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Database: UniProt/TrEMBL
Entry: A0A0M4DU24_9ACTN
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ID   A0A0M4DU24_9ACTN        Unreviewed;       407 AA.
AC   A0A0M4DU24;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
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=ABE83_19660 {ECO:0000313|EMBL:ALC29047.1};
OS   Streptomyces sp. CFMR 7.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1649184 {ECO:0000313|EMBL:ALC29047.1, ECO:0000313|Proteomes:UP000061366};
RN   [1] {ECO:0000313|EMBL:ALC29047.1, ECO:0000313|Proteomes:UP000061366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFMR-7 {ECO:0000313|EMBL:ALC29047.1,
RC   ECO:0000313|Proteomes:UP000061366};
RA   Sudesh K.;
RT   "Complete genome sequence of Streptomyces sp strain CFMR 7, a natural
RT   rubber degrading Actinomycetes isolated from Penang, Malaysia.";
RL   Submitted (MAY-2015) 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; CP011522; ALC29047.1; -; Genomic_DNA.
DR   RefSeq; WP_053560527.1; NZ_CP011522.1.
DR   EnsemblBacteria; ALC29047; ALC29047; ABE83_19660.
DR   KEGG; scz:ABE83_19660; -.
DR   PATRIC; fig|1649184.3.peg.4171; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000061366; 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:UP000061366};
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       76    325       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      134    137       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     102    102       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     103    103       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     203    203       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     206    206       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     228    228       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     258    258       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     284    284       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     229    229       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   407 AA;  43113 MW;  41F9201F26D51501 CRC64;
     MSETSRETFR ERALKLDAAD PLADRRKLFA LDDGVYLDGN SLGALPVHVP ARVQDVLTRQ
     WGELRIRSWG ESGWWTAPER IGDRIAPLVG AAAGQIVVGD STSVNVFKAV VAATRLAALA
     GGGRDEILVD ATTFPTDGYI AASAARLTGH RIVPVDPADV PAALGDRTAA VLLNQVDFRT
     GRLHDLPALT AAVHAAGAIA VWDLCHSAGA LPVGLDEHGV DLAVGCTYKY LNGGPGSPAY
     LYVAERHQAA FDSPLPGWNS HADPFGMTPD YTPADGSVRG RVGTPDIVSM LTLEAALDVW
     DGVSVDAVRA KSLALTDFFL ECVEAYVPAG RVASVTPVAH AERGSQVALR CDEAEPVMSR
     LIERGVVGDL RRPDVLRFGF TPLYVGFADA ERAARVLAEV LEEIPAG
//
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