ID A0A0Q7SAB4_9CAUL Unreviewed; 411 AA.
AC A0A0Q7SAB4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN ORFNames=ASD25_06555 {ECO:0000313|EMBL:KQY84687.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY84687.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY84687.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY84687.1,
RC ECO:0000313|Proteomes:UP000051815};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {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|PIRNR:PIRNR038800};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC and anthranilate from L-kynurenine: step 1/1.
CC {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 2/3. {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- SIMILARITY: Belongs to the kynureninase family.
CC {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY84687.1}.
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DR EMBL; LMFL01000023; KQY84687.1; -; Genomic_DNA.
DR RefSeq; WP_056617961.1; NZ_LMFL01000023.1.
DR AlphaFoldDB; A0A0Q7SAB4; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000051815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:InterPro.
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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038800};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|PIRNR:PIRNR038800};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038800};
KW Reference proteome {ECO:0000313|Proteomes:UP000051815}.
FT DOMAIN 78..345
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 411 AA; 43971 MW; 017A53776B438318 CRC64;
MTTRQTCLDR DSADPLGGVR ERFSLPDGAI YLDGNSLGAL TYAAAARVGE TTGQQWGRDL
ISSWNSHGWI RLPQQVGGKI ARLIGAGADE VIAADSVSVN LFKLAAAAVR AQGPDRKTVI
IERGDFPTDL YILQGLAEVM PGIDLRVVEP GGFEAALDDR TAVVLLSHVH YRTGMVRDMA
AQGAAVRAAG ALSLWDLSHS AGVLDIGLNR DGADMAAGCG YKYLNGGPGA PAYLFVAKRH
QATLRNPLSG WMGHARPFDF VDNYQPAPGM DRWLCGTPPI LSLTALDAAL DAFDGVDMGQ
ARIKAGALGD LFIERVEARC AAHGLALVGP REAAARGGQV SFAHPEGWAV MQNLIARGVI
GDFRRPDVIR FGFAPLYVRH VDVWDAVETL GDILDSESWR DERFQTVSAV T
//
