KYNU_BACC1
ID KYNU_BACC1 Reviewed; 428 AA.
AC Q736W3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_01970};
DE EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_01970};
DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_01970};
GN Name=kynU {ECO:0000255|HAMAP-Rule:MF_01970}; OrderedLocusNames=BCE_2787;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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:0000255|HAMAP-
CC Rule:MF_01970}.
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:0000255|HAMAP-Rule:MF_01970};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01970};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC and anthranilate from L-kynurenine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01970}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01970}.
CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP-
CC Rule:MF_01970}.
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DR EMBL; AE017194; AAS41699.1; -; Genomic_DNA.
DR RefSeq; WP_000287845.1; NC_003909.8.
DR AlphaFoldDB; Q736W3; -.
DR SMR; Q736W3; -.
DR EnsemblBacteria; AAS41699; AAS41699; BCE_2787.
DR GeneID; 59159979; -.
DR KEGG; bca:BCE_2787; -.
DR HOGENOM; CLU_003433_4_0_9; -.
DR OMA; TFPTDGY; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000002527; 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-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; Pyridine nucleotide biosynthesis; Pyridoxal phosphate.
FT CHAIN 1..428
FT /note="Kynureninase"
FT /id="PRO_0000356988"
FT BINDING 104
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 105
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 132..135
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 213
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 216
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 238
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT BINDING 295
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
SQ SEQUENCE 428 AA; 48542 MW; B3910FB7D179773C CRC64;
MYTEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS
WKEYGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG
IRTKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IHAMTDDIAL
ILLPSVLYRS GQVLDMKRLT AEAHKRGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY
LNAGPGGVAG LYVNKKHCNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS
TAPLIGSLEI FKEAGIERLR EKSLHITSYM LNLIAHELSD FEFTIGNPLE DEKRGGHIYL
EHAEAARICK ALKADGVIPD FRAPNGVRLA PVALYNTYEE VWKSVQILKK IMKDEEYKQF
ENKREVVA
