ID   HEMH_ACIBS              Reviewed;         338 AA.
AC   B0VLE0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-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};
GN   OrderedLocusNames=ABSDF3128;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(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; CU468230; CAP02408.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VLE0; -.
DR   SMR; B0VLE0; -.
DR   KEGG; abm:ABSDF3128; -.
DR   HOGENOM; CLU_018884_0_0_6; -.
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..338
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000116023"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         283
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   338 AA;  38273 MW;  932FC506A99AE2A5 CRC64;
     MSFEQKPKVT VILANLGTPD EATVPAVRRF LKQFLSDPRV IEIPKFIWWI ILNLFVLPFR
     PKRAAHAYAS VWSTDSPMRE IVFEQTQRVQ AYLERENKQF DLTVLPAMTY GNLGIDAVLE
     KLSAHPQEHV ILLPLFPQYS ATSTAPLYDA FAKWIPTQRN LPGLTIIKDY YQHPMFIQAL
     AESVLAYQEQ HGKPEKLLMS FHGIPQPYAD KGDPYADRCR ITAKLVAEAL HLKDDEWAIS
     FQSRFGKQEW VKPYTDQLLQ DWAKQGVKSV QVLSPAFSAD CLETLEELAI QNAELFQQAG
     GGSYAYIPAL NSDQAHIDLL AGLVQANLDA LTHTLAHR
//