AC   MF_00825;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00825; -; 1; level=0
XX
Names: 3_HAO
XX
ID   3HAO
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase;
DE            EC=1.13.11.6;
DE   AltName: Full=3-hydroxyanthranilate oxygenase;
DE            Short=3-HAO;
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase;
DE            Short=HAD;
GN   Name=nbaC;
XX
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate
CC       to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes
CC       to quinolinate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate
CC         6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6;
case <FTGroup:1> and <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 2 Fe(2+) ions per subunit.;
else case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
end case
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 3/3.
case <OC:Pseudomonadota>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SIMILARITY: Belongs to the 3-HAO family.
XX
DR   Pfam; PF06052; 3-HAO; 1; trigger=no
DR   NCBIfam; TIGR03037; Anthran_nbaC; 1; trigger=no
XX
KW   Dioxygenase
KW   Oxidoreductase
KW   Pyridine nucleotide biosynthesis
case <FTGroup:1> or <FTGroup:2>
KW   Iron
KW   Metal-binding
end case
XX
GO   GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity
GO   GO:0008198; F:ferrous iron binding
GO   GO:0006569; P:tryptophan catabolic process
GO   GO:0019805; P:quinolinate biosynthetic process
GO   GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan
GO   GO:0043420; P:anthranilate metabolic process
XX
FT   From: 3HAO_CUPMC (Q1LCS4)
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         57
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         47
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT   Condition: R
FT   BINDING         57
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         99
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         110
FT                   /ligand="substrate"
FT   Condition: E
XX
Size: 174-189;
Related: None;
Template: Q1LCS4; Q83V26;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in CUPMC
Comments: None
XX
# Revision 1.22 2023/06/01
//