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Database: UniProt/SWISS-PROT
Entry: KYNU_DEIRA
LinkDB: KYNU_DEIRA
Original site: KYNU_DEIRA 
ID   KYNU_DEIRA              Reviewed;         410 AA.
AC   Q9RYH5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   30-AUG-2017, entry version 107.
DE   RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_01970};
DE            EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_01970};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000255|HAMAP-Rule:MF_01970};
GN   OrderedLocusNames=DR_A0338;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(1999).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_01970}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
DR   EMBL; AE001825; AAF12444.1; -; Genomic_DNA.
DR   PIR; F75588; F75588.
DR   RefSeq; NP_285661.1; NC_001264.1.
DR   ProteinModelPortal; Q9RYH5; -.
DR   SMR; Q9RYH5; -.
DR   STRING; 243230.DR_A0338; -.
DR   EnsemblBacteria; AAF12444; AAF12444; DR_A0338.
DR   GeneID; 1799657; -.
DR   KEGG; dra:DR_A0338; -.
DR   PATRIC; fig|243230.17.peg.3230; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242437; -.
DR   InParanoid; Q9RYH5; -.
DR   KO; K01556; -.
DR   OMA; VCSLHAS; -.
DR   OrthoDB; POG091H0D63; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000002524; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030429; F:kynureninase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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   Complete proteome; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    410       Kynureninase.
FT                                /FTId=PRO_0000357003.
FT   REGION      135    138       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     108    108       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     109    109       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     176    176       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     205    205       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     208    208       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     230    230       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     260    260       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     286    286       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     231    231       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   410 AA;  43890 MW;  50177666F0EA98F0 CRC64;
     MTTLLPALDL AQLDALDARD PLAHKRAEFD LPGDIIYLDG NSLGALPRRV PARLSQVATE
     EWGHHLIRSW TRNAEAAQDW MALPDRVAAK LAPLLGAGAH EVAVGDSTSV NTFKALAAAL
     RLSGRRVILS DADNFPTDLY VAQGLARLLG DVEVRTAPGD EMTQHFTDDV GVVLLTEVDY
     RTGRRLDMRA ITAAAHARGI VTVWDLAHSA GAFAVDLGGA GADFAIGCGY KFLNGGPGAP
     AFLYVAERHL DRAEVVLSGW MGHADPFEMA RAYAPAPGAR RFVVGTPQVL SLSALDAALD
     VFGDVDLGAL REKSLSLTDT FIRLMEPLAE QYPLELVTPL AHAERGSQVS YRHPHAQQVM
     AQLIECGIVG DFRTPDILRF GFTPLYLSHG DVGRAVAGIA AVLDELEGPA
//
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