ID   D4GTS2_HALVD            Unreviewed;       425 AA.
AC   D4GTS2; L9V611;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN   Name=kynU {ECO:0000313|EMBL:ADE02278.1};
GN   OrderedLocusNames=HVO_2503 {ECO:0000313|EMBL:ADE02278.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE02278.1, ECO:0000313|Proteomes:UP000008243};
RN   [1] {ECO:0000313|EMBL:ADE02278.1, ECO:0000313|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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; CP001956; ADE02278.1; -; Genomic_DNA.
DR   RefSeq; WP_004042471.1; NZ_AOHU01000045.1.
DR   AlphaFoldDB; D4GTS2; -.
DR   STRING; 309800.HVO_2503; -.
DR   PaxDb; 309800-C498_07803; -.
DR   EnsemblBacteria; ADE02278; ADE02278; HVO_2503.
DR   GeneID; 8926216; -.
DR   KEGG; hvo:HVO_2503; -.
DR   PATRIC; fig|309800.29.peg.1517; -.
DR   eggNOG; arCOG00065; Archaea.
DR   HOGENOM; CLU_003433_4_1_2; -.
DR   OrthoDB; 195463at2157; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000008243; 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   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   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:UP000008243}.
FT   DOMAIN          84..376
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   425 AA;  46051 MW;  1305C143C28E3506 CRC64;
     MTDSGNPAVD AAREMDAADP LSDLRDRFFV PEGELYMDGN SLGPLSVDAE AALDRVVDEW
     RDLAIRGWTD ADPEWFSYGE RLGDRLAPLV GAKPEEVVVA NSTTVNIHAL VGTFYDPARG
     EKIVVDDLDF PTDHYAIRAQ LRAAGRDPDE ALRVVESRDG RTIETEDVLD AVDDDVGMVF
     LPSVLYRSGQ LFDIETLTEA AHEAGALAGF DLAHSVGAVP HSLSEVGVDF AVWCHYKYLN
     AGPGSIAGLY VNERHFGVTP ALAGWWGNDK ETQFDMAMTY EPAQSAGAFQ SGTVPVLSAA
     PLDGALDIVE DAGGVTALRE KSLALTDYLI ALVDERLPEC EVGTPRDPAA RGGHVAVEHP
     EAYRVSLALK ERGVIVDFRQ PNVVRMAPAP AYVGFEDVYR AVEHFREILD GEAYEAFEKQ
     SGGVT
//