Reviewed,
UniProtKB/Swiss-Prot P81140 (GCDH_PIG)
Last modified
January 19, 2010.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutaryl-CoA dehydrogenase, mitochondrial Short name=GCD EC=1.3.99.7 | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 408 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO2 in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. |
| Catalytic activity | Glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the acyl-CoA dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred 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 glutaryl-CoA dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | ‹1 – 13 | ›13 | Mitochondrion Ref.1 | ||||||
| Chain | 14 – 408 | 395 | Glutaryl-CoA dehydrogenase, mitochondrial | PRO_0000000529 | |||||
Regions | |||||||||
| Nucleotide binding | 147 – 156 | 10 | FAD By similarity | ||||||
| Nucleotide binding | 147 – 150 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 182 – 184 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 357 – 361 | 5 | FAD By similarity | ||||||
| Nucleotide binding | 386 – 388 | 3 | FAD By similarity | ||||||
| Region | 107 – 108 | 2 | Substrate binding By similarity | ||||||
| Region | 257 – 264 | 8 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 384 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 156 | 1 | FAD By similarity | ||||||
| Binding site | 156 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 264 | 1 | Substrate By similarity | ||||||
| Binding site | 289 | 1 | FAD By similarity | ||||||
| Binding site | 300 | 1 | FAD By similarity | ||||||
| Binding site | 385 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 386 | 1 | FAD By similarity | ||||||
| Binding site | 404 | 1 | FAD; via carbonyl oxygen By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Pork and human cDNAs encoding glutaryl-CoA dehydrogenase." Goodman S.I., Kratz L.E., Frerman F.E. Prog. Clin. Biol. Res. 375:169-173(1992) [PubMed: 1438360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 14-38 AND 375-407. Tissue: Liver. |
Cross-references
3D structure databases | |
|---|---|
| SMR | P81140. Positions 16-405. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSSSCT00000015003; ENSSSCP00000014599; ENSSSCG00000013729; Sus scrofa. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | P81140. |
Enzyme and pathway databases | |
| BRENDA | 1.3.99.7. 249. |
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. False negative. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GCDH_PIG | ||||||||
| Accession | Primary (citable) accession number: P81140 | ||||||||
| Entry history |
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| 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


