UniProt Accession

 ACDSB_HUMAN; P45954; Q5SQN6; Q96CX7 

Genbank Protein ID

 U12778; AF260678; AF260668; AF260669; AF260670; AF260671; AF260672; AF260673; AF260674; AF260675; AF260676; AF260677; AK314241; AL731666; AC012391; AC073585; CH471066; BC013756; AL831821 

Genbank Nucleotide ID

 AAA74424.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; AAF97921.1; BAG36909.1; CAI10847.1; CAI10847.1; CAI10847.1; EAW49291.1; AAH13756.1; CAD38535.2 

Protein Name

 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 

Gene Name

 ACADSB 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
70	MIKSSVKKFAQEQIA	ubiquitination	[1, 2]
284	GQIGHGYKYAIGSLN	acetylation	[3, 4]
284	GQIGHGYKYAIGSLN	ubiquitination	[1, 2]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

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. 

Sequence Annotation

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

Keyword

 3D-structure; Acetylation; Complete proteome; Disease mutation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 432 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0003995; F:acyl-CoA dehydrogenase activity; EXP:Reactome.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006631; P:fatty acid metabolic process; TAS:ProtInc. 

Interpro

 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. 

Pfam

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

SMART

  

PROSITE

 PS00072; ACYL_COA_DH_1
 PS00073; ACYL_COA_DH_2 

PRINTS