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Reviewed, UniProtKB/Swiss-Prot P70584 (ACDSB_RAT)

Last modified February 9, 2010. Version 90. 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

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.

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_0000000521

Regions

Nucleotide binding174 – 18310FAD By similarity
Nucleotide binding207 – 2093FAD By similarity
Nucleotide binding387 – 3915FAD; shared with dimeric partner By similarity
Nucleotide binding416 – 4183FAD By similarity
Region229 – 2302Substrate binding By similarity
Region291 – 2944Substrate binding By similarity

Sites

Active site4141Proton acceptor By similarity
Binding site1831Substrate; via carbonyl oxygen By similarity
Binding site2831Substrate By similarity
Binding site3191FAD; shared with dimeric partner By similarity
Binding site3301FAD; shared with dimeric partner By similarity
Binding site4151Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue2841N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P70584-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: D35380C6DE3FC7DA

FASTA43247,824
        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 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U64451 mRNA. Translation: AAB17136.1.
IPIIPI00189773.
PIRS71321.
RefSeqNP_037216.1.
UniGeneRn.44423

3D structure databases

SMRP70584. Positions 52-432.
ModBaseSearch...

Protein-protein interaction databases

STRINGP70584.

PTM databases

PhosphoSiteP70584.

Proteomic databases

PRIDEP70584.

Genome annotation databases

EnsemblENSRNOT00000027999; ENSRNOP00000027999; ENSRNOG00000020624; Rattus norvegicus. [Genome view]
GeneID25618.
KEGGrno:25618.
NMPDRfig|10116.3.peg.3122.
UCSCNM_013084. rat.

Organism-specific databases

CTD25618.
RGD2013. Acadsb.

Phylogenomic databases

eggNOGroNOG15182.
HOVERGENP70584.
InParanoidP70584.
OMASKIGTIY.
OrthoDBEOG9FFGM4.
PhylomeDBP70584.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11692.

Gene expression databases

ArrayExpressP70584.
GenevestigatorP70584.
GermOnlineENSRNOG00000020624. Rattus norvegicus.

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_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
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...

Other Resources

NextBio607379.

Entry information

Entry nameACDSB_RAT
AccessionPrimary (citable) accession number: P70584
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 9, 2010
This is version 90 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