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Reviewed, UniProtKB/Swiss-Prot Q5RF40 (ACDSB_PONAB)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 + ETF = 2,3-dehydroacyl-CoA + reduced ETF.

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 processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 432399Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000330465

Sites

Active site4141Proton acceptor By similarity

Amino acid modifications

Modified residue2841N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RF40-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 09BB4B21ED945736

FASTA43247,485
        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 

« Hide

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

CR857321 mRNA. Translation: CAH89617.1.
RefSeqNP_001124722.1.
UniGenePab.19469

3D structure databases

SMRQ5RF40. Positions 52-432.
ModBaseSearch...

Genome annotation databases

GeneID100171571.

Phylogenomic databases

HOVERGENQ5RF40.

Family and domain databases

InterProIPR006089. 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]
Gene3DG3DSA: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.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACDSB_PONAB
AccessionPrimary (citable) accession number: Q5RF40
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents