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Database: UniProt/TrEMBL
Entry: A0A0F7CP94_9ACTN
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ID   A0A0F7CP94_9ACTN        Unreviewed;       645 AA.
AC   A0A0F7CP94;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-FEB-2018, entry version 13.
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=SXIM_28820 {ECO:0000313|EMBL:AKG44266.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG44266.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|EMBL:AKG44266.1, ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces
RT   xiamenensis.";
RL   Submitted (FEB-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}.
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; CP009922; AKG44266.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKG44266; AKG44266; SXIM_28820.
DR   KEGG; sxi:SXIM_28820; -.
DR   PATRIC; fig|408015.6.peg.2918; -.
DR   KO; K01556; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000034034; 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; 3.40.50.1820; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_01970; Kynureninase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010111; Kynureninase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000034034};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034034}.
FT   DOMAIN       34    335       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   DOMAIN      449    547       Abhydrolase_3. {ECO:0000259|Pfam:
FT                                PF07859}.
FT   REGION      130    133       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     101    101       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING     102    102       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     199    199       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     202    202       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     224    224       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     254    254       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     280    280       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     225    225       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   645 AA;  67281 MW;  9D166FE59D8AA296 CRC64;
     MAADAGEPGA EARRLDAADP LRAKRAAFVL DDTVYLDGNS LGALPRTVPD RLAEVVSREW
     GQLRIRSWTE SGWWTAPERV GDRIAPLLGA APGQVVVGDS TSVNVFKAMV AAVRIAPSGR
     DEILVDATTF PTDGYIADSA ARLTGRTLRP VPAERIAEEA GPRTAAVLVN HVDYRTGELR
     DLPGITAAVH AAGAQAVWDL CHSAGALPLA LDADGVDFAV GCTYKYLNGG PGAPAFLYVR
     SGHQEAFDSP LPGWNSHAEP FAMSPRYRPA DGAPRGRVGT PEILSLLALE AALEVWDGVD
     MAEVRAKSLA LTAFFERRLA GLLPSITPAD PARRGSQVAL RCPDARRVTA ELTRRGVVAD
     FREPDVLRFG FTPLYTSFAD ADRAARVLTE VLAGTPAPPS GAGAPDTGRD ADEAAALLSR
     PPAPPARTLR YGPHPAQLVD LYGDGDPRVV IVHGGWWRES YDRAHLSPLA AALAGHGVPA
     ALIEYRRGAG SWPHAAEDVR AALDALPGSA PLTLAGHSAG GQLALWAAAR DHRRVARTVV
     VSPVADLVAA DRLGLGAGAV RDHLGGPHPQ ADPLRLPTPP GPVTVLHGAE DGQVPLAHSL
     AYATRHGATV IPLPGTGHYA PMDPGTAAGA RLIAVLAGGP AQAGT
//
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