KYNU_CAEEL
ID KYNU_CAEEL Reviewed; 478 AA.
AC Q18026;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_03017};
DE EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_03017};
DE AltName: Full=Abnormal fluorescence under UV illumination;
DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017};
GN Name=flu-2; ORFNames=C15H9.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=6936603; DOI=10.1007/bf00268072;
RA Bhat S.G., Babu P.;
RT "Mutagen sensitivity of kynureninase mutants of the nematode Caenorhabditis
RT elegans.";
RL Mol. Gen. Genet. 180:635-638(1980).
CC -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
CC hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
CC hydroxyanthranilic acid (3-OHAA), respectively. {ECO:0000255|HAMAP-
CC Rule:MF_03017, ECO:0000269|PubMed:6936603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=3.7.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) +
CC L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:58125; EC=3.7.1.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03017};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03017};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC and anthranilate from L-kynurenine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03017}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_03017}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03017}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03017}.
CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP-
CC Rule:MF_03017}.
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DR EMBL; FO080555; CCD64633.1; -; Genomic_DNA.
DR EMBL; AF303267; AAG50225.1; -; mRNA.
DR PIR; T15516; T15516.
DR RefSeq; NP_509023.1; NM_076622.4.
DR AlphaFoldDB; Q18026; -.
DR SMR; Q18026; -.
DR BioGRID; 45815; 1.
DR IntAct; Q18026; 1.
DR STRING; 6239.C15H9.7; -.
DR EPD; Q18026; -.
DR PaxDb; Q18026; -.
DR PeptideAtlas; Q18026; -.
DR EnsemblMetazoa; C15H9.7.1; C15H9.7.1; WBGene00015802.
DR GeneID; 180883; -.
DR KEGG; cel:CELE_C15H9.7; -.
DR UCSC; C15H9.7; c. elegans.
DR CTD; 180883; -.
DR WormBase; C15H9.7; CE06835; WBGene00015802; flu-2.
DR eggNOG; KOG3846; Eukaryota.
DR GeneTree; ENSGT00390000008033; -.
DR HOGENOM; CLU_003433_4_0_1; -.
DR InParanoid; Q18026; -.
DR OMA; TFPTDGY; -.
DR OrthoDB; 916879at2759; -.
DR PhylomeDB; Q18026; -.
DR Reactome; R-CEL-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR PRO; PR:Q18026; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015802; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
DR GO; GO:0030429; F:kynureninase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IBA:GO_Central.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01970; Kynureninase; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010111; Kynureninase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR14084; PTHR14084; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF038800; KYNU; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01814; kynureninase; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..478
FT /note="Kynureninase"
FT /id="PRO_0000218660"
FT BINDING 150
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 151
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 178..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 288
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 346
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT MOD_RES 289
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
SQ SEQUENCE 478 AA; 54050 MW; E889450929EC94BD CRC64;
MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD ALKEIRDLFH
YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM KDHLDKWAKM GVFGHMSGEV
PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL TVNIHVLLTS FYKPTETRHK ILLESKAFPS
DHYAIESQIR LKGRTVQDSM VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT
GQLFDMRAIT EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG
LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH TVAAMLGSLK
VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL SISIITPEEF HQRGCQLSLK
FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA PVHLYNNYVD IRRFISVLQE VAHIVESE
