ID   A0A0F0HK53_9ACTN        Unreviewed;       399 AA.
AC   A0A0F0HK53;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   19-JAN-2022, entry version 27.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
GN   ORFNames=UK14_02880 {ECO:0000313|EMBL:KJK54183.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK54183.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK54183.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK54183.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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. {ECO:0000256|HAMAP-
CC       Rule:MF_01970, 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_01970,
CC         ECO:0000256|PIRNR:PIRNR038800};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
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_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}.
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:KJK54183.1}.
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DR   EMBL; JYJI01000011; KJK54183.1; -; Genomic_DNA.
DR   EnsemblBacteria; KJK54183; KJK54183; UK14_02880.
DR   PATRIC; fig|1609137.3.peg.3159; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000033569; 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-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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF038800; KYNU; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01970};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_01970};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01970}; Reference proteome {ECO:0000313|Proteomes:UP000033569}.
FT   DOMAIN          77..363
FT                   /note="Aminotran_5"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          131..134
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         102
FT                   /note="Pyridoxal phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         103
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         200
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         203
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         225
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         255
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   BINDING         281
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
SQ   SEQUENCE   399 AA;  41694 MW;  E77E7F3155DD2CD6 CRC64;
     MPGGAADLRD RAAALDAADE LAKLRERFVL PDGVVYLDGN SLGALPAGVA ATTADVVARQ
     WGELLIRSWE ESGWWTAPER TGDKIAPLVG AAAGQVVVGD STSVNLFKAL VGAARLAAPG
     RTRMLVDAAT FPTDGYIAQS AARLTGLTVV PVDPSHAAEA MDADTAVVLL NHVDYRTGRL
     HDLPALTAAA RAAGAVTVWD LCHSAGALPV GLDAHGVDLA VGCTYKYLNG GPGAPAYLYI
     ATRHQDAFDS PLPGWNGHAD PFAMTPAYEA APGASRARVG TPDILSMLAL EAALDAWDGV
     CVEAVRAKSL ALTDFFLECV AAYVPQGLVE PVTPAEHEHR GSQVSLRTGN AREVMGELIS
     RGVIGDFRAP DVLRFGFTPL YVGFADVERA ARTLGHIFG
//