AC   MF_01272;
DC   Protein; auto
TR   HAMAP; MF_01272; -; 1; level=0
XX
Names: Heme_degrading_monooxygenase
XX
ID   HDOX
case <OC:Staphylococcus>
DE   RecName: Full=Heme oxygenase (staphylobilin-producing);
DE            EC=1.14.99.48;
DE   AltName: Full=Heme-degrading monooxygenase;
DE   AltName: Full=Iron-regulated surface determinant;
DE   AltName: Full=Iron-responsive surface determinant;
else
DE   RecName: Full=Heme-degrading monooxygenase;
DE            EC=1.14.14.18;
DE   AltName: Full=Heme oxygenase;
DE   AltName: Full=Iron-regulated surface determinant;
DE   AltName: Full=Iron-responsive surface determinant;
GN   Name=isdG;
end case
XX
case <OC:Staphylococcus>
CC   -!- FUNCTION: Allows bacterial pathogens to use the host heme as an iron
CC       source. Catalyzes the oxidative degradation of the heme macrocyclic
CC       porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a
CC       mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-
CC       beta-bilirubin) in the presence of a suitable electron donor such as
CC       ascorbate or NADPH--cytochrome P450 reductase, with subsequent release
CC       of free iron.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin +
CC         Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37039,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74361;
CC         EC=1.14.99.48;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin +
CC         Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37363,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74362;
CC         EC=1.14.99.48;
else
CC   -!- FUNCTION: Allows bacterial pathogens to use the host heme as an iron
CC       source. Catalyzes the oxidative degradation of the heme macrocyclic
CC       porphyrin ring to the biliverdin in the presence of a suitable electron
CC       donor such as ascorbate or NADPH--cytochrome P450 reductase, with
CC       subsequent release of free iron.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. Heme-degrading monooxygenase IsdG subfamily.
XX
DR   PROSITE; PS51725; ABM; 1; trigger=yes
DR   Pfam; PF03992; ABM; 1; trigger=no
XX
KW   Cytoplasm
KW   Heme
KW   Iron
KW   Metal-binding
KW   Monooxygenase
KW   Oxidoreductase
XX
GO   GO:0005506; F:iron ion binding
GO   GO:0004392; F:heme oxygenase (decyclizing) activity
GO   GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO   GO:0020037; F:heme binding
GO   GO:0005737; C:cytoplasm
GO   GO:0042167; P:heme catabolic process
XX
FT   From: HDOX2_STAAN (Q7A827)
FT   BINDING         21..28
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT   Condition: R-F-Y-x-R-x-G-I
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: N
FT   BINDING         76
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Condition: H
FT   SITE            66
FT                   /note="Transition state stabilizer"
XX
Size: 100-121;
Related: None;
Template: Q8NX62; Q2FZE2; Q2G1J2; Q99X56; Q81L50;
Scope:
 Bacteria; Bacillota
Fusion:
 Nter: None
 Cter: None
Duplicate: in STAA3, STAA8, STAAC, STAAM, STAAN, STAAR, STAAS, STAAW
Plasmid: None
Comments: Most Staphylococcus aureus strains have two family members; the second one is called isdI.
XX
# Revision 1.23 2023/01/13
//