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Database: UniProt
Entry: X0JAL2_FUSOX
LinkDB: X0JAL2_FUSOX
Original site: X0JAL2_FUSOX 
ID   X0JAL2_FUSOX            Unreviewed;       489 AA.
AC   X0JAL2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   20-JUN-2018, entry version 23.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
GN   Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
GN   ORFNames=FOIG_13756 {ECO:0000313|EMBL:EXL93350.1};
OS   Fusarium oxysporum f. sp. cubense tropical race 4 54006.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089451 {ECO:0000313|EMBL:EXL93350.1, ECO:0000313|Proteomes:UP000030685};
RN   [1] {ECO:0000313|EMBL:EXL93350.1, ECO:0000313|Proteomes:UP000030685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54006 (II5) {ECO:0000313|Proteomes:UP000030685};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum II5.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000030685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54006 (II5) {ECO:0000313|Proteomes:UP000030685};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W.,
RA   O'Donnell K., Ploetz R., Steinberg C., Schwartz D.C., VanEtten H.,
RA   Zhou S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum II5.";
RL   Submitted (APR-2012) 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_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
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_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
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DR   EMBL; JH658303; EXL93350.1; -; Genomic_DNA.
DR   EnsemblFungi; EXL93350; EXL93350; FOIG_13756.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000030685; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 3.
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; 2.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030685};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800}.
FT   DOMAIN      136    314       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      188    191       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     160    160       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     161    161       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     272    272       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     275    275       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     297    297       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     337    337       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     365    365       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   MOD_RES     298    298       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
SQ   SEQUENCE   489 AA;  53758 MW;  19A99CB2626DE523 CRC64;
     MELSGFVERL RSGAAAKFPS DANSLDFARH LDSQDKLSHL RDEFVLPTKK SLKKKALDGS
     LPGAANGTNG HSNGHTNGSA DDDQQCLYFV GNSLGAQPKA VREYLNAQLE TWASIGVNGH
     FSALGNSPLP AWQDLAEDCA IKSADLVGAS PHEIVIMNTL TANLHLLMAS FYKPNEKRHK
     VILEWKPFPS DHYAIESQVV WHGLDPEKSM VKIHPNEDHI ITTDLILSTI DEHAEDTALL
     LLPGIQYYSG QLFDIPRITA YAQAKGIVVG WDLAHAAGNV ELKLHDWNVD FACWCTYKYI
     NAGPGSIAGA YVHERHGKVE LNDATGKATY RPRLMGWYGG DKSVRFNMDN NFIPTSGAGG
     FQLSNPSAID LASLSGALSV FNKTTMHDLR SKALVLTAYA EYLLDQILAE SSDAELFRII
     TPRDPLQRGT QLSVLLKDGL LDNVSAALEE NAVICDKRKP GVIRVAPVPL YTRFEDVWKF
     MQILRTALP
//
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