KYNU_YARLI
ID KYNU_YARLI Reviewed; 437 AA.
AC Q6CDM0;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Biosynthesis of nicotinic acid protein 5 {ECO:0000255|HAMAP-Rule:MF_03017};
DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017};
GN Name=BNA5 {ECO:0000255|HAMAP-Rule:MF_03017};
GN OrderedLocusNames=YALI0B22902g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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; CR382128; CAG83495.1; -; Genomic_DNA.
DR RefSeq; XP_501242.1; XM_501242.1.
DR AlphaFoldDB; Q6CDM0; -.
DR SMR; Q6CDM0; -.
DR STRING; 4952.CAG83495; -.
DR PRIDE; Q6CDM0; -.
DR EnsemblFungi; CAG83495; CAG83495; YALI0_B22902g.
DR GeneID; 2906903; -.
DR KEGG; yli:YALI0B22902g; -.
DR VEuPathDB; FungiDB:YALI0_B22902g; -.
DR HOGENOM; CLU_003433_4_0_1; -.
DR InParanoid; Q6CDM0; -.
DR OMA; TFPTDGY; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000001300; Chromosome B.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..437
FT /note="Kynureninase"
FT /id="PRO_0000218664"
FT BINDING 99
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 100
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 127..130
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 215
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT BINDING 295
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
SQ SEQUENCE 437 AA; 48411 MW; 903018CA6020F2CA CRC64;
MPLNFRDRFN VPVLKNGEEV AYLVGNSLGL MPHKTRDYVN QEMDAWSQLG VKGHFVSGKE
DLGQDVHQGP WYSCDEPLHG LVGPILGASE DEVAIMNTLT SNIHSLFSAF YKPTAKRSKI
LFEAKAFPSD TYAMEAQARL HNLDPSEALI KLAPKDGLHT LSDDDIIKVI EEQGDEIAVV
FFSGIQFYTG QLFDIPRITA AAKAKGCVVG WDLAHAAGNV PLKLHDWNVD FAVFCTYKYM
NSGPGGIGGL FVHDKYADDQ RPRLAGWWGN NAETRFKMLD EFDPIRGARG YKQSNPSVLC
VLALRASLEL FKEAGGIEKL RERSIELTNR LLKGLLASPH YIAPENIEIF GNSGKAWFTI
ITPQAEHQRG AQLSLLFGPD GTMKKVFDYL DDHGVLGDER NPDVIRLAPA PLYNNERDVD
LAIKLINDSI NLINGSA
