYFEKSSPISSLGVGNGPNLEKVSNRVDDFLVPGSVNGNHCPSSAACDSELYRSSSDESESEGKENRLISNGCVEDTHPDLCHSIPHRIQSPVALGNVSQPNSSSAPPSTPPTSRAPPSPPPAPLPASPSSLDLKPQPPLPTLSVKPVPACFSPSSAFSKLKLAFTPQPPQKERRPKEKKGKEKRAPPCPPAAPSSRPLTSYFPSVRRSSRKPASKLQQEQLKEWEQRIASDVEEGLEVRCFPNKGRGVVALRRFQKGEFVVEYAGELVDMKEAQVREVRYAKDRNKGCYMYYFEDKNVQWCVDATKETSRFGRLINHSRTRPNIVTKTITLDGLPRLVFFATQDIQVGEELLYDYGDRSKRSMEAHPWLAY | Catalytic Activity: L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine
EC: 2.1.1.361
Subcellular Location: Chromosome
Sequence Length: 522
Sequence Mass (Da): 57259
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A0A182HEM8 | MVFMAYELAVSPYVQQRLYEEIVETNKQLGGKPPTYDTFQKMPYMDMVVSETFRKWPAGAFDRKCERDYVLDDGAGLKFTIDRGTCVWIPVHGIHRDPKYYPEPDKFDPERFSENNRAKLDMTMYMPFGAGPRNCIGSRFALMEIKAIMYALLLSFRIERNEKTSVPLQLVKGFAGLNGEGGIHLQLTLRR | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 191
Sequence Mass (Da): 22049
Location Topology: Peripheral membrane protein
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A0A949ZAE5 | MADELVIGRVIGPFGVRGELRLWVVDAAAVRDGLEMNFHLEKGETRRVTLASVRKHGKGLVAQLQGYHDRDAVALLKGARIAIKRTHLPRLTDNAHREADLVGLCVIDTRLGLLGDVQEIRHYPSCDMLVVGSRAMLVPMLHAYGLRVDRAARTISVDLPDGFEELA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 167
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 18421
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A0A8C0SNZ0 | MSVLVPQLLRGLTGLTRRLPVHRAQIHSKPPREQLGTMDVAVGLTSCFLCFLLPSGWVLSHLESYKKRE | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Location: Membrane
Sequence Length: 69
Sequence Mass (Da): 7769
Location Topology: Single-pass membrane protein
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A0A410D704 | MSTILYNDRFIDRSQGKVDMEDRGYQFGDGIYEALRVYNGKMFLLDLHMKRLERSARELRLALPYATDHLAENLDKLIKENAMDYGYVYFQITRGAIARKHRFPEQPIDTVLTASVEATDKDEDLHADGIKVSLLDDIRWLRCDIKTLNLLGNVLANQEAFERGAADAILHRDGVVTEGTTCNVFMVKDGVLITHPADHFILNGITRIFVLQLAERLGIPVDERTYTTAELLAADEVFLTSTGVRVTPVLQIDDRQVAGGKPGPITNRLLEAFNQDVEQFVTAVNA | Function: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction.
EC: 2.6.1.21
Catalytic Activity: 2-oxoglutarate + D-alanine = D-glutamate + pyruvate
Sequence Length: 286
Sequence Mass (Da): 32184
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A0A182GWW5 | MRWKELSWFAIVVIVFCVSAGDAFESYRLPNTTVPTHYDLFINTEFHNDDLDYNGTVKIVINVLEDTKQIVLHSSRSILVNVELKNDNQLPLAIVNFEFDNDREFLIVNTASVLSGGSQVVLEIDFLNSINRTDQAGFYRTTYTADDGTLKYAGVTQFQACDARSAFPCYDEPGLKTTFDVRIACGVDYHARSNAEIASISILPEGKKLVTFKRTPLMQSYLLAFLVSDYAVQRDFANAMKKIAVQSMARPTRASQLSFSLDASVKLIDELQTYFDHPYEISKIDSVGIPNSDFSAGAMENWGLVTYLESYFLISESSSDNNRRSVSTVIAHEFAHQFFGNLMAPKWWSYLWMNEGFATLYEYYLADRTHPELLIKQRFSSSALQSALQADASATVRSMTHYVETVEEINRLFDRIAYEKSGSVLRMMHYALGESTFVKGLKQYIKQRQNSVVVPQHLFDSLQKVAAEAGVLPPNASMTMILESWSNQPGAPVVTVTRQPGTDDVIFTQKRFFSTTQPTENAQTWWIPVFMYTNSSAGAHEKTPLFWIPQGSKQVTHKIPIEQDDVFLINPTQTGYYRVNYDEQTWSTLISILKTNPTSLDPVTRGQLIDDSMNLANAGLLDHDKAFQILDHLRNETNFFAWKSAYRNILDLEKLLAVDPEALDLFRKYLLGLVDNLYAVHGPEKRKDQHTNDHDAQLIAIDLACRVGQQACLDQAMNKLNVLQQRTMLAIRSEAEQKLYCHGLRTGKEVDLDKFTEAFELEDDARGRRYLVESMACVGSRGELERVLEFLVELNREVERFLEVAAEQGVGGFTVVTEFLTREKDHVDEIFGSKRSMEKLLNKLADRIVDQENADRLRLMMKVLPVSSKFAANIGNRLEEQIRWQEHNLPRIRKVLQGYA | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 900
Sequence Mass (Da): 102391
Location Topology: Lipid-anchor
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A0A3B8IFX1 | MQGVIALEGLEFYAYHGVHPEEQVIGNRFVVDLEVVTDVSKAVSHDELEGTVDYGHLYKVVEEVMAEPVKLLEHLGGKIMDRILQELPAVTQVMVSVAKANPPVGGVARQSKVRLTQARNI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 121
Sequence Mass (Da): 13302
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A0A7V7WRN7 | MACTTICRRSTGPLGSLVLAAQNGALIGAWFVDQRHFPQASASWRESPDDALLQIAGRQLGEWFAGRRRVFELPLAPVGTPFQQAVWREIAGVPFGAKVSYGAIARALGQPKACRAVGAATGRNPLSIIVPCHRLVASDGALTGYDGGLERKAALLQFEQSDGCANWGQEATVERFAH | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 178
Sequence Mass (Da): 19001
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A0A099TXZ3 | MKFHDYLFDLPTYQAGKPLEEVMASYHIPPENIIKLGSNENPFGVAPSAKKAIIEYANLASVYPDDSYSDIKKSLANKYDVKSDNIIIGSGSDQIIEFCVHSICDSAKTILMAQYTFAMYEIYAKQCNANIIKTTSFFHDLDSMIDMYHRHKPDIIFICTPNNPLGEALKRVDLIEFLNKISTDCLVILDCAYMEYCAYKDNDFAIYPKDIVEFPNVIYLGTFSKIYGLGGMRIGYGIANDNIISLLHKLRPPFNVTTLSLRAANASLQDIDFISKTLQNNFTQMQRYYVFADEYGLEIIESYGNFVTFLLHDKLNSTTISSFLLKQGIVVRDLSSYGLNAMRITIGTPSQNDFLLSKMAGILISYKDSF | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 370
Sequence Mass (Da): 41829
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A0A951C152 | MRSGQTPGVPQAPERRPATLEAALGLGGNVGDVRAAFARALLALAAAPGIELLRKSSLYRTAPWGPVSQAPFLNMAVLVRTTLSPHELLDLCLSVERQEGRVRAQRFGPRTLDLDILAVGELVLSDERLTLPHPRLLERAFALVPLAEIAPDLVIGGVTVAAAASRVDRTGVERIGP | 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 in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 177
Sequence Mass (Da): 18803
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A0A3C1Y762 | MVNTDKTICRMIASMLAGYGVKDVVISPGSRNTPLVMAICRNPVLRTRQIVDERTAAFIALGMASGCNRPVALVCTSGSAVLNFAPAVAEAYYRKTPLIVISADRPRAWIDQDDSQTIRQHGVLGGITQASCAVDDVTEDVGFQNRVLNDVLATALHGRRGPVHINVHLSAPLSDVTESGDNNDFSRVIEYIEAPQVISTAQSRRFAEYLHGRKILVVGGFMPPDARLNKALGELAALPQVAVVVEALANVHAAGAYNSPSAILSGLTPMERSDLAPDVVLSFGGALVNTQLKEFLRGAAGSETWCIGRNETTVDCFRTLSRRVEIEPAGFFHRLAGAMAFLNRKNGSTCGYSEKWRKATASAMASSADFMSATPWSDLAVVSHILQRIPHNANLQLGNGMSVRNALLHDLGAFHRVDSNRGVSGIDGCVGTAVGAASMYNGLTYAIVGDMSATYDMGALAYAAMAPGLRLIVVNNGGGGIFHFVGTTRNLPEKDMMVNSPAPPLRQLAEAYGLRYFSAGDFGSLAAAMNSMADRSPTPAVLEVFTDGESSAGIMRSYLSRNNLTNE | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
EC: 2.2.1.9
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Length: 567
Sequence Mass (Da): 60371
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A0A1S8D6D5 | MSRAPLFAAALGAALLLAGPALAQSVSLDLGQAGQPGATARLVQLTALIGLLSLAPSLLVMVTAFARITIVLSLLRSAIGAANVPPNPVLIGLSLFLTFFVMQPVVERAWEDGIQPMVEGRIGEMEGLERSAEPFRSFMAANVREGDLSLFLDLAGLAPPGGDAGKTPGKAIEAPWRALVPAFMVSELRRGFEIGFLVFLPFLVIDLVVASLLMSLGMMMLPPSAVSLPFKIIFFVMVDGWRLISESLVQGFAN | Function: Plays a role in the flagellum-specific transport system.
Subcellular Location: Cell membrane
Sequence Length: 254
Sequence Mass (Da): 26858
Location Topology: Multi-pass membrane protein
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C0HAA8 | MGFLIFTLFLFFTVICAERNGPIQTFVIPHSHMDVGWVYTIQESMHAYAANVYSSVTEALTQNKQRKFIAVEQEFFRLWWDSVATDKHKKQVRQLLKESRLEFVIGGQVMHDEAVTDLDDEILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPVLFALAGFHAHLISRIDYDLKDGMQKSKKLQFVWRGSPSLKEQQEIFTHTMDQFSYCTPSYLPFSNSSGFYWNGVALFPDPPKNGIYPNMSLPVTKETLHSYAKTMVQNIQQRAVWFRTNHVLWPWGCDKQFYNSSVQFSNMDPLVEYINQNSKEFGVTVQYATLSEYFQAVHQSNLTWEVRGSEDFLPYSTEPFQAWTGFYASRNVLKGIARRASSQLHAVETLFTRYRVNYPDGPVPKEEALQKLKALRWAVSEVQHHDGITGTESPKVSDMYIEHLTQAMMGVEELLAALFLLPQALGTASNSEAFNRQDSHSKGSHQDLEQHIIVYNPLAWNTTAIINVTVTFPMASVFDDQGQPVPAQTQSSADSNMTYDLFIVVDLGGLQHRKYLIKFSEKPSKEGSLTHQAWVVSFKRLNVSQELKTGRRLLPVLNECYKIMLDQDTNLLHSITDRHEKRTVRMSQDFWEYQVNGNVSAGPISDNYIFSANGSAVRAYKAVKMDIVPGKIITEIRQYFYREEADAEYTYSVTTRVPQSFPRGRLCYRLEQSYSLGPLVVNTEAVLRTKTSLKNNRTLFTDDNGYQMMKRPSRTFVNDTVARNYYPMVRMAYIEDDSSRLVLLSERAHGVSSQSEGELEVMLHRRLWNNQEWTLGYNLTLNDSSVVRPVLWMTLGSLAATSSLYQREALELQHRPVVMPIDRPQKAWRKEPRTRSPIRSVVLPDNLHLLTLSVPGWVYNSNHTLHLRNIETGTPGSTQPDYDRVLLRIMHLYEKGEDPVLSQPSTINMKEVLRGMGEVRALEERSLTGTWDIADLQRWKWKASEDPGRGVSVGVKRSSVGVRGEFNVTISPKEIRTFFVYFKLK | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.2.1.-
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Length: 1016
Sequence Mass (Da): 116546
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A0A7R8WMW9 | MTRDALSEIHALMERMGQSIIGQREVVERLVIGLLANGNLLVEGMPGLAKTRAIKALAKNLECDFSRIQFTPDLLPSDVTGTEIYHQSEDGAEFRFQPGPIFANIVLGDEINRAPAKVQSALLEAMEERQVTVAGKTHKMPALFMVIGTQNPIEQEGTYPLPEAQMDRFLMHVLITYPPVEDEVLVIKLVRGEEAAASAKPSDNAENEPPPAISQETVFQARREIAAVYVSDAMERYMADLVNATRVPKEFGSNLGRWIDLGASPRASLALDKSSRSHAWLSGRDYVDPADIQAIAHGVFRHRIGLSYEAQGEGINPDQVVDEMIAQVAFA | Pathway: Porphyrin-containing compound metabolism.
EC: 6.6.1.1
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Length: 331
Sequence Mass (Da): 36358
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A0A1S3Y6A8 | MLLAVLFANSEGNILVERFNGVPAEERLHWRSFLVKLGAENLKGVKNEELLVACHKSVYIVYTVLGDVSIYIVGKDEYDELALSEAIFVITSAIKDVCGKPPTERSFLDKYGKICLVLDEIVWTGLLENIDKDRIKRLVRLKPPTEF | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16625
Location Topology: Peripheral membrane protein
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