CPLM-020950

Genbank Nucleotide ID

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Protein Synonyms/Alias

SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase

Mus musculus (Mouse)

Position	Peptide	Type	References
88	SSMDENSKMEKSVIQ	acetylation	[1]
165	QKATYLPKLVTEKLG	acetylation	[1]
189	GSDSFAMKTRADKSG	acetylation	[1]
278	PETNILGKIGHGYKY	acetylation	[1]
284	GKIGHGYKYAIGSLN	acetylation	[1, 2]
426	IQLNTIAKHIDAEY*	acetylation	[1, 3, 4]

[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] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[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] 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 greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent (By similarity).

NP_BIND 174 183 FAD (By similarity).
NP_BIND 207 209 FAD (By similarity).
NP_BIND 387 391 FAD; shared with dimeric partner (By
NP_BIND 416 418 FAD (By similarity).
REGION 229 230 Substrate binding (By similarity).
REGION 291 294 Substrate binding (By similarity).
ACT_SITE 414 414 Proton acceptor (By similarity).
BINDING 183 183 Substrate; via carbonyl oxygen (By
BINDING 283 283 Substrate (By similarity).
BINDING 319 319 FAD; shared with dimeric partner (By
BINDING 330 330 FAD; shared with dimeric partner (By
BINDING 415 415 Substrate; via amide nitrogen (By
MOD_RES 284 284 N6-acetyllysine.

Acetylation; Complete proteome; Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.

IPR006089; Acyl-CoA_DH_CS.
IPR006092; Acyl-CoA_DH_N.
IPR006090; Acyl-CoA_Oxase/DH_1.
IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
IPR009075; AcylCo_DH/oxidase_C.
IPR013786; AcylCoA_DH/ox_N.
IPR009100; AcylCoA_DH/oxidase.

PF00441; Acyl-CoA_dh_1
PF02770; Acyl-CoA_dh_M
PF02771; Acyl-CoA_dh_N

PS00072; ACYL_COA_DH_1
PS00073; ACYL_COA_DH_2