| Accession | TIGR00510 |
| Name | lipA |
| Function | lipoyl synthase |
| Gene Symbol | lipA |
| Trusted Cutoff | 310.25 |
| Domain Trusted Cutoff | 310.25 |
| Noise Cutoff | 187.30 |
| Domain Noise Cutoff | 187.30 |
| Isology Type | equivalog |
| EC Number | 2.8.1.8 |
| HMM Length | 302 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Lipoate |
| Gene Ontology Term | GO:0009107: lipoate biosynthetic process biological_process |
| | GO:0017140: lipoic acid synthase activity molecular_function |
| Author | Haft DH |
| Entry Date | Oct 15 1999 3:13PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system.
The family shows strong sequence conservation. |
| References | AL ClustalW
RN [1]
RM 93352559
RT Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae.
RA Sulo P, Martin NC
RL J Biol Chem 1993 Aug 15;268(23):17634-9
RN [2]
RM 99330162
RT The lipoate synthase from Escherichia coli is an iron-sulfur protein.
RA Ollagnier-de Choudens S, Fontecave M
RL FEBS Lett 1999 Jun 18;453(1-2):25-8
DR HAMAP; MF_00206; 384 of 391 |
| Genome Property | GenProp0745: lipoyl-protein attachment (HMM) |
