ACSM1_MOUSE
ID ACSM1_MOUSE Reviewed; 573 AA.
AC Q91VA0; Q3UED4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
DE EC=6.2.1.2 {ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:12709059};
DE AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
DE AltName: Full=Benzoate--CoA ligase;
DE EC=6.2.1.25 {ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:12709059};
DE AltName: Full=Butyrate--CoA ligase 1;
DE AltName: Full=Butyryl-coenzyme A synthetase 1;
DE AltName: Full=Lipoate-activating enzyme {ECO:0000250|UniProtKB:Q9BEA2};
DE AltName: Full=Middle-chain acyl-CoA synthetase 1 {ECO:0000303|PubMed:11470804};
DE Flags: Precursor;
GN Name=Acsm1;
GN Synonyms=Bucs1, Lae {ECO:0000250|UniProtKB:Q9BEA2},
GN Macs1 {ECO:0000303|PubMed:11470804};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11470804; DOI=10.1074/jbc.m106651200;
RA Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K.,
RA Takahashi S., Sakai J., Yamamoto T.T.;
RT "Molecular identification and characterization of two medium-chain acyl-CoA
RT synthetases, MACS1 and the Sa gene product.";
RL J. Biol. Chem. 276:35961-35966(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 PROTEIN SEQUENCE OF 249-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12709059; DOI=10.1046/j.1432-1033.2003.03571.x;
RA Oka Y., Kobayakawa K., Nishizumi H., Miyamichi K., Hirose S., Tsuboi A.,
RA Sakano H.;
RT "O-MACS, a novel member of the medium-chain acyl-CoA synthetase family,
RT specifically expressed in the olfactory epithelium in a zone-specific
RT manner.";
RL Eur. J. Biochem. 270:1995-2004(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16378734; DOI=10.1016/j.pep.2005.11.006;
RA Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K.;
RT "Purification, characterization, and mass spectrometric sequencing of a
RT medium chain acyl-CoA synthetase from mouse liver mitochondria and
RT comparisons with the homologues of rat and bovine.";
RL Protein Expr. Purif. 47:405-414(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-142; LYS-179; LYS-200;
RP LYS-233; LYS-324; LYS-352; LYS-387; LYS-501 AND LYS-534, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-200; LYS-210; LYS-352;
RP LYS-387; LYS-527; LYS-534 AND LYS-545, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (PubMed:11470804,
CC PubMed:12709059). Capable of activating medium-chain fatty acids (e.g.
CC butyric (C4) to decanoic (C10) acids), and certain carboxylate-
CC containing xenobiotics, e.g. benzoate (PubMed:11470804,
CC PubMed:12709059). Also catalyzes the activation of lipoate to lipoyl-
CC nucleoside monophosphate (By similarity). Activates lipoate with GTP at
CC a 1000-fold higher rate than with ATP and activates both (R)- and (S)-
CC lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate
CC (By similarity). {ECO:0000250|UniProtKB:Q9BEA2,
CC ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:12709059}.
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:0000269|PubMed:11470804, ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
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:0000269|PubMed:11470804, ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + GTP + H(+) = (R)-lipoyl-GMP + diphosphate;
CC Xref=Rhea:RHEA:46700, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:83088, ChEBI:CHEBI:86460;
CC Evidence={ECO:0000250|UniProtKB:Q9BEA2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46701;
CC Evidence={ECO:0000250|UniProtKB:Q9BEA2};
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:0000269|PubMed:11470804,
CC ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
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:0000269|PubMed:11470804,
CC ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11470804,
CC ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000269|PubMed:11470804,
CC ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000305|PubMed:11470804, ECO:0000305|PubMed:12709059};
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:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.58 mM for hexanoate {ECO:0000269|PubMed:11470804};
CC KM=0.46 mM for octanoate {ECO:0000269|PubMed:11470804};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BEA2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11470804}. Mitochondrion
CC {ECO:0000269|PubMed:12709059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VA0-2; Sequence=VSP_028392;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney.
CC {ECO:0000269|PubMed:11470804}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB059428; BAB64534.1; -; mRNA.
DR EMBL; AK149550; BAE28952.1; -; mRNA.
DR EMBL; AK149586; BAE28977.1; -; mRNA.
DR EMBL; BC016414; AAH16414.1; -; mRNA.
DR EMBL; BC022149; AAH22149.1; -; mRNA.
DR CCDS; CCDS21783.1; -. [Q91VA0-1]
DR RefSeq; NP_473435.1; NM_054094.5. [Q91VA0-1]
DR AlphaFoldDB; Q91VA0; -.
DR SMR; Q91VA0; -.
DR STRING; 10090.ENSMUSP00000036140; -.
DR SwissLipids; SLP:000001205; -.
DR iPTMnet; Q91VA0; -.
DR PhosphoSitePlus; Q91VA0; -.
DR SwissPalm; Q91VA0; -.
DR jPOST; Q91VA0; -.
DR MaxQB; Q91VA0; -.
DR PaxDb; Q91VA0; -.
DR PeptideAtlas; Q91VA0; -.
DR PRIDE; Q91VA0; -.
DR ProteomicsDB; 285849; -. [Q91VA0-1]
DR ProteomicsDB; 285850; -. [Q91VA0-2]
DR Antibodypedia; 49877; 70 antibodies from 18 providers.
DR DNASU; 117147; -.
DR Ensembl; ENSMUST00000047929; ENSMUSP00000036140; ENSMUSG00000033533. [Q91VA0-1]
DR GeneID; 117147; -.
DR KEGG; mmu:117147; -.
DR UCSC; uc009jlm.1; mouse. [Q91VA0-1]
DR UCSC; uc012fsv.1; mouse. [Q91VA0-2]
DR CTD; 116285; -.
DR MGI; MGI:2152200; Acsm1.
DR VEuPathDB; HostDB:ENSMUSG00000033533; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000161138; -.
DR InParanoid; Q91VA0; -.
DR OMA; ECTAPCA; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q91VA0; -.
DR TreeFam; TF354287; -.
DR Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
DR Reactome; R-MMU-177162; Conjugation of phenylacetate with glutamine.
DR BioGRID-ORCS; 117147; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q91VA0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91VA0; protein.
DR Bgee; ENSMUSG00000033533; Expressed in right kidney and 37 other tissues.
DR ExpressionAtlas; Q91VA0; baseline and differential.
DR Genevisible; Q91VA0; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018858; F:benzoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0015645; F:fatty acid ligase activity; IDA:UniProtKB.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
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; IDA:MGI.
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 Acetylation; Alternative splicing; ATP-binding; Direct protein sequencing;
KW Fatty acid metabolism; GTP-binding; Ligase; Lipid metabolism; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..573
FT /note="Acyl-coenzyme A synthetase ACSM1, mitochondrial"
FT /id="PRO_0000306092"
FT BINDING 222..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 81
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 142
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 142
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 179
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 200
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 200
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 233
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 324
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 387
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 387
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 501
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 534
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 534
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 545
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 369..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028392"
FT CONFLICT 465
FT /note="D -> V (in Ref. 2; BAE28977)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="L -> F (in Ref. 2; BAE28977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 64760 MW; 557F25D467CA305B CRC64;
MQWLKSFQIC KVLQGFSLSP TQLHRRLFSR VGAPRWNDHD SPEEFNFASD VLDYWAQMEE
EGKRGPSPAF WWVNGQGDEI KWSFRKLRDL TCRTANVFEQ ICGLQQGDHL ALILPRVPEW
WLVTVGCMRT GIIFMPGTTQ LKAKDILYRI QISRAKAIVT TASLVPEVES VASECPDLKT
KLVVSDHSHE GWLDFCSLIK SASPDHTCIK SKMKDPMAIF FTSGTTGYPK MAKHNQGLAF
RSYIPSCRKL LKLKTSDILW CMSDPGWILA TVGCLIEPWT SGCTVFIHHL PQFDPKVIVE
VLFKYPITQC LAAPGVYRMV LQQKTSNLRF PTLEHCTTGG ESLLPEEYEQ WKQRTGLSIH
EVYGQSETGI SSATLREMKI KRGSIGKAIL PFDLQIIDEK GNILPPNTEG YIGIRIKPTR
PLGLFMEYEN SPESTSEVEC GDFYNSGDRA TIDEEGYIWF LGRGDDVINA SGYRIGPVEV
ENALAEHPAV AESAVVSSPD KDRGEVVKAF IVLNPEFLSH DQEQLIKELQ HHVKSVTAPY
KYPRKVEFVS ELPKTVTGKI KRKELRNKEF GQL
