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ACS2A_HUMAN
ID   ACS2A_HUMAN             Reviewed;         577 AA.
AC   Q08AH3; B3KTT9; O75202;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Acyl-coenzyme A synthetase ACSM2A, mitochondrial;
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:Q68CK6};
DE   AltName: Full=Acyl-CoA synthetase medium-chain family member 2A;
DE   AltName: Full=Benzoate--CoA ligase;
DE            EC=6.2.1.25 {ECO:0000250|UniProtKB:Q68CK6};
DE   AltName: Full=Butyrate--CoA ligase 2A;
DE   AltName: Full=Butyryl-coenzyme A synthetase 2A;
DE   AltName: Full=Middle-chain acyl-CoA synthetase 2A;
DE   Flags: Precursor;
GN   Name=ACSM2A; Synonyms=ACSM2, MACS2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 299-577, AND VARIANT
RP   LEU-513.
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [6]
RP   REVIEW.
RX   PubMed=27351777; DOI=10.1080/17425255.2016.1206888;
RA   van der Sluis R., Erasmus E.;
RT   "Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its
RT   role in fatty acid metabolism and the detoxification of benzoic acid and
RT   aspirin.";
RL   Expert Opin. Drug Metab. Toxicol. 12:1169-1179(2016).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of L64P mutant of human acyl-CoA synthetase medium-chain
RT   family member 2A.";
RL   Submitted (FEB-2008) to the PDB data bank.
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 32-577 IN COMPLEXES WITH ATP;
RP   COENZYME A; IBUPROFEN AND MAGNESIUM.
RX   PubMed=19345228; DOI=10.1016/j.jmb.2009.03.064;
RA   Kochan G., Pilka E.S., von Delft F., Oppermann U., Yue W.W.;
RT   "Structural snapshots for the conformation-dependent catalysis by human
RT   medium-chain acyl-coenzyme A synthetase ACSM2A.";
RL   J. Mol. Biol. 388:997-1008(2009).
RN   [9]
RP   VARIANT LEU-513.
RX   PubMed=12654705; DOI=10.1161/01.hyp.0000064944.60569.87;
RA   Iwai N., Mannami T., Tomoike H., Ono K., Iwanaga Y.;
RT   "An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to
RT   multiple risk factors.";
RL   Hypertension 41:1041-1046(2003).
RN   [10]
RP   VARIANT LEU-513.
RX   PubMed=16521160; DOI=10.1002/mnfr.200500241;
RA   Lindner I., Rubin D., Helwig U., Nitz I., Hampe J., Schreiber S.,
RA   Schrezenmeir J., Doering F.;
RT   "The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is
RT   associated with risk factors of the metabolic syndrome in a Caucasian study
RT   population.";
RL   Mol. Nutr. Food Res. 50:270-274(2006).
CC   -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC       acyl-CoA, the first step in fatty acid metabolism (By similarity).
CC       Capable of activating medium-chain fatty acids (e.g. butyric (C4) to
CC       decanoic (C10) acids), and certain carboxylate-containing xenobiotics,
CC       e.g. benzoate (By similarity). {ECO:0000250|UniProtKB:Q68CK6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC         ChEBI:CHEBI:456215; EC=6.2.1.25;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC         Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC         Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q68CK6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q68CK6}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23497.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK096039; BAG53201.1; -; mRNA.
DR   EMBL; AC137056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125176; AAI25177.1; -; mRNA.
DR   EMBL; AC003034; AAC23497.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS32401.1; -.
DR   RefSeq; NP_001295101.1; NM_001308172.1.
DR   RefSeq; NP_001295883.1; NM_001308954.1.
DR   RefSeq; XP_016878412.1; XM_017022923.1.
DR   PDB; 2VZE; X-ray; 2.45 A; A/B/C=32-577.
DR   PDB; 2WD9; X-ray; 2.60 A; A/B/C=32-576.
DR   PDB; 3B7W; X-ray; 2.00 A; A=32-577.
DR   PDB; 3C5E; X-ray; 1.60 A; A=32-577.
DR   PDB; 3DAY; X-ray; 1.95 A; A=32-577.
DR   PDB; 3EQ6; X-ray; 2.40 A; A/B=32-577.
DR   PDB; 3GPC; X-ray; 1.90 A; A/B=32-577.
DR   PDBsum; 2VZE; -.
DR   PDBsum; 2WD9; -.
DR   PDBsum; 3B7W; -.
DR   PDBsum; 3C5E; -.
DR   PDBsum; 3DAY; -.
DR   PDBsum; 3EQ6; -.
DR   PDBsum; 3GPC; -.
DR   AlphaFoldDB; Q08AH3; -.
DR   SMR; Q08AH3; -.
DR   BioGRID; 125840; 2.
DR   IntAct; Q08AH3; 1.
DR   MINT; Q08AH3; -.
DR   STRING; 9606.ENSP00000459451; -.
DR   iPTMnet; Q08AH3; -.
DR   PhosphoSitePlus; Q08AH3; -.
DR   BioMuta; ACSM2A; -.
DR   DMDM; 257050995; -.
DR   MassIVE; Q08AH3; -.
DR   MaxQB; Q08AH3; -.
DR   PaxDb; Q08AH3; -.
DR   PeptideAtlas; Q08AH3; -.
DR   PRIDE; Q08AH3; -.
DR   ProteomicsDB; 58672; -.
DR   Antibodypedia; 67877; 86 antibodies from 20 providers.
DR   DNASU; 123876; -.
DR   Ensembl; ENST00000219054.10; ENSP00000219054.6; ENSG00000183747.12.
DR   Ensembl; ENST00000396104.2; ENSP00000379411.2; ENSG00000183747.12.
DR   Ensembl; ENST00000573854.6; ENSP00000459451.1; ENSG00000183747.12.
DR   Ensembl; ENST00000575690.5; ENSP00000460349.1; ENSG00000183747.12.
DR   GeneID; 123876; -.
DR   KEGG; hsa:123876; -.
DR   MANE-Select; ENST00000573854.6; ENSP00000459451.1; NM_001308172.2; NP_001295101.1.
DR   UCSC; uc002dhf.5; human.
DR   CTD; 123876; -.
DR   DisGeNET; 123876; -.
DR   GeneCards; ACSM2A; -.
DR   HGNC; HGNC:32017; ACSM2A.
DR   HPA; ENSG00000183747; Group enriched (kidney, liver).
DR   MIM; 614358; gene.
DR   neXtProt; NX_Q08AH3; -.
DR   OpenTargets; ENSG00000183747; -.
DR   PharmGKB; PA162375402; -.
DR   VEuPathDB; HostDB:ENSG00000183747; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000164294; -.
DR   InParanoid; Q08AH3; -.
DR   OMA; TPSDWAW; -.
DR   OrthoDB; 683933at2759; -.
DR   PhylomeDB; Q08AH3; -.
DR   TreeFam; TF354264; -.
DR   PathwayCommons; Q08AH3; -.
DR   Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   SignaLink; Q08AH3; -.
DR   BioGRID-ORCS; 123876; 7 hits in 1020 CRISPR screens.
DR   ChiTaRS; ACSM2A; human.
DR   EvolutionaryTrace; Q08AH3; -.
DR   GenomeRNAi; 123876; -.
DR   Pharos; Q08AH3; Tbio.
DR   PRO; PR:Q08AH3; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q08AH3; protein.
DR   Bgee; ENSG00000183747; Expressed in right lobe of liver and 94 other tissues.
DR   ExpressionAtlas; Q08AH3; baseline and differential.
DR   Genevisible; Q08AH3; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018858; F:benzoate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:BHF-UCL.
DR   GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR   GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR   GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; NAS:BHF-UCL.
DR   GO; GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; IDA:BHF-UCL.
DR   GO; GO:0070328; P:triglyceride homeostasis; NAS:BHF-UCL.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..577
FT                   /note="Acyl-coenzyme A synthetase ACSM2A, mitochondrial"
FT                   /id="PRO_0000306093"
FT   BINDING         139
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         221..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7"
FT   BINDING         359..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7"
FT   BINDING         461
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7"
FT   BINDING         469..471
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         472
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         501
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         532
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         540..542
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|PubMed:19345228"
FT   BINDING         557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7"
FT   MOD_RES         513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68CK6"
FT   VARIANT         335
FT                   /note="V -> L (in dbSNP:rs4643305)"
FT                   /id="VAR_058692"
FT   VARIANT         337
FT                   /note="V -> G (in dbSNP:rs4586421)"
FT                   /id="VAR_058694"
FT   VARIANT         513
FT                   /note="S -> L (in dbSNP:rs1133607)"
FT                   /evidence="ECO:0000269|PubMed:10493829,
FT                   ECO:0000269|PubMed:12654705, ECO:0000269|PubMed:16521160"
FT                   /id="VAR_035247"
FT   VARIANT         561
FT                   /note="A -> T (in dbSNP:rs1054977)"
FT                   /id="VAR_035248"
FT   CONFLICT        463
FT                   /note="N -> D (in Ref. 1; BAG53201, 3; AAI25177 and 4;
FT                   AAC23497)"
FT                   /evidence="ECO:0000305"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:3B7W"
FT   HELIX           46..49
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           51..59
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           83..98
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           142..152
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           164..170
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          179..186
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           194..200
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          214..220
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          224..227
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           235..245
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            246..249
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          256..259
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           266..271
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           274..278
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          282..286
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           293..302
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           312..319
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            323..325
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          333..339
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           343..353
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          358..363
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            364..366
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          367..371
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          392..395
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          408..413
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           430..435
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          441..450
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          456..461
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           462..464
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          471..473
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           475..483
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          488..498
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   TURN            499..501
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          502..511
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           513..515
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           520..534
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           537..539
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   STRAND          542..548
FT                   /evidence="ECO:0007829|PDB:3C5E"
FT   HELIX           560..567
FT                   /evidence="ECO:0007829|PDB:3C5E"
SQ   SEQUENCE   577 AA;  64223 MW;  16167FC69562436F CRC64;
     MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA
     GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANVLSGA CGLQRGDRVA VVLPRVPEWW
     LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK
     LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL
     KAKMDAGWTG LQASDIMWTI SDTGWILNIL CSLMEPWALG ACTFVHLLPK FDPLVILKTL
     SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCVTVGES LLPETLENWR AQTGLDIRES
     YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQIIDDKGN VLPPGTEGDI GIRVKPIRPI
     GIFSGYVDNP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RANDIINSSG YRIGPSEVEN
     ALMEHPAVVE TAVISSPDPV RGEVVKAFVV LASQFLSHDP EQLTKELQQH VKSVTAPYKY
     PRKIEFVLNL PKTVTGKIQR AKLRDKEWKM SGKARAQ
 
 
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