Reviewed,
UniProtKB/Swiss-Prot P70584 (ACDSB_RAT)
Last modified
February 9, 2010.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||
| 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 + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | Homotetramer Potential. |
| Subcellular location | |
| 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 | acyl-CoA metabolic process Ref.1 Inferred from direct assay. Source: MGI fatty acid beta-oxidationTraceable author statement. Source: RGD oxidation reductionInferred 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.1Inferred from direct assay. Source: RGD short-branched-chain-acyl-CoA dehydrogenase activity Ref.1Inferred 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 | |||||
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
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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. |
| IPI | IPI00189773. |
| PIR | S71321. |
| RefSeq | NP_037216.1. |
| UniGene | Rn.44423 |
3D structure databases | |
| SMR | P70584. Positions 52-432. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P70584. |
PTM databases | |
| PhosphoSite | P70584. |
Proteomic databases | |
| PRIDE | P70584. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000027999; ENSRNOP00000027999; ENSRNOG00000020624; Rattus norvegicus. [Genome view] |
| GeneID | 25618. |
| KEGG | rno:25618. |
| NMPDR | fig|10116.3.peg.3122. |
| UCSC | NM_013084. rat. |
Organism-specific databases | |
| CTD | 25618. |
| RGD | 2013. Acadsb. |
Phylogenomic databases | |
| eggNOG | roNOG15182. |
| HOVERGEN | P70584. |
| InParanoid | P70584. |
| OMA | SKIGTIY. |
| OrthoDB | EOG9FFGM4. |
| PhylomeDB | P70584. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-11692. |
Gene expression databases | |
| ArrayExpress | P70584. |
| Genevestigator | 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_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] |
| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


