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HAMAP rule MF_03019

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General rule information [?]

Accession MF_03019
Dates 12-FEB-2009 (Created)
1-JUN-2023 (Last updated, Version 15)
Name 3_HAO_euk
Scope
Eukaryota
Templates Q0VCA8 (3HAO_BOVIN); Q78JT3 (3HAO_MOUSE); Q54S02 (3HAO_DICDI); P46952 (3HAO_HUMAN); P47096 (3HAO_YEAST): [Recover all]
case <OC:Eukaryota>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
3HAO
case <OC:Fungi>
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;
AltName: Full=Biosynthesis of nicotinic acid protein 1;
else
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;
end case
case <OC:Vertebrata>
Gene name
HAAO
else case <OC:Fungi>
Gene name
BNA1
end case

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> or <FTGroup:2>
Cofactor Fe(2+)
end case
Pathway Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
case <OC:Vertebrata>
Subunit Monomer.
end case
Subcellular location Cytoplasm.
Similarity Belongs to the 3-HAO family.

Keywords [?]

Dioxygenase
Oxidoreductase
Pyridine nucleotide biosynthesis
case <OC:Eukaryota>
Cytoplasm
end case
case <FTGroup:1> or <FTGroup:2>
Iron
end case
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
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.
case <OC:Eukaryota>
GO:0005737; Cellular component: cytoplasm.
end case

Cross-references [?]

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

Features [?]

case <OC:Metazoa>
From: 3HAO_BOVIN (Q0VCA8)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     Nter     160       Domain A (catalytic)        
REGION     161     177       Linker        
REGION     178     Cter       Domain B        
BINDING     47     47       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     H   1
BINDING     53     53       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     E   1
BINDING     91     91       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     H   1
BINDING     43     43       /ligand="O2" /ligand_id="ChEBI:CHEBI:15379     R  
BINDING     53     53       /ligand="substrate     E  
BINDING     95     95       /ligand="substrate     R  
BINDING     105     105       /ligand="substrate     E  
end case
case <OC:Fungi>
From: 3HAO_YEAST (P47096)
BINDING     49     49       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     H   2
BINDING     55     55       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     E   2
BINDING     97     97       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" /ligand_note="catalytic     H   2
BINDING     126     126       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240     C   3
BINDING     129     129       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240     C   3
BINDING     163     163       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240     C   3
BINDING     166     166       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240     C   3
BINDING     45     45       /ligand="O2" /ligand_id="ChEBI:CHEBI:15379     R  
BINDING     55     55       /ligand="substrate     E  
BINDING     101     101       /ligand="substrate     R  
BINDING     111     111       /ligand="substrate     E  
end case

Additional information [?]

Size range 160-288 amino acids
Related rules None
Fusion None


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