| Accession | TIGR00747 |
| Name | fabH |
| Function | 3-oxoacyl-[acyl-carrier-protein] synthase III |
| Gene Symbol | fabH |
| Trusted Cutoff | 292.10 |
| Domain Trusted Cutoff | 292.10 |
| Noise Cutoff | 135.65 |
| Domain Noise Cutoff | 135.65 |
| Isology Type | subfamily |
| EC Number | 2.3.1.180 |
| HMM Length | 322 |
| Mainrole Category | Fatty acid and phospholipid metabolism |
| Subrole Category | Biosynthesis |
| Gene Ontology Term | GO:0004315: 3-oxoacyl-[acyl-carrier-protein] synthase activity molecular_function |
| | GO:0006633: fatty acid biosynthetic process biological_process |
| Author | Haft DH, Loftus BJ |
| Entry Date | Mar 2 2000 2:33PM |
| Last Modified | Feb 14 2011 7:55PM |
| Comment | FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity.
Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. |
| References | SE EC_num
AL clustalw
DR EXPERIMENTAL; EGAD|23257|EC1091; Escherichia coli
DR EXPERIMENTAL; EGAD|22159|22835; Rhodobacter capsulatus
DR EXPERIMENTAL; EGAD|60481|63308; spinach
RN [1]
RM 20096678
RT beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.
RA Choi KH, Heath RJ, Rock CO
RL J Bacteriol 2000 Jan;182(2):365-70
RN [2]
RT The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli.
RA Davies C, Heath RJ, White SW, Rock CO
RL Structure Fold Des 2000;8(2):185-195
RN [3]
RM 94291939
DR HAMAP; MF_01815; 327 of 330 |
| Genome Property | GenProp0681: fatty acid biosynthesis from acetyl-CoA (HMM) |
