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Annotation rule MF_00825
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General rule information [?]

Accession MF_00825
Dates 21-JUN-2006 (Created)
18-NOV-2019 (Last updated, Version 18)
Name 3_HAO
Scope
Bacteria
Templates Q1LCS4 (3HAO_CUPMC); Q83V26 (3HAO_PSEFL): [Recover all]
case <OC:Bacteria>
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:Proteobacteria>
Subunit Homodimer.
end case
Similarity Belongs to the 3-HAO family.

Keywords [?]

case <FTGroup:1> or <FTGroup:2>
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
METAL     51     51       Iron 1; catalytic     H   1
METAL     57     57       Iron 1; catalytic     E   1
METAL     95     95       Iron 1; catalytic     H   1
METAL     125     125       Iron 2     C   2
METAL     128     128       Iron 2     C   2
METAL     162     162       Iron 2     C   2
METAL     165     165       Iron 2     C   2
BINDING     47     47       Dioxygen     R  
BINDING     57     57       Substrate     E  
BINDING     99     99       Substrate     R  
BINDING     110     110       Substrate     E  

Additional information [?]

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