(data stored in ACNUC7421 zone)

SWISSPROT: KYNU_ASHGO

ID   KYNU_ASHGO              Reviewed;         447 AA.
AC   Q750P5;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 91.
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=AGL098W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 175; 263 AND 273.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016820; AAS54393.2; -; Genomic_DNA.
DR   RefSeq; NP_986569.2; NM_211631.2.
DR   SMR; Q750P5; -.
DR   STRING; 33169.AAS54393; -.
DR   PRIDE; Q750P5; -.
DR   EnsemblFungi; AAS54393; AAS54393; AGOS_AGL098W.
DR   GeneID; 4622868; -.
DR   KEGG; ago:AGOS_AGL098W; -.
DR   HOGENOM; HOG000242438; -.
DR   InParanoid; Q750P5; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; Q750P5.
DR   SWISS-2DPAGE; Q750P5.
KW   Cytoplasm; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Kynureninase"
FT                   /id="PRO_0000218661"
FT   REGION          134..137
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         106
FT                   /note="Pyridoxal phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         107
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         220
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         223
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         245
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         275
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   BINDING         303
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03017"
SQ   SEQUENCE   447 AA;  49032 MW;  8B39CBFF1EA2AC8A CRC64;
     MEKARALEEQ WPGARDAFHV PSYASLGLGD QTAAVRYLCG HSLGCMPRKT RGSVEAELSA
     WSARAVEAHV RHPGGTEWVN TDLPLVPQMA RMVGASQQEV AVMGSLTANL NALLVAFYRP
     RGRRTKILLE KQVFPSDFHA FWNQAALHGL DPAATLVQVA PRAGEHTLRT EDIVAAIETH
     RAELALVCLP GVQYYTGQLL DMASIVAAAR REPSIVVGFD LAHAVGNVQL QLHEWGADFA
     CWCSYKYLNA GPGGIAGLFV HERHHGGTLP RLAGWWGTNA ATRFEMRQTY DPLPDALGFR
     QSNPSVLDVA ALRASLEVFE DFGGMERVRA RSLALTGYLY ELLTQSVFYR PEVGADGVGF
     TILTPANPAE RGAQLSLLFW PHSDDPDKNT MPRVFADLRQ NGVLGDERHP DVIRLTPCAL
     YNTFMEVFES VQLLNAALER LAPESAV
//

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