HAMAP rule MF_01272
General rule information
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| Accession | MF_01272 |
| Dates | 6-NOV-2006 (Created)
13-JAN-2023 (Last updated, Version 23) |
| Name | Heme_degrading_monooxygenase |
| Scope(s) |
Bacteria Bacillota |
| Template(s) | Q8NX62 (HDOX1_STAAW); Q2FZE2 (HDOX1_STAA8); Q2G1J2 (HDOX2_STAA8); Q99X56 (HDOX2_STAAM); Q81L50 (HDOX_BACAN); [ Recover all ] |
| Triggered by |
HAMAP; MF_01272 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HDOX |
| case <OC:Staphylococcus> | |
| Protein name | RecName: Full=Heme oxygenase (staphylobilin-producing); EC=1.14.99.48; AltName: Full=Heme-degrading monooxygenase; AltName: Full=Iron-regulated surface determinant; AltName: Full=Iron-responsive surface determinant; |
| else | |
| Protein name | RecName: Full=Heme-degrading monooxygenase; EC=1.14.14.18; AltName: Full=Heme oxygenase; AltName: Full=Iron-regulated surface determinant; AltName: Full=Iron-responsive surface determinant; |
| Gene name | Name=isdG; |
| end case | |
Comments
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| case <OC:Staphylococcus> | |
| FUNCTION | Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo- beta-bilirubin) in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. |
| CATALYTIC ACTIVITY | Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin + Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37039, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74361; EC=1.14.99.48; |
| CATALYTIC ACTIVITY | Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin + Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37363, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74362; EC=1.14.99.48; |
| else | |
| FUNCTION | Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. |
| CATALYTIC ACTIVITY | Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH-- hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; |
| end case | |
| SUBUNIT | Homodimer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily. |
Keywords
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Gene Ontology
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| GO:0005506; Molecular function:iron ion binding |
| GO:0004392; Molecular function:heme oxygenase (decyclizing) activity |
| GO:0016705; Molecular function:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| GO:0020037; Molecular function:heme binding |
| GO:0005737; Cellular component:cytoplasm |
| GO:0042167; Biological process:heme catabolic process |
Cross-references
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Features
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| From: HDOX2_STAAN (Q7A827) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 21 | 28 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" |
R-F-Y-x-R-x-G-I | ||||||||
| BINDING | 6 | 6 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
N | ||||||||
| BINDING | 76 | 76 | /ligand="heme" /ligand_id="ChEBI:CHEBI:30413" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| SITE | 66 | 66 | /note="Transition state stabilizer" | |||||||||
Additional information
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| Size range | 100-121 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Most Staphylococcus aureus strains have two family members; the second one is called isdI. |