ID   HEMH_YEREN              Reviewed;         322 AA.
AC   P43413; P77999;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 93.
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   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6471/76 / Serotype O:3;
RX   PubMed=8559076; DOI=10.1111/j.1365-2958.1995.mmi_17030575.x;
RA   Skurnik M., Venho R., Toivanen P., Al-Hendy A.;
RT   "A novel locus of Yersinia enterocolitica serotype O:3 involved in
RT   lipopolysaccharide outer core biosynthesis.";
RL   Mol. Microbiol. 17:575-594(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8081C / Serotype O:8;
RX   PubMed=8932701; DOI=10.1099/13500872-142-2-277;
RA   Zhang L., Toivanen P., Skurnik M.;
RT   "The gene cluster directing O-antigen biosynthesis in Yersinia
RT   enterocolitica serotype 0:8: identification of the genes for mannose and
RT   galactose biosynthesis and the gene for the O-antigen polymerase.";
RL   Microbiology 142:277-288(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}.
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DR   EMBL; Z47767; CAA87697.1; -; Genomic_DNA.
DR   EMBL; U46859; AAC60760.1; -; Genomic_DNA.
DR   PIR; S70735; S70735.
DR   AlphaFoldDB; P43413; -.
DR   SMR; P43413; -.
DR   STRING; 1443113.LC20_01453; -.
DR   eggNOG; COG0276; Bacteria.
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..322
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175233"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         275
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   CONFLICT        14..18
FT                   /note="GTPDA -> EHRMP (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="D -> V (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="C -> W (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..149
FT                   /note="KG -> AS (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="R -> P (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228..233
FT                   /note="QIMMTY -> TKSRVHI (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287..289
FT                   /note="VFI -> IFL (in Ref. 2; AAC60760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306..322
FT                   /note="KGHIDLLEQLVRDHLSC -> EGP (in Ref. 1; CAA87697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  36534 MW;  261CA9E21B19882A CRC64;
     MKQSKLGVLM VNLGTPDAPT PQAVKRYLAE FLSDRRVVDT SPWLWWPLLR GVILPIRSPR
     VAKLYQSVWM DEGSPLLVYS RRQQKALAER MPEIPVELGM SYGSPNLPDA IDKLLAQGVT
     KLVVLPLYPQ YSCSTSAAVW DAVARILKGY RRLPSISFIR DYAEHPAYIS ALKQSVENSF
     VQHGKPDRLV LSFHGIPKRY AQLGDDYPQR CEDTSRALRA EIALPAEQIM MTYQSRFGRE
     PWLTPYTDET LKSLPSQGVK HIQLICPGFS ADCLETLEEI KEQNREVFIH AGGEKFEYIP
     ALNDDKGHID LLEQLVRDHL SC