ID A0A2T0RAA3_9ACTN Unreviewed; 419 AA.
AC A0A2T0RAA3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN ORFNames=CLV37_101340 {ECO:0000313|EMBL:PRY18096.1};
OS Kineococcus rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=559628 {ECO:0000313|EMBL:PRY18096.1, ECO:0000313|Proteomes:UP000238083};
RN [1] {ECO:0000313|EMBL:PRY18096.1, ECO:0000313|Proteomes:UP000238083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19711 {ECO:0000313|EMBL:PRY18096.1,
RC ECO:0000313|Proteomes:UP000238083};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY18096.1}.
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DR EMBL; PVZF01000001; PRY18096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RAA3; -.
DR OrthoDB; 9812626at2; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000238083; 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 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}.
FT DOMAIN 99..336
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 419 AA; 44071 MW; A74FAB24A2E26ACD CRC64;
MSLTDRAAEL DAADPLAAHR DEFLLEAAPA VTSYLDGNSL GRPLKATPAA LDAFVRAEWG
GRLIQGWTHD AQVGEGGWMD WPTDLGDRIG RVVLGAGPGQ TVVADSTTVL FYKLVRAALD
HALAEGRDEI VADTDNFPTD RFVLEGVAAE RGATLRWIET DPAAGISAAQ VAAAVGPRTA
LATFSHVAYR SGHLADGPAI TAAVHDAGAL VLWDLSHSAG SVPLALDAWG ADLAVGCTYK
YLNGGPGAPA FAYLARRHHG LLRQPVQGWM GHADPFAMGQ GYRPDPGVRQ LISGTPPIVA
MVPVRAGVDQ LERVGIDAVR AKSTALTSFA LEVADELLVP HGVTVATPRE PAARGGHVTL
RAGDSGRDFR QTTARLWTEG VVPDFRTPDG IRIGLAPLST SFGEVLDGLL ALHRIVENS
//
