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Database: UniProt/TrEMBL
Entry: A0A1A9IYB9_9ACTN
LinkDB: A0A1A9IYB9_9ACTN
Original site: A0A1A9IYB9_9ACTN 
ID   A0A1A9IYB9_9ACTN        Unreviewed;       431 AA.
AC   A0A1A9IYB9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
GN   ORFNames=A8713_16785 {ECO:0000313|EMBL:ANH92608.1};
OS   Streptomyces sp. SAT1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1849967 {ECO:0000313|EMBL:ANH92608.1, ECO:0000313|Proteomes:UP000078022};
RN   [1] {ECO:0000313|EMBL:ANH92608.1, ECO:0000313|Proteomes:UP000078022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAT1 {ECO:0000313|EMBL:ANH92608.1,
RC   ECO:0000313|Proteomes:UP000078022};
RA   Dou G.;
RT   "Complete genome of endophytic Streptomyces sp.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
CC         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|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}.
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DR   EMBL; CP015849; ANH92608.1; -; Genomic_DNA.
DR   RefSeq; WP_064534316.1; NZ_CP015849.1.
DR   EnsemblBacteria; ANH92608; ANH92608; A8713_16785.
DR   GeneID; 32627386; -.
DR   KEGG; strt:A8713_16785; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000078022; 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; 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; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078022};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800}.
FT   DOMAIN      178    348       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      157    160       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      99     99       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     100    100       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     226    226       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     229    229       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     251    251       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     281    281       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     307    307       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     252    252       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   431 AA;  45528 MW;  BD397D84ABC3B720 CRC64;
     MPDGALAGRA EKLDAADALA AVRERFVLDD VVYLDGNSLG ALPAHVPDRV ADVVRRQWGE
     LRIRSWDESG WWTAPERIGD RIAPLVGAAP GRIVVGDSTS VNVFKALVAA VRMARETGGG
     DGSGLAGQAG QAGQGDQADQ GGEGSGRDEI LVDATTFPTD GYIARSAARM TGCEVRPVAP
     AEVPGALSDR TAAVLLNHVD YRTGRLHDLP SLTAAVHAAG AYAVWDLCHS AGALPVGLDE
     HGVALAVGCT YKYLNGGPGS PAFLYVRQDL QERFDSPLPG WNSHAEPFGM RPEYEPAHGA
     LRGRVGTPDI LSLLALEASL EVWDGVPIEA VRAKSLALTD FFLECVAAYV PAGRVECVTP
     AEHDLRGSQI ALRCPDAGPV MKRLIERGVV GDFRRPDVLR FGFTPLYVGF GDAERAARVL
     GEVLAEASDE G
//
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