HMM Summary Page: TIGR00539

Functionputative oxygen-independent coproporphyrinogen III oxidase
Trusted Cutoff205.40
Domain Trusted Cutoff205.40
Noise Cutoff179.65
Domain Noise Cutoff179.65
Isology Typehypoth_equivalog
EC Number1.3.99.22
HMM Length361
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryHeme, porphyrin, and cobalamin
Gene Ontology TermGO:0004109: coproporphyrinogen oxidase activity molecular_function
GO:0006779: porphyrin-containing compound biosynthetic process biological_process
AuthorHaft DH
Entry DateOct 19 1999 4:29PM
Last ModifiedFeb 14 2011 3:27PM
CommentExperimentally 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.
ReferencesA2 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