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KYNU_CRYNB
ID   KYNU_CRYNB              Reviewed;         453 AA.
AC   P0CO53; Q55W17; Q5KK77;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
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}; OrderedLocusNames=CNBC3200;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000013; EAL22182.1; -; Genomic_DNA.
DR   RefSeq; XP_776829.1; XM_771736.1.
DR   AlphaFoldDB; P0CO53; -.
DR   SMR; P0CO53; -.
DR   PRIDE; P0CO53; -.
DR   EnsemblFungi; EAL22182; EAL22182; CNBC3200.
DR   GeneID; 4934985; -.
DR   KEGG; cnb:CNBC3200; -.
DR   VEuPathDB; FungiDB:CNBC3200; -.
DR   HOGENOM; CLU_003433_4_0_1; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001435; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
DR   GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..453
FT                   /note="Kynureninase"
FT                   /id="PRO_0000410131"
FT   BINDING         114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         115
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         142..145
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         232
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         257
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         286
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
SQ   SEQUENCE   453 AA;  51170 MW;  36FC6C0CDDB4A102 CRC64;
     MSNDLPTKKD LVKWDQEDAL NWTRGEYEIP NSKACGGEAD GKAIYFCGNS LGLLNKKARQ
     HIMEELDVWS TSSVTGHFNH PYQRPWKHVD EPLTPHLAKL VGAREEEVAH TSTLTSNMHN
     LFTSFYQPTE KRWKIVIEKG SFPSDWYAVH SHPRLHDKVL RPEQIDNAII ALVPREGEDT
     LRTEDILKVL DDNKDSIAIV WLPLVQYYTG QLFDISSISP KVHEIGALLG LDMAHGIGNV
     ECKLNEWNVD FAVWCTYKYL NAGPAAIGGF YIRSGLEDGG RRLAGWWGND ARTRFHMSPN
     FQPTPGAKGY QHSCTPVFSS IPLLATLQLI EAVGFSNMVE KARRLTGTLE ALLKASRYYV
     HPADPKGKIG FKIITPAAPY RGTQLSLVIL PEEEHVMPKV FDRMLRKGLV GDERKPSVIR
     LSPVVLYNTF EEVGRAVEIV EEALEEEEEE RKR
 
 
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