AC   MF_01970;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01970; -; 1; level=0
XX
Names: Kynureninase
XX
ID   KYNU
DE   RecName: Full=Kynureninase;
DE            EC=3.7.1.3;
DE   AltName: Full=L-kynurenine hydrolase;
GN   Name=kynU;
XX
CC   -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
CC       hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
CC       hydroxyanthranilic acid (3-OHAA), respectively.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC         Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=3.7.1.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) +
CC         L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:58125;
case <FTTag:PLP>
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
end case
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC       and anthranilate from L-kynurenine: step 1/1.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 2/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
XX
DR   Pfam; PF00266; Aminotran_5; 1; trigger=no
DR   PIRSF; PIRSF038800; KYNU; 1; trigger=no
DR   NCBIfam; TIGR01814; Kynureninase; 1; trigger=no
XX
KW   Hydrolase
KW   Pyridine nucleotide biosynthesis
case <FTTag:PLP>
KW   Pyridoxal phosphate
end case
XX
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0030429; F:kynureninase activity
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: KYNU_PSEFL (P83788)
FT   BINDING         129..132
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: F-P-[ST]-D
FT   BINDING         97
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [TIL]
FT   BINDING         98
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [ST]
FT   BINDING         172
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: T
FT   BINDING         201
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: D
FT   BINDING         204
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: H
FT   BINDING         226
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Tag: PLP; Condition: K
FT   BINDING         256
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: W
FT   BINDING         282
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [TN]
XX
Size: 410-539;
Related: None;
Template: P83788;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.13 2023/06/01
//