ID   HEMH_RHOPS              Reviewed;         345 AA.
AC   Q13CU0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE            EC=4.98.1.1 {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=RPD_0861;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC       {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heme b + 2 H(+) = protoporphyrin IX + Fe(2+);
CC         Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1;
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; CP000283; ABE38099.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13CU0; -.
DR   SMR; Q13CU0; -.
DR   STRING; 316057.RPD_0861; -.
DR   KEGG; rpd:RPD_0861; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_0_0_5; -.
DR   BioCyc; RPAL316057:RPD_RS04380-MONOMER; -.
DR   UniPathway; UPA00252; UER00325.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:protoporphyrin ferrochelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00419; Ferrochelatase_C; 1.
DR   CDD; cd03411; Ferrochelatase_N; 1.
DR   FunFam; 3.40.50.1400:FF:000002; Ferrochelatase; 1.
DR   Gene3D; 3.40.50.1400; -; 2.
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   NCBIfam; TIGR00109; hemH; 1.
DR   PANTHER; PTHR11108; FERROCHELATASE; 1.
DR   PANTHER; PTHR11108:SF1; FERROCHELATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   SUPFAM; SSF53800; Chelatase; 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..345
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000019362"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         296
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   345 AA;  38640 MW;  03E1EBFBA96A0EDA CRC64;
     MTVIVPIHGP APAPAPVPER VGVLLVNLGT PDSCDTKGVR VYLREFLSDP RVIENQGLFW
     KLALNGIILN TRPARKAKDY QKIWNHEKNE SPLKTITRAQ AEKLAASLTD RSHLVVDWAM
     RYGNPSLRSR IEALVARGCS RLLVVPLYPQ YSAATSATVC DQAFRVLREL RAQPTLRVTP
     PYYRDDAYID ALANSINAHL ATLSFEPEMI VASFHGMPQA YIEKGDPYQS QCVATVDALR
     ERMGLDEKKL LLTFQSRFGF DQWLQPYTDK TIEKLAKDGV RKLAVVMPGF ASDCLETLEE
     IAQENAEIFM HNGGEEFSAI PCLNDSDDGI AVIRQLVMRE LQGWL
//