| Accession | TIGR00109 |
| Name | hemH |
| Function | ferrochelatase |
| Gene Symbol | hemH |
| Trusted Cutoff | 124.60 |
| Domain Trusted Cutoff | 124.60 |
| Noise Cutoff | 114.20 |
| Domain Noise Cutoff | 114.20 |
| Isology Type | equivalog |
| EC Number | 4.99.1.1 |
| HMM Length | 322 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Heme, porphyrin, and cobalamin |
| Gene Ontology Term | GO:0004325: ferrochelatase activity molecular_function |
| | GO:0006779: porphyrin-containing compound biosynthetic process biological_process |
| Author | Anolik RT, Richardson DL |
| Entry Date | Apr 20 1999 2:07PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Human 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. |
| References | DR 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 Property | GenProp0222: protoheme from protoporphyrin IX (HMM) |
