HMM Summary Page: TIGR00109

Gene SymbolhemH
Trusted Cutoff124.60
Domain Trusted Cutoff124.60
Noise Cutoff114.20
Domain Noise Cutoff114.20
Isology Typeequivalog
EC Number4.99.1.1
HMM Length322
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryHeme, porphyrin, and cobalamin
Gene Ontology TermGO:0004325: ferrochelatase activity molecular_function
GO:0006779: porphyrin-containing compound biosynthetic process biological_process
AuthorAnolik RT, Richardson DL
Entry DateApr 20 1999 2:07PM
Last ModifiedFeb 14 2011 3:27PM
CommentHuman ferrochelatase, found at the mitochondrial inner membrane inner surface, was shown in an active recombinant form to be a homodimer. This contrasts to an earlier finding by gel filtration that overexpressed E. coli ferrochelatase runs as a monomer.
ReferencesDR PROSITE; PDOC00462; DR PROSITE; PS00534; FERROCHELATASE SE TIGR GA hmmls AL clustalw RN [1] RM 10561552 RT Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. RA Burden AE, Wu C, Dailey TA, Busch JL, Dhawan IK, Rose JP, Wang B, Dailey HA RL Biochim Biophys Acta 1999 Nov 16;1435(1-2):191-197 RN [2] RM 94334300 RT Overproduction, purification, and characterization of ferrochelatase from Escherichia coli. RA Miyamoto K, Kanaya S, Morikawa K, Inokuchi H RL J Biochem (Tokyo) 1994 Mar;115(3):545-51 DR HAMAP; MF_00323; 290 of 295
Genome PropertyGenProp0222: protoheme from protoporphyrin IX (HMM)