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Database: UniProt/SWISS-PROT
Entry: KYNU_FLAJ1
LinkDB: KYNU_FLAJ1
Original site: KYNU_FLAJ1 
ID   KYNU_FLAJ1              Reviewed;         425 AA.
AC   A5FMM4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 72.
DE   RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_01970};
DE            EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_01970};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000255|HAMAP-Rule:MF_01970};
GN   OrderedLocusNames=Fjoh_0506;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101)
OS   (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / UW101;
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B.,
RA   Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W.,
RA   Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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:0000255|HAMAP-Rule:MF_01970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC         Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972;
CC         EC=3.7.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate +
CC         H(+) + L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:58125; EC=3.7.1.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01970};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01970}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
DR   EMBL; CP000685; ABQ03541.1; -; Genomic_DNA.
DR   RefSeq; WP_012022597.1; NZ_MUGZ01000026.1.
DR   ProteinModelPortal; A5FMM4; -.
DR   SMR; A5FMM4; -.
DR   STRING; 376686.Fjoh_0506; -.
DR   EnsemblBacteria; ABQ03541; ABQ03541; Fjoh_0506.
DR   GeneID; 31763377; -.
DR   KEGG; fjo:Fjoh_0506; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242438; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   OrthoDB; 1474443at2; -.
DR   BioCyc; FJOH376686:G1G8T-533-MONOMER; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000006694; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    425       Kynureninase.
FT                                /FTId=PRO_0000357005.
FT   REGION      133    136       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     105    105       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     106    106       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     218    218       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     221    221       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     243    243       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     274    274       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     302    302       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   425 AA;  48720 MW;  0070DB3521B3E741 CRC64;
     MTFQNTREFA KQLDAQDALN HYQEQFIFPK VNDKRVIYFT GNSLGLQPKR TKAYIDEVMN
     DWAELAVEGH FYAEKPWWDY QERFSEPLSK IVGALPSEVT VMNTLTVNLH LLMVSFYQPK
     GKRYKIICEE KAFPSDQYMF QSQVHFHGYK PEDAIVEIKR REGEHNIRLE DVLAKIEEVG
     DELALVLIGG VNYYTGQVFD IKTITAAGQK AGAKVGWDLA HAAGNIKLEL HDWNVDFAAW
     CSYKYMNSGP GNASGVFVHE RHHNDPDLPR FAGWWGHNKE RRFKMEPNFD PVHGAGGWQI
     SNLPVLSLAP YLASVEMFAE VGMDALIAKR DHITSYLEFI LHEIDKEVES TFEIITPSNP
     EERASQLSVF LHGEGRSLFD YLMKNGVITD WREPNVIRLA PVPLYCSYED MYDFGQILKK
     GILGK
//
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