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Database: UniProt/TrEMBL
Entry: A0A0N9UTX6_SPHMC
LinkDB: A0A0N9UTX6_SPHMC
Original site: A0A0N9UTX6_SPHMC 
ID   A0A0N9UTX6_SPHMC        Unreviewed;       417 AA.
AC   A0A0N9UTX6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
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=AN936_00670 {ECO:0000313|EMBL:ALH78936.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH78936.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH78936.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH78936.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A.,
RA   Yamazoe A., Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene
RT   Glycol-Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
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; CP012700; ALH78936.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALH78936; ALH78936; AN936_00670.
DR   KEGG; smag:AN936_00670; -.
DR   PATRIC; fig|33050.5.peg.137; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000058074; 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:UP000058074};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074}.
FT   DOMAIN       85    352       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   BINDING     103    103       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     104    104       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     173    173       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     202    202       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     205    205       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     227    227       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     257    257       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     283    283       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     228    228       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   417 AA;  44343 MW;  D1856A5B3151FC83 CRC64;
     MTLDTAMLDR AACEAMDRAD PLAPLRDRFD LPEGMIYLDG NSLGAMPKGA AARSHEVVTR
     EWGTDLIKSW NSAGWFDLPV RLGDKLAPLV GAAPGEVVIC DSTSQNLFKV LSAAAALRPG
     RSVLILEGSN FPTNNYIAEG VAAATGGRVS VRLCEKDEIA GAIDDDTIAA AITHVHYKSG
     HVHDMAAITA RAHEAGALAI WDLCHSAGAM PVDLGGAGAD FAVGCTYKYL NGGPGSPAFL
     FAAKRHQGQA LQPVTGWWGH AAPFAFEPGY RPQHDIRQFL IGTQPIVSMA LVETGLDIHL
     AADMDAIRAK SMALTDLFIR LVEARCAGHG FTLASPRDAA ARGSQVSFAH AEGYPIMRAL
     IAAGVIGDFR APDTVRFGFT PLYTGYADVW DAVDRLATIM DGGIWKLPEH QVRDAVT
//
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