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Database: UniProt/SWISS-PROT
Entry: KYNU_XANCB
LinkDB: KYNU_XANCB
Original site: KYNU_XANCB 
ID   KYNU_XANCB              Reviewed;         424 AA.
AC   B0RUZ9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   05-DEC-2018, entry version 67.
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=xcc-b100_2707;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J.,
RA   Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A.,
RA   Niehaus K., Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use
RT   for the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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:
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;
CC         EC=3.7.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate +
CC         H(+) + 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_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; AM920689; CAP52068.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0RUZ9; -.
DR   SMR; B0RUZ9; -.
DR   EnsemblBacteria; CAP52068; CAP52068; xcc-b100_2707.
DR   KEGG; xca:xcc-b100_2707; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001188; 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    424       Kynureninase.
FT                                /FTId=PRO_0000357017.
FT   REGION      134    137       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     106    106       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     107    107       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     219    219       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     222    222       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     244    244       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     274    274       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     302    302       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     245    245       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   424 AA;  46170 MW;  AAB5C7D416B3C5AF CRC64;
     MMTDPLSRSH AAALDAADPL RALRDAFVFP QHGGQDQTYF VGNSLGLQPR QARAMVSEVL
     DQWGALAVEG HFTGPTQWLT YHQLVRDGLA RVVGAQPDEV VAMNTLTVNL HLMMASFYRP
     SAERAAILIE AGAFPSDRHA VESQLRLHGL DPDTHLIEVE PDAADGTLSM DAIAAAIAQH
     GPRLALVLWP GIQYRTGQAF ALGEIARLAR AQGAAVGFDL AHAVGNIPLS LHDDGVDFAV
     WCHYKYLNAG PGAVGGCFVH ARHAHSNLPR MAGWWGHEQP TRFRMEPQFV PSPGAEGWQL
     SNPPVLALAP LRASLELFDQ AGMPALRAKS EQLTGHLEQL IHTRVPQVLQ IVTPADPAQR
     GCQLSLRVAG GRTQGRALFE YLQSVGVLGD WREPDVIRIA PVPLYNRFCD LHQLVEHVET
     WAAA
//
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