ID R1E7W3_BOTPV Unreviewed; 499 AA.
AC R1E7W3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=UCRNP2_9453 {ECO:0000313|EMBL:EOD43858.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD43858.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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. {ECO:0000256|HAMAP-
CC Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) +
CC L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:58125; EC=3.7.1.3;
CC Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=3.7.1.3;
CC Evidence={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-alanine
CC and anthranilate from L-kynurenine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC 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. {ECO:0000256|HAMAP-
CC Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
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DR EMBL; KB916790; EOD43858.1; -; Genomic_DNA.
DR RefSeq; XP_007588687.1; XM_007588625.1.
DR AlphaFoldDB; R1E7W3; -.
DR STRING; 1287680.R1E7W3; -.
DR KEGG; npa:UCRNP2_9453; -.
DR eggNOG; KOG3846; Eukaryota.
DR HOGENOM; CLU_003433_4_0_1; -.
DR OMA; LPGWNSH; -.
DR OrthoDB; 5471916at2759; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01970; Kynureninase; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010111; Kynureninase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01814; kynureninase; 1.
DR PANTHER; PTHR14084; KYNURENINASE; 1.
DR PANTHER; PTHR14084:SF0; KYNURENINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF038800; KYNU; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03017};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_03017};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_03017}; Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 126..307
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 151
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 152
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 179..182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 290
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 341
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT BINDING 369
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
SQ SEQUENCE 499 AA; 54955 MW; 75B92D590C7B0044 CRC64;
MAQDTSSELQ LDDPKSFTKE YAEALDAQDP LRKLREEFII PTRAGLKRKR LGTGAGAVEV
SEKINSLLPE NELTYPCTYL CGNSLGLQPR RTQEYIRKYL DTWANKGVYG HFQPLEDAVS
RPWVDIDEDA KVESAKIVGA QPDEVAVMQT LTANIHLLMA SFFRPTKQRY KIIIEGKAFP
SDHYAVRSQL HHHNLHPSTA LVELNPPDST TAYLPTSYIL SVIDEHADTT ALLLLPGIQY
YSGQLFDIPR ITAHAQARGI TVGWDLAHAV GNVPLSLHDW NVDFAAWCNY KYMNGGPGVI
GGLFVHSRHT SITTPSADPS SSPPTAITAS TLGYQPRLSG WWGHDKSSRF QMHSTFVPMP
GAAGFQLSNP SALDTTALLA SLSVFAQTSV ADLRAKSLRL TAYLEHLLSA AADADRPYSL
ITPKDPQERG AQLSLLLRPG LLEPVMEELE EKGVVVDERR PDVVRVAPAP LYNGFGDVWR
FVEVFKEACR KAEAAAAGK
//
