HEMH_RICPR
ID HEMH_RICPR Reviewed; 342 AA.
AC Q9ZC84;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Heme synthase {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Protoheme ferro-lyase {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=hemH {ECO:0000255|HAMAP-Rule:MF_00323}; OrderedLocusNames=RP884;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC Rule:MF_00323, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA15306.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ235273; CAA15306.1; ALT_INIT; Genomic_DNA.
DR PIR; B71651; B71651.
DR RefSeq; NP_221230.1; NC_000963.1.
DR RefSeq; WP_004599695.1; NC_000963.1.
DR AlphaFoldDB; Q9ZC84; -.
DR SMR; Q9ZC84; -.
DR STRING; 272947.RP884; -.
DR EnsemblBacteria; CAA15306; CAA15306; CAA15306.
DR GeneID; 57570007; -.
DR KEGG; rpr:RP884; -.
DR PATRIC; fig|272947.5.peg.924; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_4_1_5; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
DR PROSITE; PS00534; FERROCHELATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..342
FT /note="Ferrochelatase"
FT /id="PRO_0000175194"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 342 AA; 39611 MW; 33EA8548F5CF0372 CRC64;
MNKRIAIVLF NLGGPEDIEY VKPFLFNLFY DKAIINLPNP LRYIIAKIIS ITREKKSQKI
YSLIGSKSYL IQETEKQKLA ITEKLKEFIK EDFIIFINMR YSTPFAKEVI GQIKEYNPSE
IILLPLYPQF SSTTTGSSVK NFLQNIDIDI PIKTICCYPI EEDFIKAHVS IIKEKLYDKN
FRILFSAHGL PKRIIKAGDP YSFQIKETVN KIVKELNIKD LDYKITYQSR VGPIEWLKPN
TEDEIELAGK LKKDIIIVPI SFVSEHVETL VELDIEYKLI ADKYKIQYTR IPTLGTNKIF
INSLTNILLR FINNTNTNLV MSSSSKRICP NKFTKCLCNL TN