ID   HEMH_WOLPP              Reviewed;         317 AA.
AC   B3CLU1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   02-SEP-2026, entry version 87.
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}; OrderedLocusNames=WP0751;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54859.1; -; Genomic_DNA.
DR   RefSeq; WP_007302167.1; NC_010981.1.
DR   AlphaFoldDB; B3CLU1; -.
DR   SMR; B3CLU1; -.
DR   KEGG; wpi:WP0751; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_4_1_5; -.
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   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..317
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000116089"
FT   BINDING         190
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         270
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   317 AA;  36383 MW;  DF69E8F550217990 CRC64;
     MKKAVILFNL GGPDSLSAVR PFLFNLFYDK RIINLPNPFR FLLAKFISKR RESTAQEIYE
     HIGGKSPILE NTKAQADALE LKLNENGNHV YKIFICMRYW HPFADEVVKS VKQFDPDEII
     LLPLYPQYST TTTLSSIENW QKNAKLECNT KTIHHYYDNE DFIEAHVNLT SKYYKLASKI
     GKPRVLFSAH SLPLSIIKKG DPYASQIEKT VKLIVKKLNI EDLDWGICYQ SKVGPVKWLE
     PSTESELSRA KDDNIPVVLS PISFVSEHSE TLVELDIEYK AIIKDGYYFR VPTLSTDLLF
     IKCLADLCLD HSQSTDL
//