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HAMAP rule MF_01970

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General rule information [?]

Accession MF_01970
Dates 12-FEB-2009 (Created)
14-MAY-2024 (Last updated, Version 14)
Name Kynureninase
Scope(s) Bacteria
Template(s) P83788 (KYNU_PSEFL); [ Recover all ]
Triggered by
case c? <OC:Bacteria>
HAMAP; MF_01970 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KYNU
Protein name RecName: Full=Kynureninase;
                 EC=3.7.1.3;
AltName: Full=L-kynurenine hydrolase;
Gene name Name=kynU;

Comments [?]

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.
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=3.7.1.3;
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.
SUBUNITHomodimer.
SIMILARITYBelongs to the kynureninase family.

Keywords [?]


Gene Ontology [?]

GO:0030170; Molecular function:pyridoxal phosphate binding
GO:0030429; Molecular function:kynureninase activity
GO:0097053; Biological process:L-kynurenine catabolic process
GO:0019805; Biological process:quinolinate biosynthetic process
GO:0034354; Biological process:'de novo' NAD biosynthetic process from tryptophan

Cross-references [?]

Pfam PF00266; Aminotran_5; 1;
PIRSF PIRSF038800; KYNU; 1;
NCBIfam TIGR01814; Kynureninase; 1;

Features [?]

From: KYNU_PSEFL (P83788)
Key From To Description Tag Condition FTGroup
BINDING 129 132 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
F-P-[ST]-D
BINDING 97 97 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
[TIL]
BINDING 98 98 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
[ST]
BINDING 172 172 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
T
BINDING 201 201 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
D
BINDING 204 204 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
H
BINDING 226 226 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
Y
MOD_RES 227 227 /note="N6-(pyridoxal phosphate)lysine" PLP K
BINDING 256 256 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
W
BINDING 282 282 /ligand="pyridoxal 5'-phosphate"
/ligand_id="ChEBI:CHEBI:597326"
[TN]

Additional information [?]

Size range 410-539 amino acids
Related rules None
Fusion Nter: None Cter: None



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