ID   HEMH_RHOBA              Reviewed;         351 AA.
AC   Q7UFZ7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=RB8233;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294147; CAD78532.1; -; Genomic_DNA.
DR   RefSeq; NP_868254.1; NC_005027.1.
DR   RefSeq; WP_011121766.1; NC_005027.1.
DR   AlphaFoldDB; Q7UFZ7; -.
DR   SMR; Q7UFZ7; -.
DR   STRING; 243090.RB8233; -.
DR   EnsemblBacteria; CAD78532; CAD78532; RB8233.
DR   KEGG; rba:RB8233; -.
DR   PATRIC; fig|243090.15.peg.3968; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_2_0_0; -.
DR   InParanoid; Q7UFZ7; -.
DR   OMA; WLEPDIC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   CDD; cd00419; Ferrochelatase_C; 1.
DR   CDD; cd03411; Ferrochelatase_N; 1.
DR   HAMAP; MF_00323; Ferrochelatase; 1.
DR   InterPro; IPR001015; Ferrochelatase.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175190"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   351 AA;  39081 MW;  AF58FCEED1277164 CRC64;
     MSELPPYDSF LLVSFGGPEG QDDVMPFLEN VLRGKNVPRE RMLEVAEHYK HFGGVSPINE
     QNRQLIAALQ KRFDANGIDL PIYWGNRNWD PYFADTLRQM KADGKKRSLA FFTSMFSCYS
     GCRQYRENII QAREEVGEGA PLVEKVRMGF NHPGFIAAMA DNVSKAAQTI GASPARTKVL
     FTAHSIPMGM ADNCDYEKQL RESCRLVADA CGAVDWDLVY QSRSGPPSQP WLEPDVLDAI
     AEMDDAKKLE SLVILPIGFV SDHMEVLFDL DEEAAQLCRE RGIKMARASA AGTHPDFVEM
     ICGLVQERLG KLNEKPALGE LGPWHDVCPQ DCCLYTPRRP PVAGGRPVQA N