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

 A0A0L0P2I9_CANAR        Unreviewed;       453 AA.
A0A0L0P2I9;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
28-MAR-2018, entry version 17.
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=QG37_02511 {ECO:0000313|EMBL:KNE00480.1};
Candida auris (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
Clavispora/Candida clade.
NCBI_TaxID=498019 {ECO:0000313|EMBL:KNE00480.1, ECO:0000313|Proteomes:UP000037122};
[1] {ECO:0000313|Proteomes:UP000037122}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=6684 {ECO:0000313|Proteomes:UP000037122};
PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
Tatu U.S.;
"Draft genome of a commonly misdiagnosed multidrug resistant pathogen
Candida auris.";
BMC Genomics 16:686-686(2015).
-!- 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:KNE00480.1}.
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EMBL; LGST01000018; KNE00480.1; -; Genomic_DNA.
RefSeq; XP_018170203.1; XM_018311969.1.
EnsemblFungi; KNE00480; KNE00480; QG37_02511.
GeneID; 28876289; -.
KEGG; caur:QG37_02511; -.
KO; K01556; -.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000037122; 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; 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; 1.
TIGRFAMs; TIGR01814; kynureninase; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000037122};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:KNE00480.1};
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}.
DOMAIN 94 276 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 139 142 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_03017}.
BINDING 111 111 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03017}.
BINDING 112 112 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 223 223 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 226 226 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 248 248 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 283 283 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 311 311 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
MOD_RES 249 249 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_03017}.
SEQUENCE 453 AA; 50376 MW; B4CC96CE9FBEAFF7 CRC64;
MASSEQLPTF KPLFQVPTFK SLGLDPPAGF HDESSSVYLA GNSLGLMPKA TRQALADELD
AWGARGVESH FNHPGEGAGK TSWVDIDLPL VQPLAKLVGA TEKEVAAMGT LTSNLNALLT
SFYKPSGKRT KIMFERHAFP SDYYAFLNMV KLHGYDESHL IQLAVAPGKH YLETEEIIEV
IEKEGDEIAV ICFPGVQYYT GQFFKIPEIT AAAQKKGIVV GWDLAHAVGN VPLKLHEWNV
DFAVWCSYKY LNSGPGGIAG IFVHERHTKN NSKVNYPPRL AGWWGNNAAE RFKMLEVFDP
INSALSYRQS NPLVIDCVAL KSSLDVFELA GGLDNLRKTS VSLTGCLLRL LKGSKYYIED
PLDNALLGFK ILTPCEESER GCQLSVLFQP HDDDRSKNVM EQVNEYLHKH AIICDERRPD
VIRIAPTPLY NTLEDVRVVV KRIVEALDEL SRS


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