| Accession | TIGR00171 |
| Name | leuD |
| Function | 3-isopropylmalate dehydratase, small subunit |
| Gene Symbol | leuD |
| Trusted Cutoff | 116.25 |
| Domain Trusted Cutoff | 116.25 |
| Noise Cutoff | 81.90 |
| Domain Noise Cutoff | 81.90 |
| Isology Type | equivalog_domain |
| EC Number | 4.2.1.33 |
| HMM Length | 188 |
| Mainrole Category | Amino acid biosynthesis |
| Subrole Category | Pyruvate family |
| Gene Ontology Term | GO:0003861: 3-isopropylmalate dehydratase activity molecular_function |
| | GO:0009098: leucine biosynthetic process biological_process |
| | GO:0009316: 3-isopropylmalate dehydratase complex cellular_component |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:08PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria.
Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. |
| References | DR PROSITE; PDOC00423;
SE TIGR
GA hmmls
AL clustalw
DR HAMAP; MF_01031; 321 of 330 |
| Genome Property | GenProp0164: leucine biosynthesis from pyruvate and acetyl-CoA (HMM) |
