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Database: UniProt/TrEMBL
Entry: A0A093B6E2_9PSEU
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ID   A0A093B6E2_9PSEU        Unreviewed;       392 AA.
AC   A0A093B6E2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   12-APR-2017, entry version 15.
DE   RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN   ORFNames=BB31_24415 {ECO:0000313|EMBL:AJK56349.1};
OS   Amycolatopsis lurida NRRL 2430.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1460371 {ECO:0000313|EMBL:AJK56349.1, ECO:0000313|Proteomes:UP000029326};
RN   [1] {ECO:0000313|EMBL:AJK56349.1, ECO:0000313|Proteomes:UP000029326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2430 {ECO:0000313|EMBL:AJK56349.1,
RC   ECO:0000313|Proteomes:UP000029326};
RX   PubMed=25323720;
RA   Kwun M.J., Hong H.J.;
RT   "Draft Genome Sequence of Amycolatopsis lurida NRRL 2430, Producer of
RT   the Glycopeptide Family Antibiotic Ristocetin.";
RL   Genome Announc. 2:0-0(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; CP007219; AJK56349.1; -; Genomic_DNA.
DR   KEGG; alu:BB31_24415; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000029326; 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   Gene3D; 3.90.1150.10; -; 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   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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029326};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038800}.
FT   DOMAIN       81    293       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   392 AA;  41868 MW;  7C22FD14E7E72597 CRC64;
     MVAVTDLVAE AAALDAADPL AHKRNEFDLD ASVAYFDGNS LGAPPKHVAE RVAAVVREQW
     GGRLIRSWSE GWWEAPVRVG ERIAPLVGAA PGQLVVADST SVNLFKALVA ATRLQPGRDE
     ILVDADTFPT DGYIADEVAR LTGRTVRRVV AEDMPAQVSE RTAVALINHV DYVTGRAHDM
     AGLTAALHRA GALALWDLCH SVGALPVELD AAGVDLAVGC TYKFLNGGPG SPAFLYVATK
     WLDSFDQPLA GWAGDRDPFA MRGAYEADAG IARGRAGTPD ILSLLALDAA LDVWDGVDRG
     VLRTKGLALG DFFFRCADEL LDGATIRTPR GEDRGHQISV ADDDAAKTMA ALIDRGVIGD
     FRPPNVLRFG LAPLYTTYGE VLRAVTTLRE FR
//
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