AC   MF_00323;
DC   Protein; auto
TR   HAMAP; MF_00323; -; 1; level=0
XX
Names: Ferrochelatase
XX
case <OC:Bacillota> or <OC:Actinomycetota>
ID   CPFC
DE   RecName: Full=Coproporphyrin III ferrochelatase;
DE            EC=4.99.1.9;
GN   Name=cpfC;
else
ID   HEMH
DE   RecName: Full=Ferrochelatase;
DE            EC=4.98.1.1;
DE   AltName: Full=Heme synthase;
DE   AltName: Full=Protoheme ferro-lyase;
GN   Name=hemH;
end case
XX
case <OC:Bacillota> or <OC:Actinomycetota>
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the insertion of ferrous iron into coproporphyrin III to form
CC       Fe-coproporphyrin III.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+);
CC         Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis.
else
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
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=4.98.1.1;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
end case
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- SUBUNIT: Monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family.
XX
DR   Pfam; PF00762; Ferrochelatase; 1; trigger=no
DR   NCBIfam; TIGR00109; HemH; 1; trigger=no
DR   PROSITE; PS00534; FERROCHELATASE; 1; trigger=no
XX
KW   Cytoplasm
KW   Porphyrin biosynthesis
KW   Heme biosynthesis
KW   Lyase
KW   Iron
KW   Metal-binding
XX
GO   GO:0004325; F:ferrochelatase activity
GO   GO:0006783; P:heme biosynthetic process
GO   GO:0006779; P:porphyrin-containing compound biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: CPFC_LISMO (Q8Y565)
FT   BINDING         182
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT   Condition: H
FT   BINDING         263
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT   Condition: E
case <OC:Bacillota> or <OC:Actinomycetota>
FT   BINDING         45..46
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT   Optional; Condition: R-Y
FT   BINDING         12
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Optional; Condition: Y
FT   BINDING         29
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT   Optional; Condition: R
FT   BINDING         53
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT   Optional; Condition: S
FT   BINDING         124
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT   Optional; Condition: Y
end case
XX
Size: 303-391;
Related: None;
Template: P32396; P23871; Q8Y565;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACCR, SHEON
Plasmid: None
Comments: None
XX
# Revision 1.48 2023/06/01
//