HAMAP rule MF_00825
General rule information
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Accession | MF_00825 |
Dates | 21-JUN-2006 (Created)
1-JUN-2023 (Last updated, Version 22) |
Name | 3_HAO |
Scope(s) |
Bacteria |
Template(s) | Q1LCS4 (3HAO_CUPMC); Q83V26 (3HAO_PSEFL); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00825 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | 3HAO |
Protein name | RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase; EC=1.13.11.6; AltName: Full=3-hydroxyanthranilate oxygenase; Short=3-HAO; AltName: Full=3-hydroxyanthranilic acid dioxygenase; Short=HAD; |
Gene name | Name=nbaC; |
Comments
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FUNCTION | Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. |
CATALYTIC ACTIVITY | Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379, ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6; |
case <FTGroup:1> and <FTGroup:2> | |
COFACTOR | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 2 Fe(2+) ions per subunit.; |
else case <FTGroup:1> or <FTGroup:2> | |
COFACTOR | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; |
end case | |
PATHWAY | Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. |
case <OC:Pseudomonadota> | |
SUBUNIT | Homodimer. |
end case | |
SIMILARITY | Belongs to the 3-HAO family. |
Keywords
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Dioxygenase | |
Oxidoreductase | |
Pyridine nucleotide biosynthesis | |
case <FTGroup:1> or <FTGroup:2> | |
Iron | |
Metal-binding | |
end case |
Gene Ontology
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GO:0000334; Molecular function:3-hydroxyanthranilate 3,4-dioxygenase activity |
GO:0008198; Molecular function:ferrous iron binding |
GO:0006569; Biological process:tryptophan catabolic process |
GO:0019805; Biological process:quinolinate biosynthetic process |
GO:0034354; Biological process:'de novo' NAD biosynthetic process from tryptophan |
GO:0043420; Biological process:anthranilate metabolic process |
Cross-references
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Features
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From: 3HAO_CUPMC (Q1LCS4) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 51 | 51 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="1" /ligand_note="catalytic" |
H | 1 | |||||||
BINDING | 57 | 57 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="1" /ligand_note="catalytic" |
E | 1 | |||||||
BINDING | 95 | 95 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="1" /ligand_note="catalytic" |
H | 1 | |||||||
BINDING | 125 | 125 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="2" |
C | 2 | |||||||
BINDING | 128 | 128 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="2" |
C | 2 | |||||||
BINDING | 162 | 162 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="2" |
C | 2 | |||||||
BINDING | 165 | 165 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_label="2" |
C | 2 | |||||||
BINDING | 47 | 47 | /ligand="O2" /ligand_id="ChEBI:CHEBI:15379" |
R | ||||||||
BINDING | 57 | 57 | /ligand="substrate" | E | ||||||||
BINDING | 99 | 99 | /ligand="substrate" | R | ||||||||
BINDING | 110 | 110 | /ligand="substrate" | E |
Additional information
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Size range | 174-189 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |