ID   HEMH_PROM5              Reviewed;         391 AA.
AC   A2BVI7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=P9515_05891;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
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DR   EMBL; CP000552; ABM71798.1; -; Genomic_DNA.
DR   RefSeq; WP_011819905.1; NC_008817.1.
DR   AlphaFoldDB; A2BVI7; -.
DR   SMR; A2BVI7; -.
DR   STRING; 167542.P9515_05891; -.
DR   EnsemblBacteria; ABM71798; ABM71798; P9515_05891.
DR   KEGG; pmc:P9515_05891; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_4_3_3; -.
DR   OMA; LGDPYHC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000001589; 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.
FT   CHAIN           1..391
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000019338"
FT   BINDING         196
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"
SQ   SEQUENCE   391 AA;  44109 MW;  B9D83D80479F541B CRC64;
     MEKIGVLLMN LGGPERITDV GPFLYNLFSD PEIIRLPVPA FQKPLAWLIS TLRSTTSQQA
     YLSIGGGSPI RRITEQQARE LQSKLRDKGL NVTTYIAMRY WHPFTESAIA DMKADGIDQI
     VVLPLYPHFS ISTSGSSFRE LKKLRDSDSD FKKIPMRCVR SWFSQSGYLK SMVELISEQI
     SLCESPADAH IFFTAHGVPK SYVEEAGDPY KEQIEDCSLL IINELEKYLG HSNSYTLSYQ
     SRVGPVEWLK PYTEEVLTDL GKAKVNDLIV VPISFVGEHI ETLQEIDIEY KEIAEKAGIV
     NFRRVKALNT HPTFIEGLSD LVVSSLNGPV VNIEKASELP EKVKLYPQEK WQWGWNNSSE
     VWNGRVAMIV FLILFIELIS GSGPLHKLGI L