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Database: UniProt/TrEMBL
Entry: A0A075UPF8_9PSEU
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ID   A0A075UPF8_9PSEU        Unreviewed;       393 AA.
AC   A0A075UPF8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN   Name=kynU {ECO:0000313|EMBL:AIG74256.1};
GN   ORFNames=AJAP_06695 {ECO:0000313|EMBL:AIG74256.1};
OS   Amycolatopsis japonica.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=208439 {ECO:0000313|EMBL:AIG74256.1, ECO:0000313|Proteomes:UP000028492};
RN   [1] {ECO:0000313|EMBL:AIG74256.1, ECO:0000313|Proteomes:UP000028492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG417-CF17 (DSM 44213) {ECO:0000313|Proteomes:UP000028492};
RX   PubMed=25193710;
RA   Stegmann E., Albersmeier A., Spohn M., Gert H., Weber T.,
RA   Wohlleben W., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Amycolatopsis
RT   japonica MG417-CF17(T) (=DSM 44213T) producing (S,S)-N,N'-
RT   ethylenediaminedisuccinic acid.";
RL   J. Biotechnol. 0:0-0(2014).
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:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|PIRNR:PIRNR038800}.
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DR   EMBL; CP008953; AIG74256.1; -; Genomic_DNA.
DR   RefSeq; WP_038509040.1; NZ_CP008953.1.
DR   EnsemblBacteria; AIG74256; AIG74256; AJAP_06695.
DR   GeneID; 29592460; -.
DR   KEGG; aja:AJAP_06695; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000028492; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:0006569; P:tryptophan catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 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   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF038800; KYNU; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000028492};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038800,
KW   ECO:0000313|EMBL:AIG74256.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038800}.
FT   DOMAIN       83    293       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   393 AA;  41817 MW;  A4714528565554F5 CRC64;
     MVAVTDLVAE AAALDAADPL AHKRNDFDLD AGVAYFDGNS LGAPPKHVAG RLAAVVREQW
     GGRLIRSWSE GWWEAPVRVG GRIAPLVGAA PGQVVVADST SVNLFKALVA ATRLQPGRDE
     ILVDADTFPT DGYIADEAAR LTGRTVRRVV AEDMPAQVSE RTAVALINHV DYVTGRAHDL
     AGLTAALHRA GALALWDLCH SVGALPVELD AAGVDLAVGC TYKFLNGGPG APAFLYVATK
     WLDRFEQPLA GWAGDRDPFA MRGAYEAHAG IERGRAGTPD MLSLLALDAA LDVWDGVDRG
     VLREKGLALG DFFFRCADEL LGGAKIPTPR GRDRGHQISV IDDDAAETMA ALIDRGVIGD
     FRPPNVLRFG LAPLYTTYGE VLRAVTTLRD LRG
//
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