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Database: UniProt/SWISS-PROT
Entry: KYNU_MYXXD
LinkDB: KYNU_MYXXD
Original site: KYNU_MYXXD 
ID   KYNU_MYXXD              Reviewed;         426 AA.
AC   Q1DDU5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   07-NOV-2018, entry version 79.
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=MXAN_0917;
OS   Myxococcus xanthus (strain DK 1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK 1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF87345.1; -; Genomic_DNA.
DR   RefSeq; WP_011551038.1; NC_008095.1.
DR   ProteinModelPortal; Q1DDU5; -.
DR   SMR; Q1DDU5; -.
DR   STRING; 246197.MXAN_0917; -.
DR   PRIDE; Q1DDU5; -.
DR   EnsemblBacteria; ABF87345; ABF87345; MXAN_0917.
DR   KEGG; mxa:MXAN_0917; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242438; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   OrthoDB; POG091H0D63; -.
DR   BioCyc; MXAN246197:G1G53-892-MONOMER; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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;
KW   Complete proteome; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    426       Kynureninase.
FT                                /FTId=PRO_0000357009.
FT   REGION      138    141       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     110    110       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     111    111       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     223    223       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     226    226       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     248    248       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     279    279       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     307    307       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     249    249       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   426 AA;  47760 MW;  9F8B6DCA33680072 CRC64;
     MTTPYLFEDS ESFARKLDAE DALRGYRDAF HFPPGPDGKP VVYLAGNSLG LQPRNAARYI
     QEELEDWARL GVEGHHHGRH PWLHYHELVT EHAARLVGAK PLEVVVMNTL SVNLHLMMVS
     FYRPTKQRFK ILVEAGAFPS DQYAVASQVR FHGYDAREAV LELKPREGEE TLRTEDILET
     IERHGHEVAL VMLGSVNYLT GQAFDLAAIT KAAHAKGCFV GFDLAHGAGN LRLSLHDDGP
     DFAVWCSYKY LNAGPGALGG VFVHERHAHT KDLPRFEGWW GHDKQTRFQM GPTFSALPGA
     EGWQLSNPPI FQLAALRASL ELFDQAGMAA LRAKSERLTG YLEFLLDRLP EGFVRITTPR
     DVKQRGAQLS LRFRGEPQGL LKRLGDAGII CDFRKPDIIR AAPAPLYNSF TDVYRFVKTL
     EGHARE
//
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