HAMAP rule MF_01970
General rule information
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| 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
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Identifier, protein and gene names
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| Identifier | KYNU |
| Protein name | RecName: Full=Kynureninase; EC=3.7.1.3; AltName: Full=L-kynurenine hydrolase; |
| Gene name | Name=kynU; |
Comments
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| 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
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| Hydrolase | |
| Pyridine nucleotide biosynthesis | |
| case <FTTag:PLP> | |
| Pyridoxal phosphate | |
| end case | |
Gene Ontology
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| 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
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| Pfam | PF00266; Aminotran_5; 1; |
| PIRSF | PIRSF038800; KYNU; 1; |
| NCBIfam | TIGR01814; Kynureninase; 1; |
Features
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| 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
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| Size range | 410-539 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |