Q8HXY8 (ACADM_MACFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 56.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial Short name=MCAD EC=1.3.8.7 | ||||
| Gene names |
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| Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) | ||||
| Taxonomic identifier | 9541 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca![]() |
Protein attributes
| Sequence length | 421 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 | This enzyme is specific for acyl chain lengths of 4 to 16 By similarity. |
| Catalytic activity | A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein. |
| Cofactor | FAD By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Miscellaneous | A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues. |
| 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 beta-oxidation Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | acyl-CoA dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB flavin adenine dinucleotide bindingInferred 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 – 25 | 25 | Mitochondrion By similarity | ||||||
| Chain | 26 – 421 | 396 | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial | PRO_0000000503 | |||||
Regions | |||||||||
| Nucleotide binding | 158 – 167 | 10 | FAD By similarity | ||||||
| Nucleotide binding | 191 – 193 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 306 – 308 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 316 – 317 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 374 – 378 | 5 | FAD By similarity | ||||||
| Nucleotide binding | 403 – 405 | 3 | FAD By similarity | ||||||
| Region | 278 – 281 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 401 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 167 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 216 | 1 | Substrate By similarity | ||||||
| Binding site | 402 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 413 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 279 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 301 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Isolation and characterization of cDNA for macaque neurological disease genes." Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Temporal cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB083301 mRNA. Translation: BAC20580.1. |
3D structure databases | |
| ProteinModelPortal | Q8HXY8. |
| SMR | Q8HXY8. Positions 35-420. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q8HXY8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG000224. |
Enzyme and pathway databases | |
| UniPathway | UPA00660. |
Family and domain databases | |
| Gene3D | 1.10.540.10. 1 hit. 2.40.110.10. 1 hit. |
| 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] |
| 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 | ACADM_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q8HXY8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
