ID F0M7D8_PSEPM Unreviewed; 419 AA.
AC F0M7D8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN OrderedLocusNames=Asphe3_14180 {ECO:0000313|EMBL:ADX72592.1};
OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX72592.1, ECO:0000313|Proteomes:UP000008639};
RN [1] {ECO:0000313|EMBL:ADX72592.1, ECO:0000313|Proteomes:UP000008639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC {ECO:0000313|Proteomes:UP000008639};
RX PubMed=21677849; DOI=10.4056/sigs.1393494;
RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT (Sphe3).";
RL Stand. Genomic Sci. 4:123-130(2011).
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}.
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DR EMBL; CP002379; ADX72592.1; -; Genomic_DNA.
DR RefSeq; WP_013600531.1; NC_015145.1.
DR AlphaFoldDB; F0M7D8; -.
DR SMR; F0M7D8; -.
DR STRING; 930171.Asphe3_14180; -.
DR KEGG; apn:Asphe3_14180; -.
DR eggNOG; COG3844; Bacteria.
DR HOGENOM; CLU_003433_4_1_11; -.
DR OrthoDB; 9812626at2; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000008639; Chromosome.
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 97..368
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 419 AA; 45191 MW; 5101A40A86752D77 CRC64;
MSMDQQSPTK DAQTWLQQRA VELDNKDPLA HCRQHFIGTD TPLSYLDGNS LGRPLKRTPD
DISRFITQGW GGRLIRGWDE EWLDLPQSIG DQLGRAVLGA APGQTIIADS TTVVLYKLIR
AALAAVADPD RNELVLDTEN FPTDRYLVEG IALEEGLTLR WIQADPAAGV TVQQVREATG
PRTAVVLLSQ VAYRSGHLAD LPAITAAVHD AGALVVWDLC HSAGSVEIGL DSAGVDFAAG
CTYKYLNGGP GSPAFAYVNQ RHLASLNQPI WGWMGRKDAF EMAAGYEPAA GIRGFLSGTP
AVFGMLAMRG TLDLIEEATM AAIREKSIQL TDFAVEVFDA LLAPLGAELG TPREPARRGS
HITVDHPDFT KATVEALWAG DVIPDFRSPH GIRVGLSPLS TSFQETLQGM AAMRDRLQG
//
