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Database: UniProt
Entry: G3JC48_CORMM
LinkDB: G3JC48_CORMM
Original site: G3JC48_CORMM 
ID   G3JC48_CORMM            Unreviewed;       547 AA.
AC   G3JC48;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   05-DEC-2018, entry version 42.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
GN   Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
GN   ORFNames=CCM_02834 {ECO:0000313|EMBL:EGX94563.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94563.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX94563.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX94563.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H.,
RA   Huang Y., Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris,
RT   a valued traditional Chinese medicine.";
RL   Genome Biol. 12:R116-R116(2011).
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:0000256|HAMAP-Rule:MF_03017}.
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:0000256|HAMAP-
CC         Rule:MF_03017};
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:0000256|HAMAP-Rule:MF_03017};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03017};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_03017}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03017}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
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DR   EMBL; JH126400; EGX94563.1; -; Genomic_DNA.
DR   RefSeq; XP_006668049.1; XM_006667986.1.
DR   EnsemblFungi; EGX94563; EGX94563; CCM_02834.
DR   GeneID; 18164861; -.
DR   KEGG; cmt:CCM_02834; -.
DR   InParanoid; G3JC48; -.
DR   KO; K01556; -.
DR   OrthoDB; EOG092C20ON; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001610; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 {ECO:0000313|Proteomes:UP000001610};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN      186    357       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      244    247       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     216    216       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     217    217       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     328    328       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     331    331       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     353    353       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     394    394       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     422    422       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   MOD_RES     354    354       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
SQ   SEQUENCE   547 AA;  59925 MW;  20F17DDE035FD67F CRC64;
     MRRQRDAYKL GPWKPPPSSL PAALIPLRLP VPIGATCRRR SRLLSTTTAS VAAPSMDLPA
     YVERLRGGAP AKFPADANSL PFAQTLDSQD ALRHLRYEFV LPTKTSIKKT ALDGTLPSTA
     QTRTNGASTT NGTAPEEDPD VGIYFVGNSL GAQPKAVRRY IDAQLETWAS IGVNGHFKTL
     ENSPLTQWQD MAEACAQQSA DLVGASPNEI VIMNTLTVNL HMMMASFYKP DAKRHKIILE
     WRPFPSDYYA IESQIVWHGL DPATSMVKIE PDANSYMSTE TILAAIDANA DDTALLLLPG
     IQYYSGQLLD MPTITKYAHA RGIVVGWDLA HAAGNVELRL HDWDVDFACW CTYKYINAGP
     GAIAGAFVHE RHGRVEWPAG PDAAPTYRPR LTGWYGGDKS VRFNMDNKFV PTPGAGGYQA
     SNPSALELAN LAGALSVFNK TTMRDLRSKA LVLTAYAEHL LDGILADAEG DAPFRILTPR
     DPLQRGTQLS VMLRDGLLDD VTAALELNGV LCDKRKPGVI RVAPVPLYSR FEDVWRFMQI
     LRGALKL
//
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