| Accession | TIGR03217 |
| Name | 4OH_2_O_val_ald |
| Function | 4-hydroxy-2-oxovalerate aldolase |
| Gene Symbol | dmpG |
| Trusted Cutoff | 286.00 |
| Domain Trusted Cutoff | 286.00 |
| Noise Cutoff | 147.55 |
| Domain Noise Cutoff | 147.55 |
| Isology Type | equivalog |
| EC Number | 4.1.3.39 |
| HMM Length | 334 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Other |
| Gene Ontology Term | GO:0008701: 4-hydroxy-2-oxovalerate aldolase activity molecular_function |
| Author | Haft DH |
| Entry Date | Dec 19 2006 9:00AM |
| Last Modified | Dec 12 2011 10:29PM |
| Comment | Members of this protein family are 4-hydroxy-2-oxovalerate aldolase, also called 4-hydroxy-2-ketovalerate aldolase and 2-oxo-4-hydroxypentanoate aldolase. This enzyme, part of the pathway for the meta-cleavage of catechol, produces pyruvate and acetaldehyde. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; EC 1.2.1.10) to acetyl-CoA. The two enzymes are tightly associated. |
| References | RN [1]
RM PMID: 7496535
RT The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences.
RA Platt A, Shingler V, Taylor SC, Williams PA
RL Microbiology. 1995 Sep;141 ( Pt 9):2223-33.
RN [2]
RM PMID: 12764229
RT Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.
RA Manjasetty BA, Powlowski J, Vrielink A
RL Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6992-7. Epub 2003 May 22. |
| Genome Property | GenProp0708: catechol meta-cleavage pathway (HMM) |
