UniProt Accession

 ACSM5_MOUSE; Q8BGA8; Q8BJS0; Q8BM02; Q8BWQ8; Q8BWS7 

Genbank Protein ID

 AK040650; AK050132; AK050219; AK050288; AK050458; AK080219; AK149591; BC095985 

Genbank Nucleotide ID

 BAC30656.1; BAC34084.1; BAC34130.1; BAC34167.1; BAC34268.1; BAC37850.1; BAE28980.1; AAH95985.1 

Protein Name

 Acyl-coenzyme A synthetase ACSM5, mitochondrial 

Protein Synonyms/Alias

  

Gene Name

 Acsm5 

Gene Synonyms/Alias

 Macs3 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
96	WTFEELGKQSRKAAN	acetylation	[1, 2, 3, 4, 5]
96	WTFEELGKQSRKAAN	succinylation	[4]
151	GVSQLTAKDLKYRLQ	acetylation	[2, 3, 5]
154	QLTAKDLKYRLQAAR	acetylation	[5]
302	ELPRVDAKTILNTLC	acetylation	[1, 3, 4, 5]
302	ELPRVDAKTILNTLC	succinylation	[4]
335	QEDLTRYKFQCLRHC	acetylation	[1, 2, 3, 5]
540	RELQEHVKTVTAPYK	acetylation	[2, 3, 4]
540	RELQEHVKTVTAPYK	succinylation	[4]
547	KTVTAPYKYPRKVAF	acetylation	[2, 3]
551	APYKYPRKVAFISEL	acetylation	[4]
551	APYKYPRKVAFISEL	succinylation	[4]

Reference

 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). 

Sequence Annotation

 NP_BIND 229 237 ATP (By similarity).
 NP_BIND 367 372 ATP (By similarity).
 BINDING 454 454 ATP (By similarity).
 BINDING 469 469 ATP (By similarity).
 BINDING 565 565 ATP (By similarity).  

Keyword

 Alternative splicing; ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 578 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0047760; F:butyrate-CoA ligase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. 

Interpro

 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 

Pfam

 PF00501; AMP-binding
 PF13193; DUF4009 

SMART

  

PROSITE

 PS00455; AMP_BINDING 

PRINTS