Accession | TIGR02333 |
Name | 2met_isocit_dHY |
Function | 2-methylisocitrate dehydratase, Fe/S-dependent |
Gene Symbol | acnD |
Trusted Cutoff | 1419.85 |
Domain Trusted Cutoff | 1419.85 |
Noise Cutoff | 1137.30 |
Domain Noise Cutoff | 1137.30 |
Isology Type | equivalog |
EC Number | 4.2.1.99 |
HMM Length | 858 |
Gene Ontology Term | GO:0019629: propionate catabolic process, 2-methylcitrate cycle biological_process |
| GO:0047456: 2-methylisocitrate dehydratase activity molecular_function |
Author | Haft DH |
Entry Date | Oct 1 2004 10:30AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Members of this family appear in an operon for the degradation of propionyl-CoA via 2-methylcitrate. This family is homologous to aconitases A and B and appears to act the part as 2-methylisocitrate dehydratase, the enzyme after PrpD and before PrpB. In Escherichia coli, which lacks a member of this family, 2-methylisocitrate dehydratase activity was traced to aconitase B (TIGR00117) (PMID:12473114). |
References | RN [1]
RM 14702315
RT The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo.
RA Grimek TL, Escalante-Semerena JC.
RL J Bacteriol. 2004 Jan;186(2):454-62. |
Genome Property | GenProp0240: propionyl-CoA catabolism via methylcitric acid (HMM) |