GENTAUR Molecular Products.

 A0A063C6D8_9HYPO        Unreviewed;       505 AA.
 A0A063C6D8;
 03-SEP-2014, integrated into UniProtKB/TrEMBL.
 03-SEP-2014, sequence version 1.
 28-MAR-2018, entry version 26.
 RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
          EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
 AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
 AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
 Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
 ORFNames=UV8b_2109 {ECO:0000313|EMBL:KDB17017.1},
 UVI_02036350 {ECO:0000313|EMBL:GAO19013.1};
 Ustilaginoidea virens.
 Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
 Sordariomycetes; Hypocreomycetidae; Hypocreales;
 Hypocreales incertae sedis; Ustilaginoidea.
 NCBI_TaxID=1159556 {ECO:0000313|EMBL:KDB17017.1, ECO:0000313|Proteomes:UP000027002};
 [1] {ECO:0000313|EMBL:KDB17017.1, ECO:0000313|Proteomes:UP000027002}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=UV-8b {ECO:0000313|EMBL:KDB17017.1,
 ECO:0000313|Proteomes:UP000027002};
 Zhang Y., Zhang K., Fang A., Han Y., Yang J., Xue M., Bao J., Hu D.,
 Zhou B., Sun X., Li S., Wen M., Yao N., Ma L.-J., Liu Y., Zhang M.,
 Huang F., Luo C., Zhou L., Li J., Chen Z., Miao J., Wang S., Lai J.,
 Xu J., Hsiang T., Peng Y.-L., Sun W.;
 "Specific adaptation of Ustilaginoidea virens in occupying host
 florets revealed by comparative and functional genomics.";
 Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
 [2] {ECO:0000313|EMBL:GAO19013.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=IPU010 {ECO:0000313|EMBL:GAO19013.1};
 Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
 "Genome Sequence of Ustilaginoidea virens IPU010, a Rice Pathogenic
 Fungus Causing False Smut.";
 Genome Announc. 4:e00306-16(2016).
 [3] {ECO:0000313|Proteomes:UP000054053}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=IPU010 {ECO:0000313|Proteomes:UP000054053};
 Umemura M.;
 "Genome sequence of Ustilaginoidea virens Takahashi IPU010, a rice
 pathogen causing false smut.";
 Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
     hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
     hydroxyanthranilic acid (3-OHAA), respectively.
     {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
 -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
     hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
     ECO:0000256|PIRNR:PIRNR038800}.
 -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
     alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
     ECO:0000256|PIRNR:PIRNR038800}.
 -!- COFACTOR:
     Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
       Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
       ECO:0000256|PIRNR:PIRNR038800};
 -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
     alanine and anthranilate from L-kynurenine: step 1/1.
     {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
     from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
     ECO:0000256|PIRNR:PIRNR038800}.
 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
     ECO:0000256|PIRNR:PIRNR038800}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
     ECO:0000256|PIRNR:PIRNR038800}.
 -!- SIMILARITY: Belongs to the kynureninase family.
     {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
 -!- CAUTION: The sequence shown here is derived from an
     EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
     preliminary data. {ECO:0000313|EMBL:KDB17017.1}.
 -----------------------------------------------------------------------
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 EMBL; BBTG02000019; GAO19013.1; -; Genomic_DNA.
 EMBL; JHTR01000008; KDB17017.1; -; Genomic_DNA.
 EnsemblFungi; GAO19013; GAO19013; UVI_02036350.
 EnsemblFungi; KDB17017; KDB17017; UV8b_2109.
 UniPathway; UPA00253; UER00329.
 UniPathway; UPA00334; UER00455.
 Proteomes; UP000027002; Unassembled WGS sequence.
 Proteomes; UP000054053; Unassembled WGS sequence.
 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
 GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
 GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
 GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
 GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
 GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
 GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
 Gene3D; 3.40.640.10; -; 1.
 Gene3D; 3.90.1150.10; -; 3.
 HAMAP; MF_01970; Kynureninase; 1.
 InterPro; IPR000192; Aminotrans_V_dom.
 InterPro; IPR010111; Kynureninase.
 InterPro; IPR015424; PyrdxlP-dep_Trfase.
 InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
 InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
 PANTHER; PTHR14084; PTHR14084; 1.
 Pfam; PF00266; Aminotran_5; 1.
 PIRSF; PIRSF038800; KYNU; 1.
 SUPFAM; SSF53383; SSF53383; 2.
 TIGRFAMs; TIGR01814; kynureninase; 1.
 3: Inferred from homology;
 Complete proteome {ECO:0000313|Proteomes:UP000027002};
 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
 ECO:0000256|PIRNR:PIRNR038800};
 Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
 ECO:0000256|PIRNR:PIRNR038800};
 Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017,
 ECO:0000256|PIRNR:PIRNR038800};
 Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017,
 ECO:0000256|PIRNR:PIRNR038800};
 Reference proteome {ECO:0000313|Proteomes:UP000027002}.
 DOMAIN      140    313       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
 REGION      197    200       Pyridoxal phosphate binding.
                              {ECO:0000256|HAMAP-Rule:MF_03017}.
 BINDING     169    169       Pyridoxal phosphate; via amide nitrogen.
                              {ECO:0000256|HAMAP-Rule:MF_03017}.
 BINDING     170    170       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 BINDING     281    281       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 BINDING     284    284       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 BINDING     306    306       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 BINDING     347    347       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 BINDING     375    375       Pyridoxal phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_03017}.
 MOD_RES     307    307       N6-(pyridoxal phosphate)lysine.
                              {ECO:0000256|HAMAP-Rule:MF_03017}.
 SEQUENCE   505 AA;  55638 MW;  97D185F2E621C116 CRC64;
 MQIQFQAFVD RLRSGASPEF PADAAALAFA QELDSQDALR HLRDEFVLPS RDSLRKKALD
 GRVPGQATLD DGASGTASHQ QQQQQPSAAA ASAPCLYFAG NSLGAQPRAV RDYVNAQLET
 WASIGVNGHF TSWPNSPLTQ WQDMAEQCAR QSCDLLGASA HEIVIMNSLT VNLHLMMASF
 YRPAGRRHKV ILEWKPFPSD HYAIESHVAW HGLDPARSMV KLEPDAGGLI PTDSILRSID
 EHADETALLL LPGIQYYSGQ LFDMARITAH ARRRGITVGW DLAHAAGNVE LRLHDWDVDF
 ACWCTYKYIN AGPGAIAGAF VHERHGSVAW PRGPSGAPSY HPRLAGWYGG DKRVRFNMDN
 DFVPTPGAAG YQLSNPSAMD LAALSGALSV FNKTSMRSLR SKALVLTAYA EFLLDRMLDE
 TRGDATPLFT IITPRDPLQR GTQLSVLLRD GLLDSVSHAL EENGAICDKR KPNVIRVAPV
 PLYTRFEDVW EYMQILRRAL GLKTT

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