ID A0A0V8J965_9BACI Unreviewed; 421 AA.
AC A0A0V8J965;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AS030_12875 {ECO:0000313|EMBL:KSU83450.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU83450.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU83450.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU83450.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU83450.1}.
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DR EMBL; LNQN01000002; KSU83450.1; -; Genomic_DNA.
DR RefSeq; WP_061972289.1; NZ_KQ758618.1.
DR AlphaFoldDB; A0A0V8J965; -.
DR OrthoDB; 9812626at2; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000054099; 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; 3.90.1150.10; 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|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:UP000054099}.
FT DOMAIN 78..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 98
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 125..128
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 206
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 209
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 231
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 260
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT BINDING 288
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01970"
SQ SEQUENCE 421 AA; 47083 MW; B4C0EF01B86938BE CRC64;
MKQAYWTEMD GKDGLKHFKE EFYVKKGVLY MDGNSLGLLS KNAEKTLAEV LTDWKEYGID
GWMAGTHPWF TLSEKLGGKM APLIGAHKDE VIVTGSTTGN LHQLVSTFFQ PAGTKTKILA
DELTFPSDIY ALKSQLHLKS LTPADHLLSV KSQDGRMIEE EDIISSMTEE VALIVLPSVL
YRSGQLLDIQ RLTAEAHKRG ILIGFDLCHS IGAVPHELSN WEVDFAFWCN YKYLNGGPGS
VAGLYVNRKH FKTAPGLAGW FGSNKEKQFD MSLEFVPSDT AGAFQMGTPH VLSTAPLIGS
LELFAEAGMG RLREKSLQLT RYMMELIETE LSSFGFHIGN PREDERRGGH VCLEHSEAAR
ICKALKENQV VPDFRAPNVI RLAPVPLYTS FQDVHDTIVR LKKIMSEKQY EKFPNVREVI
A
//
