HAMAP rule MF_01970
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
[?]
FUNCTION | Catalyzes 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 | |
PATHWAY | Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. |
PATHWAY | Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. |
SUBUNIT | Homodimer. |
SIMILARITY | Belongs to the kynureninase family. |
Keywords
[?]
Hydrolase | |
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: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 |