| Accession | TIGR00713 |
| Name | hemL |
| Function | glutamate-1-semialdehyde-2,1-aminomutase |
| Gene Symbol | hemL |
| Trusted Cutoff | 527.30 |
| Domain Trusted Cutoff | 527.30 |
| Noise Cutoff | 281.90 |
| Domain Noise Cutoff | 281.90 |
| Isology Type | equivalog |
| EC Number | 5.4.3.8 |
| HMM Length | 423 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Heme, porphyrin, and cobalamin |
| Gene Ontology Term | GO:0005737: cytoplasm cellular_component |
| | GO:0006779: porphyrin-containing compound biosynthetic process biological_process |
| | GO:0042286: glutamate-1-semialdehyde 2,1-aminomutase activity molecular_function |
| Author | Haft DH |
| Entry Date | Feb 1 2000 10:52AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme, glutamate-1-semialdehyde-2,1-aminomutase (glutamate-1-semialdehyde aminotransferase, GSA aminotransferase), contains a pyridoxal phosphate attached at a Lys residue at position 283 of the seed alignment. It is in the family of class III aminotransferases.
|
| References | AL clustalw_manual
DR PROSITE; PDOC00519; Aminotransferases class-III pyridoxal-phosphate attachment site
DR PFAM; PF00202; Aminotransferases class-III pyridoxal-phosphate
DR ECOCYC; EG10432; hemL
DR EXPERIMENTAL; EGAD|19989|EC0154; Escherichia coli
DR EXPERIMENTAL; EGAD|10151|9957; Propionibacterium freudenreichii
DR EXPERIMENTAL; EGAD|76320|82044; Hordeum vulgare
DR HAMAP; MF_00375; 349 of 360 |
| Genome Property | GenProp0217: 5-aminolevulinate biosynthesis (glutamate pathway) (HMM) |
