ID   HEMH_RHOCA              Reviewed;         351 AA.
AC   Q59735;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
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};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAS100;
RX   PubMed=7592455; DOI=10.1128/jb.177.22.6693-6694.1995;
RA   Kanazireva E., Biel A.J.;
RT   "Cloning and overexpression of the Rhodobacter capsulatus hemH gene.";
RL   J. Bacteriol. 177:6693-6694(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAS100;
RX   PubMed=8621079; DOI=10.1016/0378-1119(96)00845-1;
RA   Kanazireva E., Biel A.J.;
RT   "Nucleotide sequence of the Rhodobacter capsulatus hemH gene.";
RL   Gene 170:149-150(1996).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U34391; AAA88884.1; -; Genomic_DNA.
DR   PIR; JC4752; JC4752.
DR   RefSeq; WP_013065942.1; NZ_VIBE01000009.1.
DR   AlphaFoldDB; Q59735; -.
DR   SMR; Q59735; -.
DR   PRIDE; Q59735; -.
DR   GeneID; 31489154; -.
DR   OMA; LGDPYHC; -.
DR   UniPathway; UPA00252; UER00325.
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.
FT   CHAIN           1..351
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175191"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   351 AA;  39955 MW;  1D1E61B859E2AE1F CRC64;
     MTIANRILPH APADHPPVPV PRVGVLLANL GTPDATDYWS MRRYLNEFLS DRRVIDYPIW
     KWQPLLQLII LSKRPFTSGN NYRSIWNEER DESPLMTITR DQVRKLRAAV ETRYGAGNVV
     VDFCMRYGNP STRDVLDDML AQGCERILFL PLYPQYAGAT SATANDQFFR ALMQVKRQPA
     ARTVPEYFAR PSYIEALASS VERVYATLDT RPDVLVASYH GMPKRYHREG DPYHCQCQKT
     SRLLRERLGW GPDSIDTTFQ SVFGTEEWLR PYTVEHVVQL AEAGKKNIAV ISPAFSADCI
     ETLEEINGEI REAFEHAGGE SFTYVPCLND DDLHIAALLE VVEENLAGWI D