Accession | TIGR00173 |
Name | menD |
Function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase |
Gene Symbol | menD |
Trusted Cutoff | 244.20 |
Domain Trusted Cutoff | 244.20 |
Noise Cutoff | 183.05 |
Domain Noise Cutoff | 183.05 |
Isology Type | equivalog |
EC Number | 2.2.1.9 |
HMM Length | 435 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Menaquinone and ubiquinone |
Gene Ontology Term | GO:0009234: menaquinone biosynthetic process biological_process |
| GO:0070204: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity molecular_function |
Author | Haft DH |
Entry Date | Apr 20 1999 2:08PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695).
2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis. |
References | RN [1]
RM PMID:17760421
RT Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity.
RA Jiang M, Cao Y, Guo ZF, Chen M, Chen X, Guo Z
RL Biochemistry. 2007 Sep 25;46(38):10979-89. Epub 2007 Aug 31.
DR HAMAP; MF_01659; 164 of 212 |
Genome Property | GenProp0058: menaquinone biosynthesis via SEPHCHC (HMM) |