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Database: UniProt/TrEMBL
Entry: A0A1B2HYB2_9PSEU
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Original site: A0A1B2HYB2_9PSEU 
ID   A0A1B2HYB2_9PSEU        Unreviewed;       373 AA.
AC   A0A1B2HYB2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
GN   ORFNames=BBK82_12845 {ECO:0000313|EMBL:ANZ42696.1};
OS   Lentzea guizhouensis.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Lentzea.
OX   NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ42696.1, ECO:0000313|Proteomes:UP000093053};
RN   [1] {ECO:0000313|EMBL:ANZ42696.1, ECO:0000313|Proteomes:UP000093053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ42696.1,
RC   ECO:0000313|Proteomes:UP000093053};
RA   Cao C.;
RT   "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL   Submitted (JUL-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}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01970}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_01970}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01970}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01970}.
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; CP016793; ANZ42696.1; -; Genomic_DNA.
DR   RefSeq; WP_065921021.1; NZ_CP016793.1.
DR   EnsemblBacteria; ANZ42696; ANZ42696; BBK82_12845.
DR   KEGG; led:BBK82_12845; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000093053; 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; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000093053};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   DOMAIN       21    323       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      113    116       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      86     86       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      87     87       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     180    180       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     183    183       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     205    205       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     235    235       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     261    261       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     206    206       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   373 AA;  40905 MW;  F769FC8AF3F0028C CRC64;
     MDGEELRVRR ELFDIPEGVI YLDGNSLGAP PKHVAERVQE VVKHQWGTRL IRSWSEGWWE
     APQRIGDRIG RLVGAAPGQV VVGDSTSVNV FKALMGAVKG TGRTEIVVDE STFPTDGYIA
     QSVASLTGLK IRPARPSSLD LTEDTAVVLL NHVDYRTGEL LDMAEHTERA HAVGAQVVWD
     LCHSAGVLPI ELDALNVDYA IGCTYKFLNG GPGSPAFIYV PHAKQATFEN PLSGWNGHRE
     PFGMQPSYEP DPGIVRARVG TPDILSMLAL DAALDVWDDV DLAELRQRGL QLTALFREHV
     QKLTDLEVVT PEQRGNQISV RCPDAKNVMD ELVNRGVIGD HRPPDVLRFG FAPLYVTDED
     AVKAAEVLAD VIR
//
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