HMM Summary Page: TIGR00537

Functionputative methylase
Trusted Cutoff87.00
Domain Trusted Cutoff87.00
Noise Cutoff78.10
Domain Noise Cutoff78.10
Isology Typehypoth_equivalog
HMM Length179
Mainrole CategoryUnknown function
Subrole CategoryEnzymes of unknown specificity
AuthorHaft DH
Entry DateOct 19 1999 4:29PM
Last ModifiedFeb 14 2011 3:27PM
CommentThe gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase (Medline 95189105). Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes.
ReferencesA2 hmmalign GA hmmsearch RN [1] RM 99237242 RT Functional analysis of the hemK gene product involvement in protoporphyrinogen oxidase activity in yeast. RA Le Guen L, Santos R, Camadro JM RL FEMS Microbiol Lett 1999 Apr 1;173(1):175-82 RN [2] RM 95189105 RT Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli. RA Nakayashiki T, Nishimura K, Inokuchi H RL Gene 1995 Feb 3;153(1):67-70 AL ClustalW