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Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)

 A0A063C6D8_9HYPO        Unreviewed;       505 AA.
A0A063C6D8;
03-SEP-2014, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 1.
27-SEP-2017, entry version 24.
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; -; 2.
HAMAP; MF_01970; Kynureninase; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR010111; Kynureninase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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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