ID   HEMH_ZYMMO              Reviewed;         334 AA.
AC   P57779; Q5NQS7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=ZMO0303;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee H.J., Kang H.S.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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; AF212041; AAG02158.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV88927.2; -; Genomic_DNA.
DR   RefSeq; WP_011240238.1; NZ_CP035711.1.
DR   AlphaFoldDB; P57779; -.
DR   SMR; P57779; -.
DR   STRING; 264203.ZMO0303; -.
DR   EnsemblBacteria; AAV88927; AAV88927; ZMO0303.
DR   GeneID; 58026165; -.
DR   KEGG; zmo:ZMO0303; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_0_0_5; -.
DR   OMA; LGDPYHC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000001173; 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..334
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175236"
FT   BINDING         203
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         281
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   CONFLICT        3
FT                   /note="E -> D (in Ref. 1; AAG02158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="D -> V (in Ref. 1; AAG02158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125..126
FT                   /note="SG -> FR (in Ref. 1; AAG02158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="S -> Y (in Ref. 1; AAG02158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333
FT                   /note="G -> W (in Ref. 1; AAG02158)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  37426 MW;  AA88A6B75A7BC72A CRC64;
     MTESNNPLPI SEKIGVLLVN LGTPDAPNAK ALRRYLGQFL SDQRVIELPA VFWQIILRGI
     ILPFRAPRSA RAYQKIWTNE GSPLAAITKK QAQGLQKRMP NITVDYAMRY GTPSISSRLE
     KLIASGCRRI LLAPLYPQYS AASTATVQDE AYRYLQKIRW QPNLRSLEPY YTHPAYIQTL
     KKNIEDQIKA LDFKPDSLLL SYHGMPVKTR ELGDPYYFQC QATSQALSSL LDIPVITSFQ
     SRFGSQKWFT PATDMTLKEL PSKNIRNLAV AMPGFSADCL ETLEEIALQG KSTFLEAGGE
     NFAALRCLND SEESLAMLEI LVNQGLSGWL KSGE