ID   HEMH_GLOC7              Reviewed;         387 AA.
AC   B7KGB9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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};
GN   OrderedLocusNames=PCC7424_2167;
OS   Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS   7424)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX   NCBI_TaxID=65393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7424;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001291; ACK70590.1; -; Genomic_DNA.
DR   RefSeq; WP_015954196.1; NC_011729.1.
DR   AlphaFoldDB; B7KGB9; -.
DR   SMR; B7KGB9; -.
DR   STRING; 65393.PCC7424_2167; -.
DR   EnsemblBacteria; ACK70590; ACK70590; PCC7424_2167.
DR   KEGG; cyc:PCC7424_2167; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_4_1_3; -.
DR   OMA; LGDPYHC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000002384; 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..387
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000119604"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   387 AA;  44455 MW;  6380BC538B3F1962 CRC64;
     MGRVGVLLLN LGGPDRLEDV RPFLFNLFSD PEIIRLPVPW LQKPLAWLIS TLRSRKSQEN
     YLQIGGGSPL RKITEAQAEA LEKRLEEIGH SVQVYIGMRY WHPFTEEAIA RIKRDRIQKL
     VILPLYPQFS ISTSGSSFRV LEEIWKQDPS LKQIEYSLIP SWYDNPGYLE AMADLISQEL
     GQYSNPDTVH IFFSAHGVPQ SYVDEAGDPY QKEIEECTRL IMKTLNRPND YTLAYQSRVG
     PVEWLKPYTE DALKELGEQG IKEILVIPIS FVSEHIETLQ EIDIEYREVA EEAGIDHFQR
     VPALNTHPIF IDSLAQLVIN SLTENSYTFE EITRPKKNMK MYPQERWEWG MTTAAEVWNG
     RLAMIGFIAL LIELISGHGP LHFVGLL