Ontology | Accession | Term | GO Evidence | Evidence Ontology (ECO) Code | Reference | Comments |
---|---|---|---|---|---|---|
Molecular Function | GO:0003995 | acyl-CoA dehydrogenase activity |
Inferred from Sequence Model
Term mapped from: InterPro:PS00073
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Molecular Function | GO:0016627 | oxidoreductase activity, acting on the CH-CH group of donors |
Inferred from Sequence Model
Term mapped from: InterPro:PF02770
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Biological Process | GO:0055114 | oxidation-reduction process |
Inferred from Sequence Model
Term mapped from: InterPro:PF02770
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Molecular Function | GO:0050660 | flavin adenine dinucleotide binding |
Inferred from Sequence Model
Term mapped from: InterPro:G3DSA:1.10.540.10
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
Database | Xref | Pathway | Version | Evidence | PMID |
---|---|---|---|---|---|
KEGG | bcm01100 | Metabolic pathways | 73.0+/03-31, Mar 15 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | bcm00071 | Fatty acid degradation | 73.0+/03-31, Mar 15 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | bcm00380 | Tryptophan metabolism | 73.0+/03-31, Mar 15 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | bcm01130 | Biosynthesis of antibiotics | 73.0+/03-31, Mar 15 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | bcm00310 | Lysine degradation | 73.0+/03-31, Mar 15 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
Analysis | Accession | Description | Interpro Accession | Interpro Description | Amino Acid Start | Amino Acid Stop | E-value |
---|---|---|---|---|---|---|---|
ProSitePatterns | PS00073 | Acyl-CoA dehydrogenases signature 2. | IPR006089 | Acyl-CoA dehydrogenase, conserved site | 347 | 366 | - |
PIRSF | PIRSF016578 | 148 | 391 | 1.0E-12 | |||
Gene3D | G3DSA:2.40.110.10 | 134 | 241 | 7.9E-41 | |||
Pfam | PF02771 | Acyl-CoA dehydrogenase, N-terminal domain | IPR013786 | Acyl-CoA dehydrogenase/oxidase, N-terminal | 19 | 131 | 3.7E-35 |
CDD | cd01151 | GCD | 6 | 394 | 0.0 | ||
SUPERFAMILY | SSF47203 | IPR036250 | Acyl-CoA dehydrogenase-like, C-terminal | 245 | 392 | 4.03E-42 | |
PIRSF | PIRSF016578 | 13 | 95 | 5.9E-4 | |||
Pfam | PF02770 | Acyl-CoA dehydrogenase, middle domain | IPR006091 | Acyl-CoA oxidase/dehydrogenase, central domain | 135 | 229 | 2.8E-21 |
SUPERFAMILY | SSF56645 | IPR009100 | Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily | 6 | 241 | 1.7E-78 | |
Gene3D | G3DSA:1.10.540.10 | IPR037069 | Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily | 1 | 133 | 1.9E-43 | |
Gene3D | G3DSA:1.20.140.10 | 243 | 395 | 2.0E-42 | |||
Pfam | PF00441 | Acyl-CoA dehydrogenase, C-terminal domain | IPR009075 | Acyl-CoA dehydrogenase/oxidase C-terminal | 242 | 387 | 7.0E-29 |