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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.
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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Pathways :
WP1020: Fatty Acid Biosynthesis
WP1139: Fatty Acid Biosynthesis
WP121: Colanic Acid Building Blocks Biosynthesis
WP1228: Fatty Acid Biosynthesis
WP1352: Fatty Acid Biosynthesis
WP137: Fatty Acid Biosynthesis, Initial Steps
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1685: Peptidoglycan biosynthesis
WP1700: Selenoamino acid metabolism
WP1996: Linoleate Biosynthesis
WP2316: PPAR signaling pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP336: Fatty Acid Biosynthesis
WP357: Fatty Acid Biosynthesis
WP38: Fatty Acid Biosynthesis
WP472: Phosphatidic Acid and Phospholipid Biosynthesis
WP504: Fatty Acid Biosynthesis
WP555: Folic acid biosynthesis
WP563: Glycerol Teichoic Acid Biosynthesis
WP568: Fatty Acid Biosynthesis
Related Genes :
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[Kynu] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[kynU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[Kynu] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[BNA5 YLR231C L8083.14] Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)
[BNA5 M433DRAFT_3381] Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)
[Kynu KYNU mCG_19640] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[flu-2 C15H9.7] Kynureninase (EC 3.7.1.3) (Abnormal fluorescence under UV illumination) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[KYNU] Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)
[BNA5 FOXB_00888] Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)
[bna5-2 AN1857] Kynureninase 2 (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5-2) (L-kynurenine hydrolase 2)
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