HAMAP rule MF_00825

General rule information [?]

Accession	MF_00825
Dates	21-JUN-2006 (Created) 26-JAN-2023 (Last updated, Version 21)

Name

3_HAO

Scope

Bacteria

Templates

Q1LCS4 (3HAO_CUPMC); Q83V26 (3HAO_PSEFL): [Recover all]

case <OC:Bacteria>

Triggered by

HAMAP; MF_00825 (Get profile general information and statistics)

end case

Propagated annotation [?]

Identifier, protein and gene names [?]

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

nbaC

Comments [?]

Function	Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic activity	RHEA:17953: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde EC 1.13.11.6

case <FTGroup:1> and <FTGroup:2>

Cofactor

Fe(2+)
Note: Binds 2 Fe(2+) ions per subunit.

else case <FTGroup:1> or <FTGroup:2>

Cofactor

Fe(2+)

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 [?]

Dioxygenase
Oxidoreductase
Pyridine nucleotide biosynthesis

case <FTGroup:1> or <FTGroup:2>

Iron
Metal-binding

end case

Gene Ontology [?]

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 [?]

Pfam	PF06052; 3-HAO; 1;
TIGRFAMs	TIGR03037; Anthran_nbaC; 1;

Features [?]

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 [?]

Size range	174-189 amino acids
Related rules	None
Fusion	None

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