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Database: UniProt
Entry: B8M8K3_TALSN
LinkDB: B8M8K3_TALSN
Original site: B8M8K3_TALSN 
ID   B8M8K3_TALSN            Unreviewed;       493 AA.
AC   B8M8K3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-NOV-2018, entry version 58.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
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=TSTA_037370 {ECO:0000313|EMBL:EED20516.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 /
OS   NRRL 1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20516.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomeA.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
CC         ECO:0000256|PIRNR:PIRNR038800};
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, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
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; EQ962654; EED20516.1; -; Genomic_DNA.
DR   RefSeq; XP_002480950.1; XM_002480905.1.
DR   ProteinModelPortal; B8M8K3; -.
DR   STRING; 441959.XP_002480950.1; -.
DR   EnsemblFungi; EED20516; EED20516; TSTA_037370.
DR   GeneID; 8100582; -.
DR   EuPathDB; FungiDB:TSTA_037370; -.
DR   eggNOG; KOG3846; Eukaryota.
DR   eggNOG; COG3844; LUCA.
DR   InParanoid; B8M8K3; -.
DR   OMA; AGWWGHD; -.
DR   OrthoDB; EOG092C20ON; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001745; 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:UP000001745};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:EED20516.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN      211    287       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      174    177       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     146    146       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
FT   BINDING     147    147       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     260    260       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     263    263       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     285    285       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     324    324       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     352    352       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   MOD_RES     286    286       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
SQ   SEQUENCE   493 AA;  55533 MW;  F9AC536F53777AAD CRC64;
     MGSRLHFQRI KEGPPLPHND DIRAYKREYA EALDEQDPLK SYRDQFIIPS KKDLLRKRLS
     DIEGDDESDP RCIYLCGNSL GLQPKNLRKY LDQYLRSWAI KGVTGHFVAH EDALLPPYLH
     VDDEGSKLLA PIVGASPSEV AVMGTLTGNI HILMSSFYRP TVERHKIILE GKAFPSDHYA
     IESQIRLHNF DPATSMVLIE PEDAEKPILS TKQILKVIDD NASDTMLILL PGIQFYTGQY
     FDIKTITAHA HSKGVLIGWD CAHAVGNVEL QLHDWEVDFA AWCHYKYVNS GPGAMAGLFV
     HEKHGKVNHS DTGDISYRPR LAGWWGHDKQ TRFQMDNKFI PQEGAAGYQI SNPSVLDLSA
     VASSLEIFNQ ATMPALRQKS LELTRYLEHL LLKYPLDDSS SSSNENTSEK PYTIITPSNP
     SERGAQLSIL LQPGLLDKVL EILEENGVVI DERKPNVVRV APVPLYNTFT DVWEFHRVFT
     LACRKAVKAR DGK
//
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