(data stored in ACNUC7421 zone)

SWISSPROT: KYNU_EXIS2

ID   KYNU_EXIS2              Reviewed;         425 AA.
AC   B1YHD6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 75.
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=Exig_0182;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) 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: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}.
DR   EMBL; CP001022; ACB59668.1; -; Genomic_DNA.
DR   RefSeq; WP_012369093.1; NC_010556.1.
DR   SMR; B1YHD6; -.
DR   STRING; 262543.Exig_0182; -.
DR   EnsemblBacteria; ACB59668; ACB59668; Exig_0182.
DR   KEGG; esi:Exig_0182; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242438; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   OrthoDB; 1474443at2; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001681; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; B1YHD6.
DR   SWISS-2DPAGE; B1YHD6.
KW   Hydrolase; Pyridine nucleotide biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..425
FT                   /note="Kynureninase"
FT                   /id="PRO_0000357004"
FT   REGION          129..132
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         101
FT                   /note="Pyridoxal phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         102
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         210
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         213
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         235
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         264
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   BINDING         292
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01970"
SQ   SEQUENCE   425 AA;  47194 MW;  8BDA1A8D2351607D CRC64;
     MTLTAPRKHA IEQDQQDALA PYRNEFYLQE GSIYMDGNSL GLLSKRAEAT LLESLADWRE
     LGIDGWMKGR HPWFDLSEKL AALNAPLVGG RADEVMVTGS TTVNLHQLVA TFFAPSGRRT
     KILADSLTFP SDIYALQSQL RLRGLDPAEH LVQVESRDGR FLDEADIIAA MTDDIALIVL
     PTVLYRSGQI LDMERLTREA HARGILIGFD GCHSVGAIPH AFHDWGVDFA YWCNYKHLNG
     GPGTVGGLFV HERHFGTLPG LTGWFGSRKD KQFDMNHTMT PAENAAAFQI GTPHVLSLAP
     QIGALELFAE VGIDAVRAKS LALTDYMMTL VDQELTAYGF VIGNPRDAKR RGAHLSLEHP
     EAARICKALK AHQVIPDFRA PNIVRLAPVA LYNSFEDVYE VVSILKTIMD EKQYEQFKNE
     REVVA
//

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