AC   MF_03017;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01970; -; 1; level=0
XX
Names: Kynureninase_euk
XX
ID   KYNU
case <OC:Fungi>
DE   RecName: Full=Kynureninase;
DE            EC=3.7.1.3;
DE   AltName: Full=Biosynthesis of nicotinic acid protein 5;
DE   AltName: Full=L-kynurenine hydrolase;
else
DE   RecName: Full=Kynureninase;
DE            EC=3.7.1.3;
DE   AltName: Full=L-kynurenine hydrolase;
end case
case <OC:Dictyostelium>
GN   Name=kynu;
else case <OC:Fungi>
GN   Name=BNA5;
else case <OC:Eukaryota> and not <OC:Arthropoda> and not <OC:Nematoda> and not <OC:Platyhelminthes>
GN   Name=KYNU;
end case
XX
case <OC:Mammalia>
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. Has a preference for
CC       the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
else
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.
end case
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
XX
DR   Pfam; PF00266; Aminotran_5; 1; trigger=no
DR   NCBIfam; TIGR01814; Kynureninase; 1; trigger=no
XX
case <FTTag:acetyl>
KW   Acetylation
end case
KW   Cytoplasm
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
GO   GO:0005737; C:cytoplasm
XX
FT   From: KYNU_HUMAN (Q16719)
case <OC:Vertebrata>
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT   Tag: acetyl; Condition: M
end case
FT   BINDING         165..168
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: F-P-S-D
FT   BINDING         137
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: L
FT   BINDING         138
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [ST]
FT   BINDING         221
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: S
FT   BINDING         250
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: D
FT   BINDING         253
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: H
FT   BINDING         275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Tag: PLP; Condition: K
FT   BINDING         305
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: W
FT   BINDING         333
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: [TN]
XX
Size: 396-539;
Related: None;
Template: Q16719; P70712; Q05979;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ASPCL, ASPFC, ASPFU, ASPNC, ASPOR, ASPTN, CHAGB, EMENI, NEOFI,
 NEUCR, PHANO
Plasmid: None
Comments: None
XX
# Revision 1.17 2023/06/01
//