CPLM-018452

Genbank Nucleotide ID

Acyl-coenzyme A synthetase ACSM1, mitochondrial

Protein Synonyms/Alias

Acyl-CoA synthetase medium-chain family member 1; Butyrate--CoA ligase 1; Butyryl-coenzyme A synthetase 1; Lipoate-activating enzyme; Middle-chain acyl-CoA synthetase 1

Mus musculus (Mouse)

Position	Peptide	Type	References
144	GTTQLKAKDILYRIQ	acetylation	[1]
144	GTTQLKAKDILYRIQ	ubiquitination	[2]
179	ASECPDLKTKLVVSD	ubiquitination	[2]
210	SPDHTCIKSKMKDPM	acetylation	[1]
210	SPDHTCIKSKMKDPM	ubiquitination	[2]
214	TCIKSKMKDPMAIFF	ubiquitination	[2]
230	SGTTGYPKMAKHNQG	ubiquitination	[2]
233	TGYPKMAKHNQGLAF	ubiquitination	[2]
252	PSCRKLLKLKTSDIL	acetylation	[1]
324	YRMVLQQKTSNLRFP	ubiquitination	[2]
352	PEEYEQWKQRTGLSI	acetylation	[1]
352	PEEYEQWKQRTGLSI	ubiquitination	[2]
387	IKRGSIGKAILPFDL	acetylation	[3, 4, 5]
387	IKRGSIGKAILPFDL	succinylation	[4]
387	IKRGSIGKAILPFDL	ubiquitination	[2]
501	AVVSSPDKDRGEVVK	acetylation	[1]
527	HDQEQLIKELQHHVK	acetylation	[1]
534	KELQHHVKSVTAPYK	acetylation	[1]
534	KELQHHVKSVTAPYK	ubiquitination	[2]
541	KSVTAPYKYPRKVEF	acetylation	[1]
554	EFVSELPKTVTGKIK	acetylation	[1]
559	LPKTVTGKIKRKELR	acetylation	[1]
568	KRKELRNKEFGQL**	acetylation	[3]

[1] 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]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[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

Functions as GTP-dependent lipoate-activating enzyme that generates the substrate for lipoyltransferase (By similarity). 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).

NP_BIND 222 230 ATP (By similarity).
BINDING 448 448 ATP (By similarity).
BINDING 463 463 ATP (By similarity).
BINDING 559 559 ATP (By similarity).

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO:0003996; F:acyl-CoA ligase activity; ISS:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0047760; F:butyrate-CoA ligase activity; ISS:UniProtKB.
GO:0015645; F:fatty acid ligase activity; IDA:MGI.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0006633; P:fatty acid biosynthetic process; IDA:MGI.

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

PF00501; AMP-binding
PF13193; DUF4009

PS00455; AMP_BINDING