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Database: UniProt/TrEMBL
Entry: A0A0M4M7Q5_9MICC
LinkDB: A0A0M4M7Q5_9MICC
Original site: A0A0M4M7Q5_9MICC 
ID   A0A0M4M7Q5_9MICC        Unreviewed;       421 AA.
AC   A0A0M4M7Q5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=AL755_01645 {ECO:0000313|EMBL:ALE04417.1};
OS   Arthrobacter sp. ERGS1:01.
OG   Plasmid unnamed2 {ECO:0000313|EMBL:ALE04417.1}.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE04417.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE04417.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE04417.1,
RC   ECO:0000313|Proteomes:UP000060433};
RC   PLASMID=Plasmid unnamed2 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-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; CP012477; ALE04417.1; -; Genomic_DNA.
DR   RefSeq; WP_054009434.1; NZ_CP012477.1.
DR   KEGG; are:AL755_01645; -.
DR   PATRIC; fig|1704044.3.peg.4282; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000060433; Plasmid unnamed2.
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:UP000060433};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Plasmid {ECO:0000313|EMBL:ALE04417.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060433}.
FT   DOMAIN       85    322       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     206    206       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     209    209       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     231    231       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     261    261       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     287    287       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     232    232       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   421 AA;  45421 MW;  A82F1403AA2CB344 CRC64;
     MDQAPPSTLD ACAAADAADP LRRFRDEFLL PDGVIYLDGN SLGPRPRTAL GVATRVMEDE
     WGTGLIRSWN TAGWFELPGR LGDKLAGLIG AGPGEVVITD TTSLNLFKAL AAALRIQQAA
     DPARTVIVTE RDNFPTDIYM AEGIADFLNQ GYSVRLVDDA LPLAAALGPD VAVVALSHVN
     YRTGAMWDMP GTTAKVHDAG ALVVWDLAHA AGAVPVDLRD SGADFAVGCT YKYLNGGPGS
     PAFIWVHAGH QDRFWQPLSG WWGHARPFAM EDSYEPVSGI GRFLCGTQPI VSMALVECGL
     DVSLAAEIDA VRAKSLALTD LFISLVAARR GDHPLELITP LDHGVRGSHV SYKHPEGYAV
     MAALIARGVI GDYREPHVLR FGITPLYLGF VDVWNAVDAL FDVLDNRLWD APQFRERLKV
     T
//
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