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Database: UniProt/SWISS-PROT
Entry: KYNU_SHEWM
LinkDB: KYNU_SHEWM
Original site: KYNU_SHEWM 
ID   KYNU_SHEWM              Reviewed;         430 AA.
AC   B1KJM4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 66.
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};
GN   OrderedLocusNames=Swoo_1405;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-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.
CC       {ECO:0000255|HAMAP-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;
CC         EC=3.7.1.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate +
CC         H(+) + 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-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from 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.
CC       {ECO:0000255|HAMAP-Rule:MF_01970}.
DR   EMBL; CP000961; ACA85697.1; -; Genomic_DNA.
DR   RefSeq; WP_012324043.1; NC_010506.1.
DR   ProteinModelPortal; B1KJM4; -.
DR   SMR; B1KJM4; -.
DR   STRING; 392500.Swoo_1405; -.
DR   EnsemblBacteria; ACA85697; ACA85697; Swoo_1405.
DR   KEGG; swd:Swoo_1405; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242438; -.
DR   KO; K01556; -.
DR   OMA; AGWWGHD; -.
DR   OrthoDB; 1474443at2; -.
DR   BioCyc; SWOO392500:G1GBD-1537-MONOMER; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000002168; 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;
KW   Complete proteome; Hydrolase; Pyridine nucleotide biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    430       Kynureninase.
FT                                /FTId=PRO_0000357012.
FT   REGION      133    136       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     105    105       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
FT   BINDING     106    106       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     218    218       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     221    221       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     243    243       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     274    274       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     302    302       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   430 AA;  48545 MW;  BCF6BDB84CF10CDC CRC64;
     MIFENTLAFA QQQDRNDPLA HYSDQFHHPV IDGKEVLYFT GNSLGLQPKT AKEHINQELE
     DWAKWGVEGH FHAVNPWVSY HEILTPASAE LVGANESEVV CMNSLTTNLH LLFVSFYKPT
     AKRFKIISEA KMFPSDRYLL ETQVRHHGLD PDDAIIEISP REGEYLIREE DIIAAVNDNA
     DELALLFFGG VNYFTGQLFD MQRLTKAAHG VGALAGFDLA HAVGNVPMHL HDWDVDFAAW
     CTYKYLNSSA GNVGGIFVND RHGNNTKINR FGGWWGHNKE RRFLMENSFE PMTGAEGWQI
     SNAPVMGMAI LKSSLDIFHE AGIENLRAKS LKLTAYLEFV FNDIVNQFTD IKLEIITPTD
     PTQRGCQLSI KLVGTNKEFF EALTKAGVIA DFREPDVIRL APTPLYNSFE DVYLLGQTLK
     VLAQNWRQHG
//
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