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stringlengths 6
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A0A1S3CLN5 | MPSFRAFLNSPVGPKTTHFWGPVANFGFVAAGLADVKKPADMISGRMTAVLCVYSLLCMRFGYMVRPRNYLLMGCHAANESVQLYLLSRWAMGQRKTVDYSNE | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 103
Sequence Mass (Da): 11529
Location Topology: Multi-pass membrane protein
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Q7ZW80 | MQVTRSQISLFLCLLSCVSVIGARYTPDWTSLDSRPLPGWYDEVKFGIFVHWGVFSVPAFGSEWFWWYWKGAQNPDYVQFMIKNYPPGFSYADFAPNFHAQFFDPDAWADIFEASGAKYVVLTSKHHEGFTNWGSPTSWNWNSVDDGPHRDLVGDLGNAIRKKGLHYGLYHSLYEWFNPLYLSDKQSGFKTQEYVARKAMPELYDLVSRYKPDLIWSDGDWEAPDTYWNSTEFLAWLYNDSPVKDIVVVNDRWGNGCYCKHGGYYNCADKFNPQKLLNHKWEKCQSVDKISWGYRRNMKLSELMDLPELVQDLVYIVALGGNYLLSTGPTADGVIAPVFEERLRGIGAWLQINGEAIYGTSFWRVQTENATVPVWYTAKKSTVYAIFTTNPMQNTFQLSAPNTTDSTVVTLLGSPKPLKWAPLQSSGLMVVLPELPFSPAYAWTLKMEGVA | Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
EC: 3.2.1.51
Catalytic Activity: a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a neolactoside nLc4Cer(d18:0) + L-fucose
Sequence Length: 451
Sequence Mass (Da): 51543
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A0A174EYE9 | MRRLVTGKQMKEIDAYAIQTIGILSMVLMERAALAVADELMQEYQRRGRKPVLDARVLVFCGTGNNGADGAAIARILHLRGISVSIITVGDRSRWTGEMERQISIDEKLGIAIEDFGGYLPGRFDVAVDAMFGVGLSRELEGEFREAVVFLSGLKPEFTVAVDIPSGICSETGRILGAAVEADLTVTFGYEKVGTAIYPGKGYCGRVEVKDIGFPGYDGYSGTRFFTYDTSDLSRIPQRKQDSHKGTYGKVLIAAGSGGMCGAAYLSALAAYRTGAGLVKILTVETNVQILQTLLPEAIIASYPEGMEAEEPEAFRELVERECAWASVIVLGPGLGRGRHVVKLTEYVLLSAYVPIILDADGLNTVAEYPHLSEFFTENVIVTPHLGEMARLTGQEVETLKEDLPGAAVAYCEDKGVTCVLKDAVSVVAGKDGSVFINSSGCGAMAKAGSGDVLTGLIAGLIALGLQEDEAASLGVWLHGLAGDRAAKRKGDHSILAREIADSIMQEDDNGRTIQQGLCGNQP | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 523
Sequence Mass (Da): 55783
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T1FMR9 | MHLLILMAVLSMSPAAAAIISSNDADQVIGDLLKRVPLIDGHNDLAHQIFARKKNKINDLDLQNWTEVHTDIKRMKQGGVGAQIWAVYAGCSTQYRDAVRACLEHLDTIQRFVYKYPNELQMAYSSQEITETFKKGKISSLLGVEGGHCLDSSLSVLRMLYQLGTRYMTLTHNCDTPWVTNNLRDRNATNVAGLTQFGKDIIREMNRLGMIVDMSHVSKAAMVDVLATSVAPVIFSHSNSYKLAPHTRNVQDDVLLLLKKNKGLIMITFPSSFLDVSGEASISSVADHLEYIYKLIGIDHVGIGSDYDGTPSLPVGLEDVSKFPDLLKYLYVNREWTVTMLEKLIGQNFLRVFQDVERVSKSLKGMMPLEDRLPQSQLVNTTCRSAEY | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 388
Sequence Mass (Da): 43428
Location Topology: Lipid-anchor
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D8J2E9 | MNFETWEPIYESIITDFGFDRREDERARDALARLVEPFDERRLAALGDATVAVAGAGPSLPDDLDRVAGADYVIAASTAADTLLAAGLDPDLMVTDVDKNPETARRLTRLGTPVAVHAHGDNLGLVERWVPRLGAESVLPTTQAAPRGPVRNFGGFTDGDRGAFLADHFGASELLFPGWDFEDPSVGATKARKLRWAERLLYWLETRRGERFGVLDGRRDGIEPVV | 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 diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP).
EC: 2.7.6.3
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Length: 226
Sequence Mass (Da): 24743
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A0A961A9M7 | MDQKEYTQDLQALGSHTDYPTRPDISILECFPNPSPGSDYSIRFDCPEFTSMCPVTGQPDYGRFEFEYEPDELCLESKSLKLYLFSFRNEAAFWEELSNRIADDLFTLLKPHSLRLTGYMNPRGAISITTTVRRGRSASER | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
EC: 1.7.1.13
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 16237
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A0A174MZ94 | MGTEKRTEKRTEEQRRAEALALLKHILDIPSVNGKDREQETAVYLAEYLKRKGMETRVQLIDEHHGNVIGVLKGKTEETILFNGHLDTVPYGDINEWNTNPAVCTEQDGRLYARGASDMKSGLAVMAFVLGELAESGCVPQKTIVFAGTCDEERGGLGAKEIIKEYPDLFPELLLIGEPTSCQAGVAQKGCIWLKLSVSGKTSHGAEPWQGINALEQGFGLLADLREELKREEHPVLGRSTLQITMAEGGIAPNMTPDRAKFLADIRIVPPLNEKEVLNRLECLMQKRCEVYNGGLAFVPEITNYRMPAETGPENQWLHRLKGFIGDDAGETGINYFTDASILLTAWPDSPALLFGPGEPQMCHKPNEYVEISKYLEAIRVMEKFCWYIAK | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 391
Sequence Mass (Da): 43505
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D8J3R4 | MTDDVDRRAFVERLLAFDTTDGNEAPAQEWFGCRLDELGFETYHWKPDSERLVTHPSFPDDPAEIETTGRPNVAGVIELGSGKGPTLLLNGHADVVPAEADQWSSDPFEPTWTDETLTARGAADMKAGLVASVFAARQLAEADLDGRVVVESVVGEEAGGIGAAESAQDPPYPVPDAAIIAEPTDLTPVIATEGTLMKRLTLTGRSAHAATPWHGEDVLDHFERVRNALADLEAERARGITHPLYEPFPRPVPIVAGTVHAGSWASSVPAHLESEFRIGVAPGETVDEVEQEVDRRIAAVVADSEWLTEHPPRFERFSVQFEPAEISPEEPIVRAVCEALDAAGRDSTVRGATYGTDARHYIEAGIPTVVFGPGSIRQAHFPDESIDWSEVTTGIDLLESAGKRFFTRNTR | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 411
Sequence Mass (Da): 44556
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Q6P978 | METVVHLMNDSVEFYKWSLTIADKRVEKWPMMSSPLPTLGISVLYLLFLWAGPLYMQNREPFQLRKTLIVYNFSMVLLNFYICKELLLGSRAAGYSYLCQPVNYSNDVNEVRIASALWWYYISKGVEFLDTVFFIMRKKFNQVSFLHVYHHCTMFILWWIGIKWVPGGQSFFGATINSGIHVLMYGYYGLAAFGPKIQKYLWWKKYLTIIQMIQFHVTIGHAAHSLYTGCPFPAWMQWALIGYAVTFIILFANFYYQTYRRQPRLKTAKSAVNGVSMSTNGTSKTAEVTENGKKQKKGKGKHD | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that specifically elongates C24:0 and C26:0 acyl-CoAs. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
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: Endoplasmic reticulum membrane
Sequence Length: 303
Domain: The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
Sequence Mass (Da): 35226
Location Topology: Multi-pass membrane protein
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A0A7W0F830 | MKSSKKNFAKRISVDYSASLSGAIGAGGLSEGDLSKISASVKTAVKKLNARRASGEVGFAELPDDFKNASDIKKYADKLKGKCRNFAVLGIGGSALGPRALIDALAPSFYNMRDLAGRGGRPRIIIADNISPEFVKGIFDIAPVSDTVFNVITKSGTTGETLSIFSAALAMLKKKTGKSWKKHIVITTDPEKGYLREFARKNGIDSFSIPSNVGGRFSTLSSVGLLPAAAAGIDIKKLLKGAGDAGKFCFKEGLKDNPAALYAAMHYLFYKRGRRINVFMPYSENLATVSEWFAQLWAESLGKKKDRNGRDVFVGPTPVKAKGVTDQHSQLQLYTEGPQDKVVTLLSVEGIGSFKIPKLGDFVFGGRDISELFKAEEAGTALSLGEARRPVITIKMPEVTPEYVGQLLMMLMAATAIYGEMLNINTFDQPGVEYGKIIAKKILSAKGRGNKRQSNHKGNNVDCLSQTPEKRRRAPRFADKYRV | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 483
Sequence Mass (Da): 52338
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E7FC00 | MKMEDVSLSSMDNSKMEGFAQEILSDLVEDACLGLCFEVHRAVKQGYFFLDDTDQESMKDFEIVDQPGVDIFGQVYNQWKNKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIASGNNTNKSESDQEDNDDVNDNDWSYGAEKKAKKRKSDKNPNSPRRSKSMKHKND | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription.
Subcellular Location: Nucleus
Sequence Length: 175
Domain: The C-terminal SGF11-type zinc-finger domain forms part of the 'catalytic lobe' of the SAGA deubiquitination module.
Sequence Mass (Da): 19872
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A0A913ZYR3 | MTSLGLYVFLALAVCVAAAPQPKSVIEFGDMIRCLTDRNIISSWLDYDGYGCYCGFGGTGTPLDDTDRCCQAHDNCYDVVMKSGKCPYESHVYIINYDATIENCRQPDAVVTCKRAEDYGFLDSPWSECAAAMCECDRAGAECFAASHYDTSLKNWSQDYC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 161
Sequence Mass (Da): 17814
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A0A133Z7L7 | MVKTRVAVIGGGLSGLVAAYEISRCDPNADVVVYEASDAVGGKLKTVDLATGSVDVGAEAYLAFRADATRFFTSLGLKDRLRYPSDLKSGLWIGDGTLHSVPSRTVMGIPADSSSVKDLVDSETCARIDAEGEAYPIPWVEGEDALLGALVAERMGQQVVDHVVSPLLGGVYSSRAEDLGLRATIPELAAAMDDLSNHGESVTLTRAAAAVLQQRDEAREARVAGGAADEESSSASAKKPPVFASFVGGYRDLIDALVEQSSATIRVDSPVTAVLPAEAGSSHRFRVVSGSSTETEEFDAVVVATPADVAGQQLAEVAPVAADILGSMDLASSVVLGLRLPNEEAIPEKTGILVSPDAGLHAKAFTFSSRKWPHVDDHVGAFIRASFGHWGDDSLVREDEDTLVKYAIDDFETITGQRLHPEETVLQKWWGGLPRYGMGHDELINVALKDISQVEGLEAAGAIWHGVGVPACIAQAREAAKKVMDTVM | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular Location: Cytoplasm
Sequence Length: 488
Sequence Mass (Da): 51486
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A2RV27 | MQTAGKCAVRLDLSHVFCPSSVWNCRAVNRVNGLVSCRRYSVIPPPRDEQEKAMLDRMLRVDHAGEYGANRIYAGQMAVLGRTQTGPLIQHMWDQEKIHLEKFNEILGEHRARPTLLLPLWNIAGFALGACTALLGKEGAMACTVAVEESISEHYNSQIRTLMEADPDRYTELLQLIKEFRDDEIEHHDTGLEHDAESVPGYMLLKTAIQAGCTAAIYISQRI | Cofactor: Binds 2 iron ions per subunit.
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner.
EC: 1.14.99.60
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O
Sequence Length: 223
Sequence Mass (Da): 25033
Location Topology: Peripheral membrane protein
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A0A2E4QTA4 | MTKPVLLCILDGVGLASPGPGNAVTLADTPFIDKLFETRAHSALRTDGPFVGLPEGQMGNSEVGHMTIGSGRIIRQSLEQVRHDLANGTLEALPGYSAFKQKAKEKRAIHLIGLISSGGVHSHMDHIVGIAKSLSKLGKPVYIHGLTDGRDTDPQAAKEEIPAFVSQIADIPGVELVSLVGRYYGMDRDGRWERMEIAWKLWTQGIGEEAADYNAAIAKVHEAGKTDEFLPALNLMPGDRDAQIQSGDAVMVCNFRADRARQIVELLMQTQDSAKLEPVVNIDAIATLTEYKSDFPKPVDVLYPNREFTGLLGDVVAAAGLKQLRISETEKYAHVTYYLNCGRETPFDGEDRILVDSPREVATYDEKPEMSLPEVSEKLIEQIHSGKYSLIVLNIANGDQVGHSGNIPASLKAMEFVDKYLSNIVTELEKAGGEGVIIADHGNIEELLQNGEMSTAHSMNPVPCIYIGNRKVKLHDGGLKDVAPTMLDLIGLPKPSEMEGNTLIES | Cofactor: Binds 2 manganese ions per subunit.
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 506
Sequence Mass (Da): 55009
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A0A352ZCH1 | MHSINTDELKKRFIVIEGIDGAGTTTQMNLLAGSLRALGLSCVTTAEPTTSPIGMLIRSVLSGKNEAAPSTVAHLFAADRNEHLYGKEGIAQKVEEGALVISDRYVLSSLAYQGVTCGPEIPWQLNSRFPAPGLTLLFEVDPEVCIKRIDTRSNKEIYETLEFQKRVHDMYAVMADRLEQQGWHIERINADGDIETVRQRIEAVVFAFLGVPSGGITGSASRLHS | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 225
Sequence Mass (Da): 24640
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L1J3G7 | MRRAWQRTVKAAMAWEGQGLHGGERARMVVHPAAGNAGILIQGIRASWESVVDTSLSVTLGQPPKNGLQRTLAAAGVWISRGGAQTLGHLLSGPTVSTVEHLMAALSGCGVDNARVEVSGGEVPIMDGSAKEFVSMLKDNVVELPEFERRWIVVEKEVIVDDGHGRMAMLSPPSHAERSRGSLRLHVEVNYDEKFEQGAGVTSEGEGAGGAGGWRGRWGGSRVFEFEREEFEGVASARTFCFHQDVEQMRRMGLARGGSLLNAVVFKGGEVMNEEGLRFPDEMVRHKALDALGDLSLGGRLVGRYQSVKAGHGINVQLLRKLFASGENYRCA | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses.
EC: 3.5.1.108
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Length: 332
Sequence Mass (Da): 35873
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H1XTK1 | MRPLFKSATLRLKMMLAVGGVVVVFMVFISIGIALHWRSMILQQLQQKAEAVTSAFGISVLDALIYSENENFQVEDLLESYMLGLKEKIPEIQYIVVTDTHNRVIAHTDPRMYNRLLTDELSGRLAKTTGLVSGIYRTPQFGWLIETALPLQVGGKRWGILRIAFEAESTRREIARLFYLLVGITLLLTLVVLAVLNYLIKHTVRSLMLLVQAMDSMELDSSAPLELPERADEIGALTRHFELLRQRLQNSQAQLLEAQKQIYHAEKLASIGRLASGVAHEINNPLNGIKHCVYAIEKEPQNQKQLKEYLALINEGLEHIESVVRKLLGFSRKSARDKEWVDLNQVVRQVVELLAYRLNQRHIDLQLQLAADLPPVYGDASLLQEVVMNLLLNGYDAVEDGGRVIVRTEALPSHQVRLTIEDNGMGINETDLEKIFEPFYTTKEPGKGTGLGLSVALNIVQAHGGQIVAHSQPAKGTRFEVILPYGERQ | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 489
Sequence Mass (Da): 54935
Location Topology: Multi-pass membrane protein
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X1WER9 | MSGFNRSFTLLRAAMRHQLIPKANITAKPAKHALSAGEQVIALSVMFVTILGPSGWILSHLEDYKHRPGAAQE | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 73
Sequence Mass (Da): 7982
Location Topology: Single-pass membrane protein
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T1EHZ7 | VLFLFVVCNFMLSTFLDPGKYPKAHEVKDNNAPMYKNVEIEGTSVSLKWCRTCKMYRPPRTTHCNECNYCVEIFDHHCPWVNNCIGRRNYRYFLQFLWLLIMHMLFLFSLLVVFIWQHRHDLKASNIIIAFCILIVIGLLCWPITGLAMFHVMLVSRGRT | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 160
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 18952
Location Topology: Multi-pass membrane protein
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B2MYU5 | MTYWGQLGFQDACSPLMEQIIFFHDHAMFAIIMVLTMVMYMSMILMTNKFSCLNITESQKIETVWTIAPALILLFLALPSLRLLYLLDETNDPLITIKTMGHQWYWSYEYSDFLDIEFDSYMVPTNDLELGNFRLLETDHHLILPMKTNTRIIVSSADVIHSWTVPSLGVKVDAIPGRLNQLMLYPSRPGLYYGQCSEICGANHSFMPITLEIVNMDYFIKWLNLMNEQ | Cofactor: Binds a copper A center.
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
Subcellular Location: Membrane
Sequence Length: 229
Sequence Mass (Da): 26572
Location Topology: Multi-pass membrane protein
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A0A817XGQ2 | MLTSLSIDHTLLKPDATLKQIDQLCTEAIECKFATVCIQPCHVKYVVDKYSVRVCTVIGFPLGTTTTETKLFECQQALNDGAQDIDMVINIGKVKDENFEYVQNEIEQLAKLVHSSGENNILKVIIETCLLNDNEKQKLCQIVGNAGADFIKTSTGFSTGGATLNDIKLLRQYSPKNVQVKASGGIRDSNFAKELIQAGATRLGTSSGVALMKDIPSTSNYYYGDNGTFSPPMDVTNQIQNGIIQHTSGNSNYSSGSGGDSPTSLSPVPMSSGGQFMGIGGNSNSSTSSTPTATTSGGMGSAAAAAAAAAAAASRYACVICGDKASGKHYGVHSCEGCKGFFKRTVRKDLTYTCRDNRDCIIDKRQRNRCQYCRYQKCLNVGMKKEAVQEERQKSGMNGEGESPSSPGTSIGSGSTSTHMGIGSSGSNSDDDMLIEKLIAAELSVEPKIETFHEEECSYDRLLSTTNSQLAQLTDWAKRVPHFSTLSLDDQVALVRASWKDILCCSLAYRSIMAPDCGLILSDGSYVRPHTAVDQSLQFFITRLYHDVVTIMRELNVDKVEITCLKAIFLFDPDAKDVVDTCRVSELREKVCMSLASYCKKVHSDDVARFAKLLLRMPPIRGWCIKGIENLFFAGAARSADSEIIHMIRNRQL | 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.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
EC: 4.1.2.4
Subcellular Location: Nucleus
Sequence Length: 653
Sequence Mass (Da): 71001
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Q6P2U2 | MMFNKGRVSSAFLISWMYFVYISSGLETTIDPTAESITLSDIIGNATEWMMDFTDIESKFSFRTLEEPEDDLCYIVPGQPQSIKDCNFNTETKTFIVIHGWTVTGMFESWVPKLVTALYEREPSANVIVVDWLSRAQQHYPTSASYTKLVGKDVAKFVNWLQAEIDYPWEKLHLLGYSLGAHVAGIAGLLTKHKVNRITGMDPAGPTFEYADSLSTLSPDDANFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDLQNTMLMVATTGLRNMDQIVKCSHERSIHLFIDSLVNQDHESMAFRCSSRDSFNKGMCLSCRKNRCNKVGYAVNKIRTRRSSKMYMKTREMMPYKVFHYQVKVHFFGKTQLSYTDQPMKISLYGIHGEKENIPYIMPTLNTNSTVSFLLTTDADIGELLMVKLLWEKDTLISWPWWNSDTFHIRKLRIKSGETQSKIIFSAKESEFSYLSRGGEAAVFVKDKEAQSSRKNQRLHKMKMHGSSFKQNNE | PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.
Function: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
EC: 3.1.1.34
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Subcellular Location: Cell membrane
Sequence Length: 511
Sequence Mass (Da): 58292
Location Topology: Peripheral membrane protein
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B0UXE0 | MRKKNVESALLFLTGVVCLLIITNKNDSKEDDVNLKSKKTEEILHNQEDFSRTETLPPSTSYCQPNMSFYKLPEFSTLPDHIKDFLLYRHCKSFPMILDVPDKCGGAQNSADVFLLLVIKSSPENYDRREVLRKTWAEERLHKGVWIRRIFIIGTSSSGLGKRRMNRLLKLENNENKDILQWDFNDSFFNLTLKQILFLEWMDRRCPHARFLLNGDDDIFANTFNMIEYLQGQEDNDGSRHLFTGNIIQNVGPIRKRSSKYYIPVQIQESDIYPPYCGGGGFLLSGFTARTIYNMSHSVILLPIDDVYMGMCLKKAGIKPTSHFGVRTAGLRVPVGIVDKFDPCYYREILLVHRFLPHMIFVMWDEIQNPNLRCAKNNFKRTKEQGVFQREI | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 392
Sequence Mass (Da): 45555
Location Topology: Single-pass type II membrane protein
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L1IIS5 | MRSVAFAALIGSAAAFSPSMSLDVSRRQVVQTGAAAAAVAPFLQQVPAQAAMDKSGRAPVITIFDHRGCTAHANKEYTGAKANSQDDEMCVKVASAKIAVSEGDAARKLQEFISYQAKGIDGPYTGKGKK | Function: Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
Subcellular Location: Plastid
Sequence Length: 130
Sequence Mass (Da): 13533
Location Topology: Peripheral membrane protein
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I3R9R6 | MVIELTGSDLTIEDAVACARDHEEVSVSDEALKRVRTARSNLESRIGTGEIIYGVNTGFGASQNEVIDPEDVATLQKNLIRSNAVCIGDPVDEDEARMMMLLRLNSLLSGSSGVRVHVVLKLRDLLNAGFYPHVPRKGSVSASGDLAPLAHVALAMLGEGKARHEDEWVPSSEVLTSIEVDPLTTEEGEPGLEAKEGLALINGTNYITAVGALAVHDAETLLDTADTVGTMTLEAFRGISDPFRAEIHELRNQPGQKHVAERIRNGIEGSELVTSAAEANRAQDSYSLRCIPQVHGASRDTLTHVRGVIERELNAVTDNPLVLQRGAGDVVSGGNFHGQPVAFALDMLSVAVSEVANISERRIFKLTGGDAAGRSDGKTDSMPSDSLPPFLVEDSGLNCGFMMPQVTAAALVSENKTLAHPSSTDSIPTSDNQEDHVSMGANGANHLVEILGNVETVLAIELFAAYTALSYRVDSPGQKATEIVSLLEEIVTPLKEDRLMQNDFSSLRSLIRAGEVR | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
EC: 4.3.1.3
Subcellular Location: Cytoplasm
Sequence Length: 517
Sequence Mass (Da): 55254
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A0A1S3BTX0 | MEQNYSVPEAYLESEQDVSLKQNWKSISTESTISEDANGCFDCNICLDSAADPVVTLCGHLYCWPCIYKWLHVQISSNEPENTQNCPVCKASITPSSLVPLYGRGTSNSDSESKKSHLGMAVPRRPPPSMNTPPPSNSSSASYPSQELHSNYIRSPSHPIYHQQYFPQAYGNFASYAPSYLGNAVITSLLNPTIGMFGETVFTRIFGSVDGNLLPYPPYNNSISGNASTRMRRQEMQLDKSLNRVSIFLFCCFIICLLLF | 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
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 260
Domain: The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence Mass (Da): 28898
Location Topology: Single-pass type IV membrane protein
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L1JV99 | MKKGLGADVKKTKASKKDLLTEIDPICQKIIEDEVLKQFPLHKFLGEESVDPGSAASSKALSELISSEWLWVVDPIDGTTNFAQGMPMSVISIGVAHRGKPVVGVILDPFRDELFHAKLSCGAFLNGQRIVCGSESAVEDSVIVAGSPTNLRSIAPSLRGINALMPHCRSIRMLGSAALHLAWIACGRLTAYFEPDLNSWDTAAGAVILREAGGRLTDLEGSDYQLTTRAVSVSTGFVTRE | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 241
Sequence Mass (Da): 25836
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C8XTB7 | MAIHLVEYECNLFMMDECFHENDYLVSRPIYSNQIFDQVHERRNQETQSLQERLSRTFGHTDKWAVQKVKGLLPIMEWLPKYPVKQWLPGDVVSGVTTGLVCCLQGVAYALLTSVAPVYGLYSAFFPILTYFVLGTSRHISVGPFPVTCLMVGSVVLTLAPDEHFLRSVNMTDVNETMVEDTLMEVDVEAREAQRVMVACTMTVLVGLMQVAMGLMQVGFLVRYLSDPLVGGFTTAAAFHVFISQIKTILSVPTHNHNGFFSFAYTLIDVGSNINQANMADLIAGLLTISIVMAVKEINTKFQHKIPVPIPIEVIVTVIASAISHVMDLNSQYGASIVHNLPRGFASPQPPNIELIGSILGSSFSTAVVGYAVAVSVAKVYAAKHDYTVNGNQELIAFGVSNIFGGCFSSFVASTALSRTAVQESTGGKSQVAGLISAVMVMIVILALGPFLQPLQKSVLAGIVIANLKGMFLQISEVPVLWRQNRTDCFIWIASCLASVVLGLDVGLLAGLVFEMGTVVVRTQFPSCATLGNVPNTDIYKNMKDYKKVDEIPGVKIFKCNSPIYFANIDYFKEKLRDEVGFDAVRVFKKRNKALKKIHKLIKKGKLQVTEAGLVPVASLGVENKGFENEPGHEMEKQASKTDSEVKIQVDWTSELPVSVSVPRVHIHSLVVDFSSVSFLDVVAAKSLKLVVKEFIRIGVSVYIAGCDGELVRKMEALSFFDEEVNRDLLFLSVHDAILFIQHQNSIGYEDNPLAEKTIL | Function: Sodium-independent transporter of chloride and iodide.
Subcellular Location: Membrane
Sequence Length: 760
Sequence Mass (Da): 83523
Location Topology: Multi-pass membrane protein
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A0A1R1XRL0 | MSAPPAFSHLDQPSKPINNNITPWQKKLYINQDYADDYVDKTFLIEFQKNVNVRIYVYWEVVSESIVVTQHFSSILIFIALFIYLYRESVSNYHLLYTSLIGLLIGSLIWDSIMSKHSPPQPLVLNMKMVRSVITFALILYFLSPVLRTLTKDTSSDTIWALTVVFFILNLAFHDYAANNLTRISSIGSISMNAAVLACVLLASRLSSDNAVFAFLVVALLWFALFPLLRRLLIIHSKPCSIVLTIIMVILATVAFFPISKAVSLLCFSLPFFITFLCPIWLIWIQRYKNEIHGPWDEATPIVHK | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 305
Sequence Mass (Da): 34814
Location Topology: Multi-pass membrane protein
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T1FMS0 | MKLFAINILYKGTNGKVKKLTGSSELSSFGFFQRSSAQEFMDFTSKIIVERTNTSQRSSVKEQEYVCHLYVRGDSLAGVVISDDEYPSRVSFTLLNKVLDDFSAKYPAHQWPDAQENSLPFTELAEFLQKYQNPKEADAMTRIQSDLDETKIILHNTIESVLERGEKLDDLVAKSEGLTYQSKAFYKTAKKTNSCCVLL | Function: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 199
Sequence Mass (Da): 22565
Location Topology: Lipid-anchor
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L1JMG4 | MHFRVNTKGISAEAQQAVVDSIRVVPNFPKPGLFFKDLSLLLGNPAAFGSTIDALVHKYAGRGITAVVGIECRGFCFAAPVAIALKVPFVPFRKPGKLPCKSIGIDFKQSAGKHSAYFGKDRLEMHEDGLTAGSKVLVIDDLLGTGSTMFGACELVEKVGATVVECACIVEVKELAGRERVKRDIFILIEDAED | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 194
Sequence Mass (Da): 20824
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Q2MLR9 | MIMNHFLWLLPLVFPHLSSPVILLERNDGNLFHNWSYQMKGDKMVLHRSKRDWMWRQFFLSEEYMGNNNQYVGKLRSDKDRGDGTARYVLSGEGAGTVFRIDEKSGDLHATQRLDREEKSSYTLQAQAFNRITGLPLEPATEFIVKIHDINDNEPKFTRAVYAASVPEMSDVGTFVIEVNATDADDATYGNSAKLVYSILQGQPYFSVEPETGIVRIALPNMDREVRKDYQVVIQAKDMAGQMGGLSGTTMVNVTLTDVNDSPPRFAYSSYHLSTYESAEIGSTVGRIKANDGDEGENAEMKYRMSDGDGKEYLDIITDEISQEGVIVIKKKLDYETKRVYTVKVEVSNTHQDPNFFHLGPFSDTAIVKVTARDVDEPPVFSRTQYVFEVNEDTPKGTVIGTVTARDPDATDYPILYAIDQHTDPERLYHIDPKNGSITILKSLDREVSKWHNISVLASEMNNPHQRSRVPVLIKVLDVNDNAPEFAMIYETFVCENFKAGELIQTISAIDTDDPLVGHKFVFSLSSLNPNFTIFDNEDNTARILTRRSGFNRREMSVYYLPVVISDSDYPIQSSTSTLTIRVCSCDATGTMRSCSVDALLLSAGLSTGALVAILLCILILLMIVVLFSALKKQRRKEPLIISKEDVRDNVVSYNDEGGGEEDTQAFDIGTLRHPEVIESNKLRRDIIPEMLFPYHRPSPMKECADVRDFIISRLQENDTDPFAPPYDSLATYAYEGNGSIAESLSSLESSLTEGDHEYDYLSNWGPQFKKLADMYIGKDTGIAN | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 785
Sequence Mass (Da): 88270
Location Topology: Single-pass type I membrane protein
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L1J5J7 | MQGLVRAVRRFGCSNFQRRFASTLVIAEHDNSALNAITRSAVTAASKLGGDVDLLVAGNNCDKVVEEAAKISGVKRVLKASAPHLERRLAEELEALILHAQNSNKYTHIMGASSACTKSVLPRVAAKLDVNQISEVIAIESEDTFVRPIYAGNALATVKSSDAVKVMTTRATSFDKAEMNGSASVEEISSAAVGASEWKSEELSKSDRPELTAANVIVAGGRGLKSSENFQMLYKFADKLGAAVGASRAAVDAGYMPNDAQIGQTGKVVAPDLYFAIGISGFTGAIQHLAGMKDSKTIVAINKDPDAPIFQVSDIGLVDDLFNVVPTMTEEIKK | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Subcellular Location: Mitochondrion matrix
Sequence Length: 334
Sequence Mass (Da): 35360
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T1G7H1 | MCPAAVLDRESRRRSIADKVKSYPDFPKPGILFRDMFPLLRNPTDYRECINLFVEEIREKYPSTEVVVGIESRGFLFAPLMAQQLNVAFIPIRKAGKLPGQTISYSYALEYGNDTIEITRESIEAGQHVVVVDDLLATGGTLSASIELMNKAGASVECCMVLLELCDLKGRKKIKSPVYSMIPLN | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 20634
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E7FEB4 | MMGVRSVCCFLLISLLKSSSAHSDFFTSIGHMTDLLFTEKDLVTSLKDYIKAEESKLEQVKQWAEKLDALTATAVQDPEGFLGHPVNAFKLMKRLNTEWGEVEDLVLKDMSDGFISNLTIQRQYFPNDEDQNGAAKALLRLQDTYKLDTQTISSGDLPGVNTGLPYKSTLTVEDCFELGKIAYSDADYYHTELWMAQALKQLDEGEESSVEIATALDYLSYSVYQQGELERALEYTKRLLTVEPEHQRALGNLKYFDYQLAKQKKAEKEQSTKEESKKEQETSDGKKEYLPEKRKYEKLCRGEGLKMTPRRQKHLFCRYFNGNRHPFYTIGPVKQEDEWDRPRIIRYHEIITEQEIEKIKELSKPRLRRATISNPITGVLETAHYRISKSAWLAAYEHPVVDRINQRIEDITGLNVKTAEELQVANYGVGGQYEPHFDFGRKDEPDAFKELGTGNRIATWLFYMSDVAAGGATVFPEVGAAVKPLKGTAVFWYNLFPSGEGDYSTRHAACPVLVGNKWVSNKWIHERGQEFRRPCGLKETD | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 541
Sequence Mass (Da): 61877
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A0A0A7S3Q9 | MNNIAHNYWVIWVTIIIGLLLQIMPWSSSFYIFKPHWLMLILCYWFVALPHRVGITTAFLSGIIIDLFLGTMLGVHAFIFTVIAYLILFRFQLIRNLARWQQCFIIFGLSICYDLLLLLFQIAIYRTITLTPMIFLSSFVDGVLWIWIFSLLRQIRRRFAID | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 162
Sequence Mass (Da): 19227
Location Topology: Multi-pass membrane protein
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Q1Q1P7 | MRNVRLTIEYEGTNYAGWQWQKNAISVQETLTHAVRTVIREEVEIHGAGRTDAGVHALGQVANFKTYSAIPAKQLLRAINFHLPQDITIKDVADMEEGFHARYSATSKVYRYTVLNDWLRTSLNRNFCYVYGFPLDLSKMMTAAQYLIGTHDFTSFTTKALDNKDRIRTIKNLEIQKEGKYIYFVVEANGFLYKMVRTIVGTLLEIGRGKMDVYLIRKLLETGNRDDAGPTAPAKGLCMKEVKY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 244
Sequence Mass (Da): 27876
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A0A1B8RG03 | MTTYTITLQNCAFFARHGVHDEEEFLGQRFFVDAELDVVAGEALESDSINDTVNYGIAFTVIEQIVTGKRRYLIESLALDIAKGLCETFPQIRRAKITVRKPNAPVPGVLDFVQVSVEHFA | 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): 13534
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A0A944VL56 | MKKKIAIIGGSGFYDVENPAEVEELSIVTPWGPTSDSILKSETDDLEIYFLSRHGRGHLIGPSQVNYRANIYALKFLGVDWILSISAVGSLKEEIPPGMIVVPDQFIDFTKNRFNTFFDEGIVAHVSMAKPVSETLSLSIFEACKKLQLPVQKGGTYVCIEGPQFSSLAESNFYRSLGADIIGMTNMPEAKLAREAEICYSTLALSTDYDCWHKSHDSVTVDEVLKTIKKNVDNAKSIVKEVLNNIPKEKDVYIANALQASIISSIDSITDESKEKLSAIIRRYLLS | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
EC: 2.4.2.28
Catalytic Activity: phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Length: 287
Sequence Mass (Da): 31792
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A0A2C9CH83 | MNPLLMLKEYGQSVWLDYIQRGLITTGELRRFVEEYGLGGVTSNPAIFEKAITGSADYADMLDTLQQKKDMDAMAIYEYLAIRDIQDAADVLMPVYEKTGKRDGYVCLEVSPFLANETQGTIVEARRLWKAVGRQNVMVKVPATSEGIPAIEQLISEGINVNVTLLFSRETYEHVTQAYINGLEKLASRGGDVRTIASVASFFVSRIDTLLDSIIEARVKTSAHANEQALLQGIMGKVAIANARLTYQRYKEIFRGDRWQKLAEKGAQTQRVLWASTSTKNPKYRDVTYVEELIGPDTVNTMPLSTIEAFRDHGRPRASLEENIVAAYDTMKTLEQLDISMKECTDNLLREGLRLFADAFGKLLNALDTRGIKGA | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
EC: 2.2.1.2
Subcellular Location: Cytoplasm
Sequence Length: 375
Sequence Mass (Da): 41924
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A0A1S3BCE4 | MISVCSARTIQASPSSIHFFFPRNRRRIDSNVLRFSANFSSRCSDYDEYSEAQSERIANYAGTRLEETVDINPGKVRLDSWISSRINGISRARVQSSIRAGLVSVNGRVIDKVSHNVKAGDVINCTISELQPLRAEPEDIDLDIVYEDEHVLVVNKPAHMVVHPAPGNATGTLVNAILNHCSLPMVSTSTGEHQSDSDVSDDEFSSIEVFSRVSEAPIRPGIVHRLDKGTSGLLVVAKDEHSHAHLSAQFKQHSIERVYISLTCGVPPSTAGRIEIPICRDPNNRIRMTATHGTKNNPHAKHAASRYNVMEILAQGGSSLVEWRLETGRTHQIRAHAKYMGIPLLGDEVYGGTKSMAMSLLRTRASSNCHGQLMQLVSSLERPCLHALTLGFVHPHTGKNIRFSCPPPTDFAEILSQLREIGTKKLQVTKS | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 431
Sequence Mass (Da): 47474
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A0A6P4ZCP5 | MSTGFHLLAVVIIWSQRAQAADILVATNTFGSHWLNLAKIAEALTSRGHIVTVVAPASEKSDLTTKWPSFRYETFGDPEKAPLFIEVLKNTPPEIMFQVLTSITWLDSHMMMNEAATDDCQNMLSDIQLLRRLKNSHYNVVLTYPGMSCGSLVAQYLDLPLVCTLMFMPFVLVVFCCHVTEIQATGVPNPVSYIPTVMLGLTDQMTFLQRVKNTLVYFGLTIMGQVIAERGFDAIASRTIGSNFTIFSALARTDVWLYQTGVMFDYPKPTMPNMVSIAGYMADEAKPLSEDLDSFMQSSGDAGVVIVTFGNLITVMPAERAEMLAAAFSRLPQKVVWRNAGTPPPSLGPNTRIMEWLPQSDLLAHSKTKAFVSHCGYNSISEAMYHGVPLVGMPLFADQHENIARVVARGMAVTLDIHTVTSEEVYQAITAVIFNPKYKEKAKRVSTILRDQPQPPMERAVWWIEHVIKHGGLPHLRSRATELPFYQYYLLDVLALIVSVLAVILLAGWKCCLCACSRCKWGRNNIIKKTN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 531
Sequence Mass (Da): 59121
Location Topology: Single-pass membrane protein
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X1WFG3 | MAELNRQLQEYLAHSKSGAKTISQSSSSTTIDVDGDVPVSGSWFGRWSSPFSGSSSRGATSGQGSSGGFSWPWSSEPDPCLPGLSRSQRLVAFGTCIFFSALCFGLSALYAPLLLLKARKFALLWSLGSVFALLGAAILRGPSKLIATPTPGAAVYLCSLAGTLYAALSLHSTLLTALGACLQIAAIVGYIVALLPGGSAGMRFVGGMAASAIKRTVTGKTMPI | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 23043
Location Topology: Multi-pass membrane protein
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A0A2C9CHJ6 | MLLGVHCSIKGSLHNAFNEAASLGIDTFQIFTKNQRQWKEKIVGPAEKTIFRETLRQSNIKTIFSHASYLINLATSDSRIHALTHNSLLGEIQRCDDLGIASIIIHPGFTKNTGKQTGMKNVIKMIKSVLKKTNNSPVKILMENTAGQGSSIGYHFKQLQQLIEGIGSGRIGVCFDTCHAFAAGYDIRTKIGFETTMEELDATVGLNSLYAIHLNDSKGALGSKIDRHEHIGQGAIGLEPFRQIMNTMKHIPKILETPKEGGMDVKNLNILKGLVENR | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Length: 278
Sequence Mass (Da): 30636
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D3XDB4 | MQGCMSLVFLWTSLLLSLPSGYNADKILVFPIDGSHWVNMEVLVKKLQSRGHELSVIRLEDSWFIKGNSPYYSSITVTLKKKFIDLDLFETAVKKILDARRDGPIMGVLAQMSEFIGILKVGHGANIAMLTSMLENKVLMSQIKMANYDLMLTDPAMPGGVILAHYLHLPMVYNVRWMSFGEGHFSIAPSPISFVPVPGSGLTDRMGLLERSRNFLHYGLNLIQERWMVIPMYTSLLLNHFPPGTDLLTMQRSAELWLVRADFVFEFPRPSMPNLVYIGGFQCRPAKPLPADLEEFMQSSGDHGVVVMSLGTLIAGLPKEVMEAIASAFAQIPQKVIWRFIGQRPSTLGNNTLLIQWLPQNDLLGHPKTRAFVAHGGTNGLYEAIYHGVPVLGLPLLFDQLDNIVRLQARGGARMLDAATCSTKEFLVALTDILENPTYRQNMQKLSNLHRDRPLHPLDKAVYWIEFVLRNKGAPHLRAEAYNVSEFSYYCLDVVALVLFMLLGTLGGVYTICKRRPKRQENKTGGDWNKKGLK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 59988
Location Topology: Single-pass membrane protein
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A0A084J7S2 | MNIDWSIIVPSTINFFIFYLILRKFVFNKTLAVINTRKEEVESAFKKARDEEERAKLLKQKYDEDVKRYRNDGLKLVESYKQKADKVYAEIVEDSQREVANIKERATKEIKREREKASKEIKQEIIDLSMKLAEKTLEKEINEESHRELIDKFIAKVGI | 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: 159
Sequence Mass (Da): 18916
Location Topology: Single-pass membrane protein
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L1INC3 | MEAENLLPSESESARRVRTLAKLNEMCRDFVKRVYEKNNLMEQYSEENPPYQLRTFGSYRLDVHLPGADMDTVMIVTRHIHRDDMFNDLYVAMQARKDITNLIKVQEARVPVIKFQMDEFEFDLAMARLSYATIPEDFDVTDDKHLKNVDQQSVTSLNGVRVTDTIRSLVPTMKTLKYCIRALKLWAKKRGVYKNVLGFLGGISLEIMAARIGQLYPKALPSRLLYFFFFTYSQWKWPQPVGLTEVIANSHDLNLPVWGFGATEMSDRRHLMPIITPCYPAQNATANVSKSTLKVMQEEFTRAKDICKQILEGNAEWSDLFEPLDPFSKASVKPTFVP | Cofactor: Binds 2 magnesium ions. Also active with manganese.
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 338
Sequence Mass (Da): 38951
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H1XR43 | MQSAFQLHIDDQNIALLYFDLPDEKVNLFNERVFDELDEILDRLEKAQPAALLILSKKEGIYIAGADVNAFQKIDTLEMGWQAARRGQLVFHRLSKLPFATIAVIHGACMGGGTEMSLACDYRLATDHPKTRIGLPEVRLGILPGWGGTQRLPAVTGLSAALSVILTGKAVSAKKARAIGLVERLLDPHKAVEEQALSFAREAIQKGSKIKKRKIFRVERIGFIRRLIFSQARKRVLKQTQGFYPAPLKAIEVIEKTWNMPIEQGLEVEARALAELIITPQSKNLVRLFIWSEELKKEARNMLSGYQAGQTQRIFFFNVDSTFSALFPVLLRKGMKVAVIDFDKERLSAVRQSFLRQLKRQRQKKKITAVEFDRLLQDISFLDTLPAIEQSDLLFTGPCNESLWRQIQQKAPETVRPIPVAPPFISKSSNCAAALNFCTWQKNPFAAEVILSDNEAQESFRPLLDLLLRINRLPVMTRDYSIGLATRLFLTLVGEAARMFNEEYAEKQIDEALTRFGWTQGPFEMARKMGLKNLRLWLQQVDPQKDDTLRLDVKAVLEWSGNTRFRRGAVKATEADAQNIQNRVHLLLINRAAFLLEKGLAQRARDVDFLMVGALGFPPFAGGILKYGDHIGINAVINQLKQLSQRLGERFETSALLKQMSRERQLFYP | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 4.2.1.17
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 669
Sequence Mass (Da): 75782
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A0A235BQH3 | MRVGLVVNPNKPSSKILVPKITSWLKEKGVTVLDEPDVSSADIVLALGGDGTFLRVARLVDPYDIPILGVNLGGLGFLTDIKEEDVFTALELVLKNDYRLEERITLSLNIMDKSLFALNDVVVSTVKVGRMIDLQLSVDGKHLSEISCDGLIIATPTGSTAYSLSAGGPIVFPHLNVILVTPICAHTLSMRPLILSSKSTLTVTSISGKSMACCDGQVKLPVDTGVPVTVKTGEHTIKLIKFDMSYFEILRRKLGWNKRANQ | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 262
Sequence Mass (Da): 28371
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L1J976 | MKDDGHLALGLFFGTITFYHLSEFVLACTYNPSTVSIDSFLANQGSYMGAMLFGMSEYFIGHTFFPASKGWRACRFIGLAGVLFGEFFRKGALIQAGSNFTHKISDGEKRSSHTLVTTGLYSISRHPGYFGWFYWSISTQVLLCNPISTILYSIASWKFFQDRIPYEEYHLCRFFQDYPAYRDRVPTRIPFIP | 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: 193
Sequence Mass (Da): 22113
Location Topology: Multi-pass membrane protein
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A0A183IKL3 | MKVIANGFLLHSGAYLRNGWNILDFLIYCTFNSQYSWVRRESFASFSCAATASTGLQVVLNSILRAMVPLFHIALLVLFVIIIYAIIGLELFCGKLHKTCVNANSGEIVGEPGPCGESRTSYHCDHGHDIICTDNHTWPGPNNGITNFDNFGLAMLTVFQCISLEGWTDVMYWVNDAVGCEWPWIYFITLVILGSFFVLNLVLGVLSGEFSKEREKARARGLFQKFREKQQLEDDLKGYLDWITQAEDIEPVNEEEETESTTREGANAAFRKLALFTLLSLLEPVEGEATDEGSKEEFRTQSWWLKRIRRIKKLNRRCRRFCRKLVKSQAFYWLVIVLVFLNTMVLTSEHYGQPDWLDKFQEIANLFFVILFTLEMFLKIYSLGFVNYFVALFNRFDCFVVISSILEFALTFAGLMKPLGVSVLRSARLLRIFKVTKYWNSLRNLVASLLNSLRSIASLLLLLFLFIVIFALLGMQLFGGKFNTIDVTMVKPRANFDSFVQSLLTVFQSAGIIVCIYFIVLFICGNYILLNVFLAIAVDNLADAESLTAAEKDDENKPEDSNLQEVIYADGNDTNQADQYSGYIEHAECQLTARPHRISEINIPKKVKAIPNASSLFIFSATNPLRVYCNRFINHSYFTNAVLICILVSSAMLAAEDPLQASSFRNEVLNYFDYFFTTVFTIEISLKVLVYGLVLHKGSFCRNAFNLLDMLVVGVSLTSFGLKSGAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVIVAVKTIGNIMLVTFMLQFMFAIIGVQLFKGTFFRCNDPSKMTMKECRGSYINYEGGDINNPQVRNREWQNNDFNFDNVQHAMVALFVVSTFEGWPDLLYVAVDSREEDYGPEYNARITVAVFFIAFIVVIAFFMMNIFVGFVIVTFQNEGEREKCIEFALTAKPQRRYIPKNRFQYRIWWFVTSQPFEYGIFVIIMLNTLILGMKVSASD | Function: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death.
Subcellular Location: Membrane
Sequence Length: 969
Sequence Mass (Da): 110519
Location Topology: Multi-pass membrane protein
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B9UVE2 | LYLIFGAWAGMVGTALSLLIRAELGQPGSLLGDDQIYNVVVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLSGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL | 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: Mitochondrion inner membrane
Sequence Length: 231
Sequence Mass (Da): 24842
Location Topology: Multi-pass membrane protein
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L1JW27 | MVLQPSSSEALRLFTCFGLFLLSNSFQAVNIAVRDVNSDKSSTKLYSSQQDTRRICNVFDFRRLVPYQEGLQLQQNLQQDSIKALVGGHQTSDALILLEHPTVYTLGSSSVLSDILFELPDIDITNVGAKVVVEDYPEMPPFSIFRVQRGGKVTYHCPGQLVVYPILDLNYHGKDIERYLRNLEQLIINTLARFGVRGAREEGLTGVWISGKKVAAIGIGASRWITMHGIALNINALMKGFEMIVPCGIKDRDVTSLHQILGDSCPSVEEVKLCLKDEFAKIFELQLCDVEFPNKSSY | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 298
Sequence Mass (Da): 33289
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L1J5W2 | MGKKQHSKDKMYILHSEWQTEGGGYKSKGGLAAKAPHRCLPFFCCSLSLQPFEDPMMTPQGVVYDMLNIIPYVQKNKRCPVTGQPLSVKELTKLTFHKNEKDEYHCPIMFKTFTAHTHIVAIKTSGHVYCHEAIDTLCLKTKNMRDLITDEPFTKKDIITLQDPHNFSNREINKFQHIQSGEDTKARKVAEMKVDEETRRILDKAGLSAPGATGAQRPSQASLLAAEAKAKRAREEAMEAERNDPLKLTSDCASKRKKGISSGAMAASFTSSAIDVHYKVEEQAMSEKEIKQERWRIMRQIGKKGYVQLKTTHGDLNLEIRCDWVPSTSENFLTLCARGYYNGTKFHRLIPDFMIQGGDPTGTGRGGESCWGEKFEDEIDSRLSHNARGILSMANAGPNTNGSQFFITFKACPHLDKKHSIFGSVVGGIDTLRKLERIETDAKDCPTEDIIVKEVVVFVNPFETDLKAYFEEKKSNEIKEARGHFTQWYSNPSAAAASKVTLYKEGVGKYIAPKKEEEGKKEAAEQQDNGDDMWVNVPLSKQKNKAAPRAGFGDFSR | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 557
Sequence Mass (Da): 62504
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L1JAA8 | MGIDEAGRGPVIGPMVYGACIICSKRNNELKEMGFADSKTLTEEKREVLFERIKESNVLGWLVEVLSAKQLSGSMLQRAPYNLNAISHDTAIGMIRKVLAANFNLKKVFVDTVGDPERYESKLSSLFPSIEFAVRKKADSLFPVVSAASICAKVTRDRCVRDWQFKETGVSFSTDYGSGYPSEPQVFGYPDLVRFSWSTTKKIIETQGESFEWEADEMEEDQSQSKINGFFTTQAGWLQMF | 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.
Sequence Length: 241
Sequence Mass (Da): 27079
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Q7ZUL4 | MADLEMDLQSKRLNNGPENLESPQKSGNEDENGDISGEDEEEGEEEVEMNGEKQDISSKHHSSKHKKKKHKHRSKHKKHKHASEEDKNRKRKHRRKHKKHKRKEEASSSAISRKAEDGSMLLSSANLDDKALLEDLEKQRALIKAELDSQMMGGKVQSGMGLILQGYNSGSEEDEERQRARNGEQRQNSSGGRTRSPRDQIGGMGRSRRDLDTSKPSAKQQSHSHSRERAGRDSKLERATKSAKETVKERSKSKEKKRSRSRDKSKDRGKKSQSPSIRRHSADRKPDQKGRPDRRSSPHMDEKREQVRQRSDSQGGKSQSQGSKDGQNVGRSENDREKRPGKSPSKDPSSGKENRSPQQRPALSPQHRRSSSPRHRDRQSNQPRFSSVDRSSKLSHSPSRNRSLARRARSRSNERRRDSPSRKRLRVDGVGRSRETTPVRRRVSRSPLRRRSVSPRRQSRSSPRRRSRSPQRRRSVERDRFGRPRPRRSTSRNRDRRRRRSRDEDKFKGSLSEGMKADQESSSEEVMEDFDAEEEDEEALIEQRRQQRLAIVQKYKAGNEDSNLGSMASEPSSPQSSSRSRSPSPDDILERVAADVKEYERENVNSFEANIKAKHNLIAQEKEGNNPKKPSAPDMFTESDDMFAADFDGARLRAAGIGKDFKENPNLRDNWTDAEGYYRVNIGEILDKRYDVYGYTGQGVFSNVVRARDTARAGQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESKTILKLCDFGSASHVADNEITPYLVSRFYRAPEIVIGKPYDYGIDMWSVGCTLYELYTGKILFPGSSNNHMLKLAMDVKGKMPNKMIRKGLFKDQHFDQNLNFLYIEVDKVTEREKVTVMSTINPTKDLLADMVGGQRLPEDQRKKVMQLKDLLDGTLMLDPAKRISINQALQHPFIQEKI | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 1010
Sequence Mass (Da): 116053
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A0A183ICD5 | MSNASLNEELVSSFSNTPQRWFHLKKFLERPGPFAHPEFIPSPQNIDFIHQCKILVVGAGGLGCELLKNLGLMGFQDIHVIDMDTIDISNLNRQFLFRHFCRIQDMTADFYQSFSIVISGLDSVSARRWINGMLVGLLHYDENGELDTSSVIPLIDGGTEGFKGNVRVILPGVTPCIECTLSLYPPQVNYPMCTIAHTPRSPEHCVEYVRMILWGKLSPFGTACSLEAFKIASSSALPLNNYMNFQDSDGVYTGVVELQRKVLNFQEDCLVCSQKPQKITFPEDAKLEDIVSFLINSAEYQMKSPSLTALTPKFTTLYMPTVPSLEQQTKMNLEKSLKGTYFLLMSFKII | Pathway: Protein modification; protein neddylation.
Function: Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
EC: 6.2.1.64
Catalytic Activity: ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.
Sequence Length: 350
Sequence Mass (Da): 39333
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A0A183IW02 | MSGLHGRVKETVNVETAEVERKQKEEKLRRYLQARNVLFEKIRNNVFDEDDGEWQKVPRHVFDAEMSLTEVGLAKNPKSYSAWHHRVWMITVAGVKDDCETELRHCEKALEMDDRNFHCWDYRRFICRFGQRSAAEELAFIDKKVSENFSNYSAWHSRSALLPVVHPPLKTTEDEDGLSNGEETKNLPVDVATFEQELNFVQNAFFTDPEDQSSWFYHNWLFAVSEPRPLNLLQAVFDPATAGICLVFDQAISAETSIVVVSVRRDSNKECLHLHLPWRTSDGTRSCRLLCAPLPDVSLGDLPCLQVEYRQKPSSGKDNRGQTITRKLENWTKHRVLVWTDLTAYRNYMFSSMFASGLKRALEEDLYGCKKLIELEPDNHWAYLTAVNAMIALDPLQFSNDIVGYLNKLVTLDPSRKKMYLHFLSRYLIKFQLVHSLSGGTPDKRLDLSDRDLHSLCDGVWFVHLTVLVVNRNRLCSLQPLKYALHLEELYANDNRLTSLVGLEDLQKLRNVSVANNRLRKPADLRPLVNIRALHVLVVSGNVICEHYNRQDIVKFLPSSDSLIIEL | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 567
Sequence Mass (Da): 65372
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L1JXR6 | MEQPKKRITAMCTAYGVDGAVRGGMIGLMWGLFQGTYYGWQDQLRGRLLGMHVARNLAANTVGFAAFLGIYQIAHCSMENSRKRSDWKNAAAAGLVTGGVMGLPLAVRTGEPRWALFAAGFTAALTGSLDLARPR | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Subcellular Location: Membrane
Sequence Length: 135
Sequence Mass (Da): 14508
Location Topology: Multi-pass membrane protein
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A0A822CRH4 | MEALARQHLYKPIEVTVGGRSIVCQDVVQNVLIFDDDDQKYAKLLELLGLYQPYGSVLVFVESQIRCDELIKKLMSHSYSCMPLHGGLDQYNRDSTITFFKNGDIPLIIATSVAARGLDVKNLILVVNYDCPNHYEEYVHRCGRTGRAGNVGYAYTFITSAQGKFVGAIIKALETSGASVPAELTLLWDNYVKQMEAQGKKVQDIRGSFGGRHGYNFDSSDKQHKNIQKRMQGILIGLEDVDDDDEEIDQQIESIYKSNRSISTKDEVPVTQNETSSPLETAKRITARLSAIQYENPGVPHDVTLSLAAARQRAQELNAKLNYEKPPDKTELNESTPTTYEEELEINDFPTNVRSRIVSTAILNHVRDYADVDIYVRGEYYPKNKKLLSGEKKLHLQIRSLNEYGLQIAKAEITRLIKEEMIKMQNTSLQSANRGRYKVV | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 440
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): 49722
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T1G0T9 | VGHMNVSLEDLMNSTIEKLFENLTSKIELGGSWRPKNCISRHKLAIIIPFRDRENHLNVLLSLLHNMLPRQLLDYRIYVVEQIGNDTFNKAQLMNAGFLEASKQNDFHCYIFHDVDLLPKDDRNLYTCSNQPKHLSVAIDEMKYKLNYLYLVGGVLNIRKEHFLALNGYSNLYWGWGAEDDDMACRMFFSGLRITRPPITIARYKTIKHIKRKPSGLYKR | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 220
Sequence Mass (Da): 25705
Location Topology: Single-pass type II membrane protein
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T1G5Y3 | LVLFFFQAVFNYMIPDHKADVFNPPHTTNISNTFVSVLFDGLTNRWDAIYFIHIAEHSYTFENTLVFFPLFPLIVKLLTFSLFYPFTFFLSIRNVLQIVAVLINFILFILSALTLYKFGLAVLKNEHLSYRAAQLFCVNPASIFFSAAYSESLFSLLTFAGLLKLQSNKVLHASILFGLSAATRSNGLVNMGFIVYYFLHFHLKAILKFDLSFCHNLLLFFIYIFLCCSWFIFYQLFAYIIYCEVNKSHFKNLITNELRNYGKEKGYFTLGDSPSPPWCKLTVPISYSSIQNSHWNLGFLKYYQVKQLPNFFLASPMLFICFYLVLTYFKNRFYRSVFLEMMPRCLIKKLTNDYELKSKYSLHDVTKKEILVHVCHIFFLTIFALFFMHIQVITRLICSSCPVVYWFLAQKSITQEEKIAIAMWKENINDDQFKNSSVFDVCGKDICKSTVENNHSRYRSTTTIIKKVKVNKQKLNSLHERTKVITDTLTESELINWNESLFNKFFSAYTHIYLFVGVAAFCNFFPWT | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 528
Sequence Mass (Da): 61877
Location Topology: Multi-pass membrane protein
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A0A834Y9K3 | MELARPGDQILGGNHQLYNVLITAHAPLMIFFMVMPAMIGGSGNWSVPILIGAPDMAFPRSNNISFWLLPPSLLLLLSPALVEVGSGTGWTVYPPLSGITSHSGGAVDSAISSPHLSGVSSILGSINFITTISNMRGPGMTMHRSPLFVWSVPVTAFPLLLSLPVLAGAITMLLTDRNFNTTFSDPAGGGDPILYQHLFRFFGHPEVYIPILPGSGIISHIVSTFSGKPVFGYLGMVYAMISTGVPGSLVRAHHMFTVGSDVDTRAYFTAATMIIAVPTELTDRKEGDLLSLLYSRNRLSTRPGKEKRFKYPATLSFSEAVKMVGFDHWTRRK | 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: Mitochondrion inner membrane
Sequence Length: 333
Sequence Mass (Da): 35979
Location Topology: Multi-pass membrane protein
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A0A813X2X2 | MDLLHLVNNFSGVLSFANVRAKADDFVIDRLSYKFTSAILCVFALFCGVKSSYTVPIICWTPAQLKRYEKAITAYCFANNTYYVPDDQRVPSTTNERYEGLIIYYQWLPWIFALQAVLFYLPKLIWRLAVSGSQHDIRSLLDNASELYFIPNFGKKKSLTKFRNDKLDYLDSRLFVREDGDIVTDRLHHHSRTFSCYLIICYIGVKLLYLLNCLFQISLIHFMIGTRPFGINRFQHLKEDTFETHFIGQFINKISSGVSELIDTSAFPKRTLCDFTFRELASNHAYTVECILPLNIIVEKMYVFLYIWFIFLAFIIFIDLMKWIGHLIHYLVSSDKTREHYVRTHLIHRRKDTPIDITSFAKEHLTGNNYFILKLLSKNISSFVVVDLLDYHFNPKPNNKKDE | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 47305
Location Topology: Multi-pass membrane protein
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Q1Q760 | MSNFIEPITLWPLLLYTVAVVSLVIGILIISYFLGERHKEPSTDVPFESGITPTGSARIRFSAHFYIAAMFFVIFDLEAIFIFAWAVAFRDVGWNGYIGVLIFIGIIIAVLIYVWRLGALDFGPQGKKILSAFEKLKG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen 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: 138
Sequence Mass (Da): 15449
Location Topology: Multi-pass membrane protein
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A0A183ISU3 | MCIRHKLSRILRSTVARHETTQQASVKSTTENVPMAEVRFDDPKEIYRSKTTAELIRSALILKLCSIELLTRNSERLMNIGRLLLGKSLFKILMKNTIYGQFIAAENFKQLKPEVEKLERNGIRSILDYCIEKDINQRQAKGITEASLEQSLKIILESIDMATAVKGNLQMVAVKVTSITEPLFLAKLNDVIEASQQFLEELYHDSWDNIVQIKTSVEELMTKVKMVRRNAERINSQWIEYVKESADTANKRTDFSKERHFDQTLSWEQFSGAFMPPEKQKAPAWTRNDYQQYKALVGRLSKIADYAATKRVPVMIDAEQTYFQAAIDYLSYSLMRIYNREMPLIIPTYQAYLKNAMKRVKTGLNLSRIWNYYFAAKLVRGAYMDTERARAKELNYEDPINESYEATNQMYNSIINVLFQESKQSSDGKVWFMCATHNEESIRKLLTLLSDPTAKDVKKRLAFGQLYGMFDHLSFPLAQAGYTVYKYVPFGPLELTLPYLVRRAQENSSTFHDCKHQIGMMRQEIARRRSRKK | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 533
Sequence Mass (Da): 61887
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T1G567 | MFKKKKKQRKKKNKSNDKTEPSKSCYGAQQLLHQHSNGQLQQKQPDDVSSKIDGMENWLDLRIPNPILRCLKELGFTNPTPIQSRVLPSAIEDKMDIIGAAETGSGKTLAFAIPIVTHILNLNADDDDDDDDDDVDTINNNNDTDVDEESQRDTLDVDDINDEEDDDDDEVLGKMHNDDKNDHHHPHHYHHHHHNKPMYALVITPTRELAIQIREHIDNVTKYTDVKCLAIVGGMSIERQNRLLKKFSPQIVVATPGRFWELVQQKCPHLSHVKDLRFLVIDEADRMIEKNHFEELEKIMNYINLNLCSPLRRQNFVFSATLTFIHKTPYRFDVGKKKKMKELTLEDKLASLQRKLHMSSKPEVVDLTGGQKMTAQKLTELKVNCTYQEKDLYLYYFLKNNKGRTLVFANSKDCIRRLTSLLAMLHCKPLPLHADMHQKQRLKNLDRFKENERGLLLATDVAARGLDIPNVKHVIHYQVPRTTENYVHRSGRTARSNTAGISLALVCPEEVKLFNGIQAALKRGIIKFFNEIMCKWMNGLVNE | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 543
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): 62569
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A0A183IHH3 | MGIXXXXXXXXXXXXXXXXXXXXXXXSVNCRTSRKFTEILKMHEVHRIALSRRFRARLCSTAALLHVVLFLLTLLLSLLFAFRTHESRFETVQVTEQPTVLYQQQFLIVLTSATSGRYWLWSSSLATNQRERDHLKPSLIRFCVKDYNNDGRPDSFRLIAVFPLAEGEVVYGINALFAFDYSIAERSAVELQAIAHVQHESSHPGLEYRVTGEMKAVQKTPVKLRSPGDTYGQVIDFGKQGISYERLLDLLSRSNNRNLSITFVPHFSKWSEKPANTTADFTLHIKINYLEDTFLHHSCFYEVLKWGWIQFYAVFVILFYIYSCCQSFVFENRLVAVEEETIIVRL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 346
Sequence Mass (Da): 39969
Location Topology: Multi-pass membrane protein
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T1FFK7 | MENLSTSDEYPKHDPDLMRLYSMRFCPYAERIRLMLQFTKIKYEIININIFDKPKWFIANVNPDGTIPVLQYKNAILTQSSICNEYLNEEFGENKFLSKKPLSRAQQRALIASFDKVSTPFSEINKTSDRSVHKANLPKLLDGLGFYEKELKGPFFGNQKYPSLIDIAIWPWFERFPAISKLNHLDIMSEREFPKLSCWVKNMKKLKSVQRVSLPVDYHVKFYEKKQIGFTDIVDIGL | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid
Sequence Length: 238
Sequence Mass (Da): 27901
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M5C7A2 | MGLAVVGTPLNWEETQKCADYIREHGITQFLNIWRKQQNRKDYPFLWGDEIECMVISYDDEGRDARLSLRQSELLPKIQACERRLRQLSPDNADSVPEFQPECNRYMLESAPGSPYNGSIESLLSVEKDMRNRRKLAKAYLLPRESLITLTSFPRLGVREPFTHHPENDPAHSKTSESLFLSGDITSPNARFPSLVANMKSRRGAKVAANIPLYFDTNTPRPFVDPSIPWETGVSPEDRGAIKHDHIYLDTTSFGAGCCCLQVTMQARDVNEARVVYDSLVPITPIMMALTASSPAYRGYLADVDCRWDILEASCDDRTEEEKGLKPLKDGQQRIPKSRWSSVDMYLSENAENRPEYNDIPVPIHEAVYSRLRDNSVDNLLAKHLAHLFVRDPLLALPETLEQDDEVSTEHFESFQSTNWQSLRLKPPSQNGDCGWRIEFRTMEVQPTDFENAAMSLFVVLLSRAILNFGLNFYLPISKVDENMKRAQRRDAARGERFWFRKHVGSIARELPGGTSNGHSPVASDAPLGSVEQEYEEMTMNEIINGKGAYPGLLGIVDAYIASLDVDATQKLKLKNYLELIQRRADGSLQTPATWIRNFIHSHPAYKHDSVVSREANYDLMKAIDHIEQGDRHAPELLPSGYVGSKYDDPNQQLGFSQNE | 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: 660
Sequence Mass (Da): 74839
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A0A183IH89 | MTGKLLHYRNCCFHRVVKNFMIQGGDFTAGNGTGGESIYGGTFADENLELRHDSPFLLSMANRGKDTNCSQFFITTRPTPHLDGVHVVFGKVISGYQINCGELMLVKKSRRRSSGSCSTDEVKITGDRPSKEGAAEAEAKEAESAMTTTPAVEIPDIPPNRFLFRRSKTPEDIKKKENDKEKDKRKEERRDVRERPRTFSRRVLYSKSGHRIRGRGKLR | 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: 219
Sequence Mass (Da): 24768
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A0A815IF77 | MRRFPNAHFLVVSDDKSYCKNLFRHRSNIVVTSRTFSIGDDLITLSLCEHSIITGGTFRWWTGYLANDEVIHDKIYPSGCERREYYYPLWFLIDGNVRAYKNGNYTRDVHRG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 112
Sequence Mass (Da): 13228
Location Topology: Single-pass type II membrane protein
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A0A7C4JBV1 | MKDSSIPKKVILASKSDPAAQNIKRHLLRLGNFIEIEKGVYTSQKALLIETSPQSVSLPSGTDEVIVASRHASQSGRPSLTVHVPGLPEKSLLPPASPSTVRAALLELRNQVARLNLPHQVSLEATHHEPGDFAVPITFVEIGSEEKEWVNENAGEAVARAILSALDPHPCKFAIGVGGPHYSPLYTRISFESNIGFGHILSKHAPANVELIRLALEKSSSRMIVLDWKGATREQREICLEISENFGIEVVKAGSLLVKKL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
EC: 3.1.1.96
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Length: 261
Sequence Mass (Da): 28345
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A0A0B7BRW4 | YALIGTIHDVIQSKVPFSLGATPFPLDRTTDRMTFFERLKYTIIYIARINFDLFHDSSLVSRFAPHKPYKSINDIAANAEVFIAEVDHILDYPRSVFPNTKLIGGSSASPAKPLVGEFKKFVDESKNGIIVFTFGGSIINVPTQITSKLLSAFQQLDLGVVWKVNITSPDPSRIMTSKWIPQNDLMGHEKAKLFISHCGKNGQYEALYHAVPILCLPIFGDQGYNSERVVIKELGLRADMREASADELASMVKEIVYDGKYTRNMKKASDLYRKLYKVPKKEAAFWLDHVMEYGGAYMRSTAQQMPWYQIFVLDVLAFLFAIVIFIFLSLYFLIKKCYQCFRGASVKPVKSVKQKSKKQ | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 359
Sequence Mass (Da): 40777
Location Topology: Single-pass membrane protein
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A0A815BX94 | MDDYSKRCGITSLMGPKRFRPPALTIEDLPNDLDAILISHNHFDHLDYLSVKRLNDRYGERLTWFCGRGTRQWFLVHGVKNVVELDWWEEYHFSKKAVNIAFCPAQHWSRRTAFDMNKALWGGYAVWDHTHKFYVAGDTGYTHNISIFRQIGKKYGPFDLSAIPIGAYEPRWMMEAQHVSPDEAVQIHIDVQSKKSIGIHWGTWALANEYFMEPPEKLSQAVENNQLDPSSFIVVKHGEIFDLS | Cofactor: Binds 2 zinc divalent cations per subunit.
EC: 3.1.4.54
Catalytic Activity: H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine
Sequence Length: 244
Sequence Mass (Da): 28328
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T1EG16 | MAEGGVDKKDSEEELHKEVVELDSKEVVKESACNNNFLQSIAAKFMGLFKSKPEDRSLVSVDLDGVVEFIRSGRCKNIISMAGAGLSTSAGIPDFRSPGSGLYDNLDEYDLPYPAAIFDLSYFKKNPEPFFVLAKNLLPTELIPTPCHHFLKLLHDKGLLMRHYTQNIDTLERLAGLPNEVLVEAHGTFNSGHCLKCRSKYDFDWMKNKIMSDTVPKCMKSGCKGVVKPDVVLFGENLPMKFFSLLIQDFSKCDLLIVLGTSLNVQPFASLVHKVPKKSPRLYVNLQKTSGSSFASWLIGGGSGFKFDDPDNERDVFWKGTCDDWCQLMAKKLNWECELNELITNQTTKIIK | Cofactor: Binds 1 zinc ion per subunit.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Length: 352
Sequence Mass (Da): 39451
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A0A4Q9P1B9 | MATIICRVCLEALQDKTVVSTQCGHLFCSECAGSVFSYIPTPCPICRKPQSSHSLIRLFPEWETPSETVTNTVLGQPAARNVSSPLETPHVVSRLDSDSSTSSTAFQPMSTASRPRRRGLMEDVSGTVDPEAPISTAFRPRRGVPIQLPTARRSVSHTTRSPPSPSDLRRTARGLNAVYVARGPQVTPPVAVVAVQRAPPVTLRSRSMAIAFALDLDISLSRTPRAR | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 227
Sequence Mass (Da): 24556
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A0A385I858 | WFFGHPEVYILILPGFGLVSHAVMVSSGKPSPFGVPGMFLAITSIGVLGCVVWAHHMFSVGLDMDTRLYFTAATMIIAVPTGIKVFSWLVSFSGSKMLMAPLQLWILGFLFLFTVGGLTGIVLANGTLDLLYHDTYYVVAHFHYV | 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: 145
Sequence Mass (Da): 15876
Location Topology: Multi-pass membrane protein
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A0A183IDP4 | MHGGGFGQFAAVPLNLMSLSKGTAQPSADYFISGSWSKLAAKEASKFLTVTEPIDPPLLQYNEFPEESEWKLNPAAAYAFYCANETIDGLSRDDGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMVCDMSSNMATKRIDVSKYGVIFSCTQKTLGIAGLSVVIVRRDLLGHSSARCPSILDYTLQSKANSCFNTPPVFAIYVTRHMLKWMKESGGIVEMQRQTIAKSNMIYEVIDSSHGFYKNRVALRNRSRTTIPFHLLDESMDERFLAQAAERGLHGLRGHRYVNKY | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
EC: 2.6.1.52
Catalytic Activity: 2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
Sequence Length: 289
Sequence Mass (Da): 32243
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A0A8H6C4D6 | MTSQEIYFYRFLVSKQVFYKSRYTYALVNLKPLVPGHVLVVPLRTNVLRFGDLSPEESVDYMHTLQLIHKFIQKVYKADSLNLAIQDGPESGQSVPHLHTHIIPRHKGDGYGDSIHTMLESDEERVARSESVMSEEAVWLAQNKNDRTPRTSIYDVLSSRLLASVLSIKNSTDLLNDMTSYHISDGGHSYINSIHGSSSKPSQSSAVSKPSSTNTGTNATTTPITLTTPSGATVPSTVSNGISTSTEIASGVFDTLLNDVVMNDDHLYIDEIPLYGEGSTLERLGLKGNKDAGLSL | Function: Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all dinucleoside polyphosphates, provided the phosphate chain contains at least 3 phosphates and that 1 of the 2 bases composing the nucleotide is a purine. Is most effective on dinucleoside triphosphates. Negatively regulates intracellular dinucleoside polyphosphate levels, which elevate following heat shock.
EC: 3.6.1.29
Catalytic Activity: H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+)
Sequence Length: 296
Sequence Mass (Da): 32447
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A0A1B3NJN6 | MPIVRFINLLSLWSGRVGAVVVVPLVLAMVFEVVSRYAFAAPTQWAFELSYMMMGTIFLLGLSYAVLTDQHVNVDFIHQLLPRRAVATIDAVGYLIMAGMLAWLTNALVGNVASVYRTGEGTGLSAWNPPIWPYRVIYVIGFALFSLQCFAKAIENLLVVFGRATESPAR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 170
Sequence Mass (Da): 18745
Location Topology: Multi-pass membrane protein
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T1FV65 | MWRVPTNLPKCLARTHVAVAVKRNIRTSKVLQSQDVNSAGGGGGGILKKLIALTFAGAGGVVGYSWYDPEFKKLVEENVPYAKECYDAVFQYLPESASTIEDAVKRLPIKTTEITTVPPPVQAPIQEDSKPEVKAEEKVKTKKEREKEKKEEAEKLLKLREENEINQNKALEALLMRTFTESASVMEAAMKSAHSAAEAVKEHTVKLKEALQKVDAKEGEWEAVTRAHDAKVKAMQHFEEVNEKAKQELAKLREVISTGKSNKVTKKNKLLWSTEDEANKLNRSFNTALNEVSKAEADSKVFKEYRDLIKKGKEQFKKELESIMPDVKKATTSVAKLTEDELNALIAHAHKRIDQLQRQLAEQQALEQLRINEALSRQREEDAAILLVSINKEKELWDNEINLIKAKWDIDARVNFEEELKLQLTRQAAAHSDHISEVLRAQQRELEAKFSLMLSEHVENERREFQRQVAGWVARLHGIEDAIDKRASLEKQGHQVQKLWLACESLQTVLNTGKLGATSWEGRLKPLAADVELIRSASTGQPAVEIILDSIPEVALNRGVWTEAALIERFKRVCKISKRVAMIDETTGVSGSLFKYGLSYLQSMFVVTGVGRIYDSSDLEIDPDEIKDTFVLLDNAQACLDRGDFAQAVRFVNHLSGEAKTAASDWLAEARLLLETKQAAVALLATASAAGFTSIAGCT | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 699
Sequence Mass (Da): 78097
Location Topology: Single-pass membrane protein
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A0A183PD56 | MISAIKHHNKNIVSHEEGPNIPSDQSIVNSIYDLVNNLGSLAARLLFLPLEESCHFMFSQCIQRDVSPNKQDKKLLMDAFRMLKTALRISSLIAWIGVTYAQANSRLLLMIYAGHRLADNYVAVNLLQLYSAYVLLLAWNGSTEALLNSAMSTVEKVFHVYYINKFLAKIDEPTNIEKQNNLDDDDNDSSCSSSGKSSTFVVLSNCEMEKFSNISLLSLMFPSYSEMCILSISLVCTLISQYFFCCSFGILWMILHGTITFGFLFITLIIIYYEEVDILQLIQNRLPSPLRYKKSQ | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 296
Sequence Mass (Da): 33581
Location Topology: Multi-pass membrane protein
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A0A183J936 | MFVIDKSRYDTTDCYLHPCNAPYNDVDLQYDPNTYSLLVENGVDTMLAKHVAHLFIRDPLQVYKGRIEQDDKLSSEHFETIQSSNWLNMRFKPPPIDASSIGWRVEFRPTEVQLTDFENAAYVCFVVLLTRVMLSYHIIFTIPISEVNENMKRAQK | 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: 156
Sequence Mass (Da): 18225
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A0A183ISY6 | MILFGCSKPNHPTGGVWDCEHHSVCDKENPKILFSWARNAPSLSLPDNVGVAVGGDSGIDNYVVQVHYNAKFTGEVLDYSGVVLNVTSLKPRYFADVLLMVSSAYYNIPPHMSEVALNISCTYYGPTPLHIFAYRTHAHSLGRIITGYNILNDQWTLIGKGNPQWPQRFYPTTPEVVAEPGSILAAQCIFNSTTRDTVTYIGAHGKNEMCNFYMYIYVESEYGTMLKQLGECLDSNDTKLFAKYPAEARKPLERNPLLEMEANMTMERFGEN | Cofactor: Binds 2 Cu(2+) ions per subunit.
EC: 1.14.17.3
Catalytic Activity: a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical
Sequence Length: 272
Sequence Mass (Da): 30484
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A0A183NHC3 | MFCLNVEIVQCFGFLSYGVLSNRSPTYKRLRAKQLVEVNYLCVHKKLRSKRMAPVLIREVTRRVHLRGRFQALFTSGTLLPKPVSKCRYWHRPLNPRKLLECGFSHLTHNMTLQRTIKLYRLPEAPLVKGFRQMTKKDVPKAWPLLSEYLEKFNIHPIFTKEEFQHFFVPRDDVVYSFIVENGDGQITDFCSFYVLPSSVMKSKQHNSLRAAYSFYNVSTVTPWPALIQDMLISAKQVSLHIYSC | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
EC: 2.3.1.97
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Sequence Length: 245
Sequence Mass (Da): 28681
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A0A1S1NT41 | MRLRFTGSCAGVPSRQRNVSGLTLQPEHSRRWYLIDCGEGTQHQLMRMSLSLARLEAVLITHVHGDHCYGLPGLLASASMAGRRTPLTLIGPQAVWTFLTAVRETTGLHLDFPLHFIDAATLTESLVLTEFTITAAALSHGIECHGYAFEERGIEASLDTARLEADGVPRGPLWGRLQKGETVYDAQGRQLKGEHYQLMARRPRRLVVSGDNNVPARLTGLCQGADLLVHEATYTEEVIERLGTDNGHCSAARIAAFAEAEGVPNLLLTHFSPRYGRDRRAQNSMAELEREARDRYTGCLALAEDLQPYVLSREGELIIAAA | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Sequence Length: 322
Sequence Mass (Da): 35450
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A0A0B7B0I7 | MVLSQLLLRKRVGQAFVLLGLTTTIMCLWIAQHEWEYHSSDTHSLRRHLNGDKVREYVFVNALLDEIHGDADIKQDSNDYNDMLQQKISDKSSEPSFQEPCPLYPSDVLVGRLAGIKECVAPEELALMYPDVEVGGRVRPKNCTAAEKVAIIIPFRKRFTHLYILMNNLIPLLQRQLIDARFFIIEQAMPTTFNRASLFNIGFLEALKFDNYDCFIFHDVDLIPLNDKNLYRCDDHPIHFAVAMDKYNYQLPYKTYFGGVVGFTKEQYLKINGNSNLYFGWGGEDDDLYERIINKKYEIARPYNDVGKYDMIRHIQDSGNEDNCDRRRLLKSATERQDIEGLNTVKYQKMYINVKSHMTWINVFLDMNEILATAPDSLRQEMEMKHSDARSNLCNFSRGASIHE | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 404
Sequence Mass (Da): 46953
Location Topology: Single-pass type II membrane protein
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T1G1I0 | EEKPVKIDKWDGSALKNALDDHTKKIFKEKFGYVESFRLMDGRLILCTISVVFALFAFAWDYIYPFPKSRDVLIICIYYTYFVMMLVLTIYMTYIEKGCFMLALEKDKTMLDPDNIWKLTSKLKRFDDKYELHISYTNGISKKNKSGHFVKSVCNFFDEEGQLCENSFEKEVLNLHASLSPNKKEN | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 186
Sequence Mass (Da): 21871
Location Topology: Multi-pass membrane protein
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A0A183J6C5 | MDCLNQLGSVPWIVNKRVLDVMLTIFRDKGDEKLSIPRSPWNLPKLPKIISADHQEMVKIXXXXXXXXXXXXXXXXXXXXXXEIKKLRTKVYSLWCATLYKLSIANHFRDRVLFFPHNLDFRGRVYPFPRYFNHIGDDVSRGLLKFAKGYPLGKDGLNWLKLHCVNLTGSKKRDAVAIRLKYAEEKMDDILDSADNPLTGRRWWTKSDEPWQTLACCIEIADAVRSPNPEEHICHFPVHQDGSCNGLQHYAALGRDSIGAHQVNLRAVDTPQDVYSGVATLVEAKRQRDAAAGMAIAQSLKGVVKRKLVKQTVMTTVYGVTMYGARRQILKQLQSLDNFPKDLNFNASYYLMKLTFQSLGQIFNSARMIQHWLTDVANLISKDCMQSVRWRTPLNFPVTQPYYRQKMVKMIQSILENMGRWFIDAYLQKGEWNDDERQAMKYYMRNRFASLPKKGDFDLNEVLSSTYFFS | 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)
Sequence Length: 470
Sequence Mass (Da): 54268
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A0A2D0V164 | LLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIFGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWLGKITGYCYNELYGKAHFWLMFIGVNLTFFPQHFLGLTGFPRRYSDFADYFAGWNLVSSLGSTISIVGVVFFIYIIYDVYVWEEQFIAWIEDGGESWASLEWAHFSPPSFHTYEVLPLLYDADKNIKYFRMFDFGIIFFGLCKPIGFLKGYVSIKSLILFTQVFSACLLTDAMVAYVEESEYASFHFASLGEYGTAAIYNAIALCGHNPAIFGVEYLENGTRVAAHSCKLTMHSILPGITESYHPEVSGAFYDRLPLWLPKGEGAVMRANMTPSLYSYVSEVTLKALLWNDTELVQRMLKVLMTQFQFPLDNLTYISTDEGYQNWAKKLNKSCNIRVPSDKWCSYEENVYVTSFKRKIIIKWEPSYR | 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: 555
Sequence Mass (Da): 63131
Location Topology: Multi-pass membrane protein
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A0A7G9AE66 | EDFDRREIVRKTWGREGLVNGEQIQRVFLLGTPKNRTVLATWETLMHQESQTYRDILLWDFTDTFFNLTLKEIHFLSWAAEFCHNVKFIFKGDADVFVNVENIVDFLKRHDPTEDLFVGDIIYNARPIRVRKSKYYIPESMYGLSIYPAYAGGGGFLLSSCTMRKLSRACREVELFPIDDVFLGMCLQRISLKPILHEGFKTFGIVKPSAAPHLQTFDPCFYKDLMVVHSLKVA | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 234
Sequence Mass (Da): 27157
Location Topology: Single-pass type II membrane protein
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T1EE36 | MEYMATSSPSSSPEWPAKFSHIRKVLGRAGPLSCPDFEPGPENLNFLQNVCKVLIIGAGGLGCELLKDLALFGFCNIHIIDMDTIDLSNLNRQFLFRHHDIGKPKAIVAAEFIKSRISDCNVTPHYAKIQDFYSEFYREFHIIVCGLDSIVARRWINGLLVSMLVYDDDGNLDQSSIIPLVDGGTEGFKGNVRVILPGLTPCIECTLDFYPPQVNYPLCTIAHTPRLPEHCIEYVRLLLWPKENPFGDTVSIDGDNPEHIQWILKKAVERGNEFNIHDITYRLTQGVVKNIIPAVASTNAVIAALCATEVFKLAVSCYSPLNNYLIFNDLEGIYSHAFEAEKKEDCAVCSQVPQSLAFSYSDTLLSLINFLQESKQYQLKSPGIITEVAGKTRTLYMSTVKSLEAATKANLRKTLAELELENGQLIYVADQTSPSNLTFKLVLS | Pathway: Protein modification; protein neddylation.
Function: Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
EC: 6.2.1.64
Catalytic Activity: ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.
Sequence Length: 444
Sequence Mass (Da): 49463
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H9LDA7 | YIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYTKTFQGPPHGIQVERDKSNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIFKSQAETGEIKGHYLNATAGTSEEMMKRAECARELGVPIVMHDYLTGGFTANTSLAHYCRNNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREATKWSPDLAAACEVWKEIKFEYETIDTL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 379
Sequence Mass (Da): 42192
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V5IQZ6 | MNDISDNSSNSLANGGTVANSDIPKDGTGVLSIDPWLEPFKDTLKSRYSKAQSWIDTINKTEGGLEKFSRGTEIFGFNVDKDNTITYREWAPNAKQASLIGEFNNWDRNAHRMKKNEFGVFEITIPPTANGQPAIPHNSKIKITLELPDGQWVDRLPAWIKYVTQDLSVSPAYEARFWNPPQSERYTFKHKRPSKPESLRIYEAHVGISSPECKVATYKEFTKTMLPRIKNLGYNAIQLMAIMEHAYYASFGYQVNSFFAASSRYGPPEDLKELVDTAHAMGIAVLLDVVHSHASKNVLDGLNEFDGTDHQYFHGGGRGKHDLWDSRLFNYGHHEVMRFLLSNLRFWMDEYAFDGFRFDGVTSMLYLHHGIGTGFSGGYHEYFGPDVDEEAVVYLMLANEMLHQLYPNVITVAEDVSGMPALCLPLSLGGVGFDYRLAMAIPDMWIKILKEKKDEEWDMANITWTLTNRRHGEKTIAYCESHDQALVGDKTLMMHLCDAELYTNMSILTPLTPVIDRGMALHKMIRLLTHSLGGEGYLNFEGNEFGHPEWLDFPREGNQNSFWYARRQLNLTEDGLLRYQYLNNFDRSMNLTEDKYGWLHAPQAYISLKHEGDKVIVFERAGLVFVFNFHPSNSYTDYRIGIEQAGTYRIVLDSDTKEHGGFNRLDPQTRFFTSDLPWNNRKNSTHVYIPARTAFVLALESTLSE | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.18
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Length: 705
Sequence Mass (Da): 80524
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T1F2C9 | MKRQKCFYFNDDDEPKKKKFNADLDSLILDTNPDCIDHTSSPRFRYPTEVGFFSLDSESNFRDDNSSLTYLYGKRLKNKKLNLDLKVGYDTFVGKKENDIQGLGDIFKWISLHPPFNTLTKKGEKLKSLQTDFICWRGLLRKFLCTPYELNENWLIIVRKFKGTHYLVEIKTDEKKQEEREQTTRLKEMSYWGFKFEQYMTTEKPDGKPVTNVPVNNHKQFVSVFLEEKLIAKKIKMTRYKLLKWWSQSILIGVKKIVAGFRDDDGIVREVTKLYTKNIPDQCQSIRNAWNPKVCFNFLDKLLDFIRENVTDENRSYMFEFEPGKKIVKCFHLHQDQAKDGSVTASNTITTTATETSTTVTATTSTAAATTEESANVSTAAATSDTIGNDGACSSNSNNDNNVDENSDDKMNYAKIEVLPQWYRDLFRK | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 429
Sequence Mass (Da): 49664
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T1FQG8 | MCHLICRYHQCVFISVHSWKQVVGPVWIAVIYVNQVAYAVSLVAEGSKMDETSECFSLSKLNVRHLVAIILFALATNVQYKTFAYLASLRRNKAGHVVTTNYKPPNAGMFQQLNLSSPHYFAEIVIYFAVLVAMGTNCLTWMTVTYCVACHMTYLAYVTHQYYLDTFSNVYPKHRNIIIPFLF | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Catalytic Activity: di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH
EC: 1.3.1.94
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 183
Sequence Mass (Da): 20952
Location Topology: Multi-pass membrane protein
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A0A1E7U006 | MRARFVPPLILVLLLVILQWQLWNGRGSVREVAQLRTQLADQKDANAKAALNNERLASEVNDLKDGLEMVEERARAELGMVKPNEVFVQIAH | 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: 92
Sequence Mass (Da): 10416
Location Topology: Single-pass type II membrane protein
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T1FZU4 | LSSGNSSNDLASLFECPVCFDYALPPIMQCQSGHIVCSHCRPKLQFCPTCRGALGNIRNLAMEKVASQVLFPCRYMSNGCEASLPHTDKANHEDGCEFRPYNCPCPGASCKWQGSLEQVMPHLLQQHKSITTLQGEDIVFLATDINLPGAVDWVMMQTCFGHHFMLVLEKQEKSEGNQLFYTIVQLIGTRKQAESFAYRLELNGQKRRLTWEATPRSIHDGVQSAINSSDCLVFDTNVARLFADNGNLSINVTINTC | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
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: 257
Domain: The RING-type zinc finger domain is essential for ubiquitin ligase activity.
Sequence Mass (Da): 28597
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