Accession | TIGR00539 |
Name | hemN_rel |
Function | putative oxygen-independent coproporphyrinogen III oxidase |
Trusted Cutoff | 205.40 |
Domain Trusted Cutoff | 205.40 |
Noise Cutoff | 179.65 |
Domain Noise Cutoff | 179.65 |
Isology Type | hypoth_equivalog |
EC Number | 1.3.99.22 |
HMM Length | 361 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Heme, porphyrin, and cobalamin |
Gene Ontology Term | GO:0004109: coproporphyrinogen oxidase activity molecular_function |
| GO:0006779: porphyrin-containing compound biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Oct 19 1999 4:29PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Experimentally determined examples of oxygen-independent coproporphyrinogen III oxidase, an enzyme that replaces HemF function under anaerobic conditions, belong to a family of proteins described by the HMM hemN. This HMM, hemN_rel, models a closely related protein, shorter at the amino end and lacking the region containing the motif PYRT[SC]YP found in members of the hemN family. Several species, including E. coli, Helicobacter pylori, Aquifex aeolicus, and Chlamydia trachomatis, have members of both this family and the E. coli hemN family. The member of this family from Bacillus subtilis was shown to complement an hemF/hemN double mutant of Salmonella typimurium and to prevent accumulation of coproporphyrinogen III under anaerobic conditions, but the exact role of this protein is still uncertain. It is found in a number of species that do not synthesize heme de novo. |
References | A2 hmmalign
AL ClustalW
RM 96303504
RT Characterization of Bacillus subtilis hemN.
RA Homuth G, Heinemann M, Zuber U, Schumann W
RL Microbiology 1996 Jul;142 ( Pt 7):1641-9 |