Reviewed, UniProtKB/Swiss-Prot P70584 (ACDSB_RAT)

Names and origin

Protein names

Recommended name:
    Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=SBCAD
    EC=1.3.99.-
Alternative name(s):
    2-methyl branched chain acyl-CoA dehydrogenase
      Short name=2-MEBCAD
    2-methylbutyryl-coenzyme A dehydrogenase
      Short name=2-methylbutyryl-CoA dehydrogenase

Gene names

Name:

Acadsb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF.
Cofactor	FAD.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer Potential.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Ref.1 Inferred from direct assay. Source: RGD short-branched-chain-acyl-CoA dehydrogenase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 432	399	Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial		PRO_0000000521
Sites
	Active site	414	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	284	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P70584-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: D35380C6DE3FC7DA	FASTA	432	47,824
	10 20 30 40 50 60 MAVSAFQLWR AGGLLRRNFL THSSSWKIPP RVLKSSQPEA LLSVTNNALC FAPLQTFTDE 70 80 90 100 110 120 DIMMQKAVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ GMMGIEVEAK YGGTEASFLC 130 140 150 160 170 180 SVLVIEELAK VDASVALLCD IQNTVINKLF RKHGTEEQKA TYLPKLVTEK LGSFCLSEAG 190 200 210 220 230 240 AGSDSFALKT RADKSGNYYV INGSKMWISN AEHAELFLVF ANVDPPSGYR GITCFLVDRD 250 260 270 280 290 300 TEGFQIGRRE NKMGIRASST CQLTFENVKV PETSVLGKIG HGYKYAIGSL NEGRIGIAAQ 310 320 330 340 350 360 MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAHVA TQLEAARLLT YNAARLVEAG 370 380 390 400 410 420 RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGTSNIQ 430 LNTIAKHIDA EY

References

[1]

"Cloning of a cDNA for short/branched chain acyl-Coenzyme A dehydrogenase from rat and characterization of its tissue expression and substrate specificity." Willard J., Vicanek C., Battaile K.P., van Veldhoven P.P., Fauq A.H., Rozen R., Vockley J. Arch. Biochem. Biophys. 331:127-133(1996) [PubMed: 8660691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-59. Strain: Sprague-Dawley. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U64451 mRNA. Translation: AAB17136.1.
IPI	IPI00189773.
PIR	S71321.
RefSeq	NP_037216.1.
UniGene	Rn.44423
3D structure databases
HSSP	HSSP built from PDB template 1BUC based on UniProtKB Q06319.
SMR	P70584. Positions 52-432.
ModBase	Search...
PTM databases
PhosphoSite	P70584.
Proteomic databases
PRIDE	P70584.
Genome annotation databases
Ensembl	ENSRNOG00000020624. Rattus norvegicus. [Contig view]
GeneID	25618.
KEGG	rno:25618.
NMPDR	fig|10116.3.peg.3122.
Organism-specific databases
RGD	2013. Acadsb.
Phylogenomic databases
HOVERGEN	P70584.
OMA	P70584. IEWMGGV.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11692.
Gene expression databases
ArrayExpress	P70584.
GermOnline	ENSRNOG00000020624. Rattus norvegicus.
Family and domain databases
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	607379.

Entry information

Entry name

ACDSB_RAT

Accession

Primary (citable) accession number: P70584

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)