Q5RF40 (ACDSB_PONAB) Reviewed, UniProtKB/Swiss-Prot

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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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 transcript 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 By similarity.
Catalytic activity	Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
Cofactor	FAD By similarity.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer Potential.
Subcellular location	Mitochondrion matrix By similarity.
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
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
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_0000330465
Regions
	Nucleotide binding	174 – 183	10	FAD By similarity
	Nucleotide binding	207 – 209	3	FAD By similarity
	Nucleotide binding	387 – 391	5	FAD; shared with dimeric partner By similarity
	Nucleotide binding	416 – 418	3	FAD By similarity
	Region	229 – 230	2	Substrate binding By similarity
	Region	291 – 294	4	Substrate binding By similarity
Sites
	Active site	414	1	Proton acceptor By similarity
	Binding site	183	1	Substrate; via carbonyl oxygen By similarity
	Binding site	283	1	Substrate By similarity
	Binding site	319	1	FAD; shared with dimeric partner By similarity
	Binding site	330	1	FAD; shared with dimeric partner By similarity
	Binding site	415	1	Substrate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	284	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RF40 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 09BB4B21ED945736	FASTA	432	47,485
	10 20 30 40 50 60 MEGLAVRLLR GSRLLRRNFP TCLSSWKIPP HVSKSSQSEA LLNITNNGIH FAPLQTFTDE 70 80 90 100 110 120 EMMIKSSVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ GLMGIEVDPE YGGTGASFLS 130 140 150 160 170 180 TVLVIEELAK VDASVAVFCE IQNTLINTLI RKHGTEEQKG TYLPQLTTEK VGSFCLSEAG 190 200 210 220 230 240 AGSDSFALKT RADKEGDYYV LNGSKMWISS AEHAGLFLVM ANVDPTIGYK GITSFLVDRD 250 260 270 280 290 300 TPGLHIGKPE NKLGLRASST CPLTFENVKV PETNILGQIG HGYKYAIGSL NEGRIGIAAQ 310 320 330 340 350 360 MLGLAQGCFD YTIPYIKERI QFGKRLFDFQ GLQHQVAHVA TQLEAARLLT YNAARLLEAG 370 380 390 400 410 420 KPFIKEASMA KYYASEIAGQ TTSKCIEWMG GVGYTKDYPV EKYFRDAKIG TIYEGASNIQ 430 LNTIAKHIDA EY

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR857321 mRNA. Translation: CAH89617.1.
RefSeq	NP_001124722.1. NM_001131250.1.
UniGene	Pab.19469.
3D structure databases
HSSP	HSSP built from PDB template 1JQI based on UniProtKB P15651.
ProteinModelPortal	Q5RF40.
SMR	Q5RF40. Positions 52-432.
ModBase	Search...
Proteomic databases
PRIDE	Q5RF40.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100171571.
KEGG	pon:100171571.
Organism-specific databases
CTD	36.
Phylogenomic databases
HOVERGEN	HBG000224.
InParanoid	Q5RF40.
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_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. [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.
KO	K09478.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACDSB_PONAB

Accession

Primary (citable) accession number: Q5RF40

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	December 21, 2004
Last modified:	November 16, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program