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 27-MAR-2024, entry version 125.
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; 3.
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; 9606-ENSP00000459451; -.
DR PeptideAtlas; Q08AH3; -.
DR ProteomicsDB; 58672; -.
DR Antibodypedia; 67877; 93 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 AGR; HGNC:32017; -.
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; FISLNCT; -.
DR OrthoDB; 5474118at2759; -.
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 1097 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 95 other cell types or 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; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR43605:SF14; ACYL-COENZYME A SYNTHETASE ACSM2A, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//
