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HAMAP rule MF_03017

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General rule information [?]

Accession MF_03017
Dates 12-FEB-2009 (Created)
1-JUN-2023 (Last updated, Version 17)
Name Kynureninase_euk
Scope(s) Eukaryota
Template(s) Q16719 (KYNU_HUMAN); P70712 (KYNU_RAT); Q05979 (KYNU_YEAST); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_01970 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KYNU
case <OC:Fungi>
Protein name RecName: Full=Kynureninase;
AltName: Full=Biosynthesis of nicotinic acid protein 5;
AltName: Full=L-kynurenine hydrolase;
Protein name RecName: Full=Kynureninase;
AltName: Full=L-kynurenine hydrolase;
end case
case <OC:Dictyostelium>
Gene name Name=kynu;
else case <OC:Fungi>
Gene name Name=BNA5;
else case <OC:Eukaryota> and not <OC:Arthropoda> and not <OC:Nematoda> and not <OC:Platyhelminthes>
Gene name Name=KYNU;
end case

Comments [?]

case <OC:Mammalia>
FUNCTIONCatalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
FUNCTIONCatalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.
end case
CATALYTIC ACTIVITY Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine; Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=;
CATALYTIC ACTIVITY Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972, ChEBI:CHEBI:58125;
case <FTTag:PLP>
COFACTOR Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
end case
PATHWAYAmino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
PATHWAYCofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
SIMILARITYBelongs to the kynureninase family.

Keywords [?]

case <FTTag:acetyl>
end case
Pyridine nucleotide biosynthesis
case <FTTag:PLP>
Pyridoxal phosphate
end case

Gene Ontology [?]

GO:0030170; Molecular function:pyridoxal phosphate binding
GO:0030429; Molecular function:kynureninase activity
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
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00266; Aminotran_5; 1;
NCBIfam TIGR01814; Kynureninase; 1;

Features [?]

From: KYNU_HUMAN (Q16719)
Key From To Description Tag Condition FTGroup
case <OC:Vertebrata>
MOD_RES 1 1 /note="N-acetylmethionine" acetyl M
end case
BINDING 165 168 /ligand="pyridoxal 5'-phosphate"
BINDING 137 137 /ligand="pyridoxal 5'-phosphate"
BINDING 138 138 /ligand="pyridoxal 5'-phosphate"
BINDING 221 221 /ligand="pyridoxal 5'-phosphate"
BINDING 250 250 /ligand="pyridoxal 5'-phosphate"
BINDING 253 253 /ligand="pyridoxal 5'-phosphate"
BINDING 275 275 /ligand="pyridoxal 5'-phosphate"
MOD_RES 276 276 /note="N6-(pyridoxal phosphate)lysine" PLP K
BINDING 305 305 /ligand="pyridoxal 5'-phosphate"
BINDING 333 333 /ligand="pyridoxal 5'-phosphate"

Additional information [?]

Size range 396-539 amino acids
Related rules None
Fusion Nter: None Cter: None

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