HAMAP rule MF_03017
General rule information
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| Accession | MF_03017 |
| Dates | 12-FEB-2009 (Created)
23-MAY-2024 (Last updated, Version 18) |
| 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
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Identifier, protein and gene names
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| Identifier | KYNU |
| case <OC:Fungi> | |
| Protein name | RecName: Full=Kynureninase; EC=3.7.1.3; AltName: Full=Biosynthesis of nicotinic acid protein 5; AltName: Full=L-kynurenine hydrolase; |
| else | |
| Protein name | RecName: Full=Kynureninase; EC=3.7.1.3; 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
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| case <OC:Mammalia> | |
| 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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. |
| else | |
| 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. |
| 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=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. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the kynureninase family. |
Keywords
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| case <FTTag:acetyl> | |
| Acetylation | |
| end case | |
| Cytoplasm | |
| 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:0006569; Biological process:tryptophan catabolic process |
| 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 |
| GO:0043420; Biological process:anthranilate metabolic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| 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" /ligand_id="ChEBI:CHEBI:597326" |
F-P-S-D | ||||||||
| BINDING | 137 | 137 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
L | ||||||||
| BINDING | 138 | 138 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
[ST] | ||||||||
| BINDING | 221 | 221 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
S | ||||||||
| BINDING | 250 | 250 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
D | ||||||||
| BINDING | 253 | 253 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
H | ||||||||
| BINDING | 275 | 275 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
Y | ||||||||
| MOD_RES | 276 | 276 | /note="N6-(pyridoxal phosphate)lysine" | PLP | K | |||||||
| BINDING | 305 | 305 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
W | ||||||||
| BINDING | 333 | 333 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
[TN] | ||||||||
Additional information
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| Size range | 396-539 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |