HAMAP rule MF_01970
General rule information
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Accession | MF_01970 |
Dates | 12-FEB-2009 (Created) 1-JUN-2023 (Last updated, Version 13) |
Name | Kynureninase |
Scope | Bacteria |
Template | P83788 (KYNU_PSEFL) |
case <OC:Bacteria>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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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 | RHEA:16813: H2O + L-kynurenine = anthranilate + H(+) + L-alanine
EC 3.7.1.3 |
RHEA:25143: 3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine |
case <FTTag:PLP>
Cofactor | pyridoxal 5'-phosphate |
end case
Pathway | Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. |
Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. | |
Subunit | Homodimer. |
Similarity | Belongs to the kynureninase family. |
Keywords
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case <FTTag:PLP>
end case
Gene Ontology
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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: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.
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 (Optional) | 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 | 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 | None |