KYNU_PSEFL
ID KYNU_PSEFL Reviewed; 416 AA.
AC P83788;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
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};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP CATALYTIC ACTIVITY, HOMODIMERIZATION, AND MUTAGENESIS OF ASP-132 AND
RP ASP-201.
RX PubMed=14756555; DOI=10.1021/bi035744e;
RA Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S.;
RT "Three-dimensional structure of kynureninase from Pseudomonas
RT fluorescens.";
RL Biochemistry 43:1193-1203(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.
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 ECO:0000269|PubMed:14756555};
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, ECO:0000269|PubMed:14756555};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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 ECO:0000269|PubMed:14756555}.
CC -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000255|HAMAP-
CC Rule:MF_01970}.
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DR PDB; 1QZ9; X-ray; 1.85 A; A=1-416.
DR PDBsum; 1QZ9; -.
DR AlphaFoldDB; P83788; -.
DR SMR; P83788; -.
DR DrugBank; DB02343; 3,6,9,12,15-Pentaoxaheptadecane.
DR BioCyc; MetaCyc:MON-7065; -.
DR BRENDA; 3.7.1.3; 5121.
DR SABIO-RK; P83788; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR EvolutionaryTrace; P83788; -.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Pyridine nucleotide biosynthesis;
KW Pyridoxal phosphate.
FT CHAIN 1..416
FT /note="Kynureninase"
FT /id="PRO_0000357010"
FT BINDING 97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970,
FT ECO:0000269|PubMed:14756555"
FT BINDING 98
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970,
FT ECO:0000269|PubMed:14756555"
FT BINDING 129..132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 172
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970,
FT ECO:0000269|PubMed:14756555"
FT BINDING 201
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970,
FT ECO:0000269|PubMed:14756555"
FT BINDING 204
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01970,
FT ECO:0000269|PubMed:14756555"
FT BINDING 226
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000305|PubMed:14756555"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000305|PubMed:14756555"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000305|PubMed:14756555"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 132
FT /note="D->A: Reduces binding to pyridoxal phosphate and
FT strongly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:14756555"
FT MUTAGEN 132
FT /note="D->E: Enhances binding to pyridoxal phosphate."
FT /evidence="ECO:0000269|PubMed:14756555"
FT MUTAGEN 201
FT /note="D->E: Enhances binding to pyridoxal phosphate."
FT /evidence="ECO:0000269|PubMed:14756555"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 203..208
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 243..248
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 303..325
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1QZ9"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1QZ9"
FT HELIX 385..401
FT /evidence="ECO:0007829|PDB:1QZ9"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1QZ9"
SQ SEQUENCE 416 AA; 45905 MW; 50C3DE62A20C779D CRC64;
MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA VIAEEWGNGL
IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN LFKVLSAALR VQATRSPERR
VIVTETSNFP TDLYIAEGLA DMLQQGYTLR LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY
MHDMQALTAL SHECGALAIW DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW
VSPQLCDLVP QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ
TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP EGYAVIQALI
DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD RKTWAQAQFQ VRHSVT
