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Entry: A0A077ZA92_TRITR
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ID   A0A077ZA92_TRITR        Unreviewed;       787 AA.
AC   A0A077ZA92;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   05-DEC-2018, entry version 21.
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=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
GN   ORFNames=TTRE_0000559801 {ECO:0000313|EMBL:CDW57307.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57307.1, ECO:0000313|Proteomes:UP000030665};
RN   [1] {ECO:0000313|Proteomes:UP000030665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA   Schwartz K.J., Yoon K.;
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW57307.1, ECO:0000313|Proteomes:UP000030665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate
RT   host-pathogen interaction.";
RL   Submitted (MAR-2014) 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: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; HG806148; CDW57307.1; -; Genomic_DNA.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000030665; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; 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:0042853; P:L-alanine catabolic process; IEA:InterPro.
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   CDD; cd05305; L-AlaDH; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01970; Kynureninase; 1.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010111; Kynureninase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42795; PTHR42795; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00518; alaDH; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030665};
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:UP000030665}.
FT   DOMAIN      419    551       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      563    712       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   BINDING     100    100       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     208    208       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     211    211       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     233    233       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   BINDING     262    262       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_03017}.
FT   MOD_RES     234    234       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03017}.
SQ   SEQUENCE   787 AA;  86490 MW;  B9A138584A1E61A9 CRC64;
     MNTTFQTGLA YAKELDTKDE LHQYREDFFI QPGEIYMDGN SLGMASKAAV TSIEKMIERW
     KKEGVQAWND LYIYGEKISA LMAPLINAKP QEITVTGSTT SNIHSALATF YHPTKDRYKI
     LVDDLNFPTD RYAVDSMVEI KGYSIEEAVK VIRSADGEFI DEDAVIEAMT DDVAVILLPT
     VLYRSAQIID MKRLTEEAHK RGIIIGFDLC HAIGAIEIDF KEIQPDFAVW CTYKYLNGGL
     GSTAGLYINQ KHFDKKPGLA GWFGNRNDTQ FQLKHQFDPQ PDASGWQIGS PTIFSMAGLE
     GSLQIFNQLG MKKIRANSLN KTAYLMFLID KELADYGYSY GNSTDDKVRG GHVCLQHEEA
     YRIAAALRNN GVVPDFREPN VIRLAPIALY TSYEEINLVV QTLKKIVAEK IYEEYSNTRI
     PKEIKNNENR VALPPSGVFG LTNLGHKVLV ETKAGLGSAI TDKEYEEAGA TIVPDAMSAW
     AAEMVLKVKE PLAEEYRYFR KDLLLFTYLH LAANKPLTKA LLKAGVHSIA YENVQPADNS
     LPLLAPMSEI AGRMAAQIGA NFLERVNGGR GVLLSGVPGV ARGNVVVIGG GVVGMNAAKI
     AAGLGANVTI MDVSVPRLKQ LDLIFDGNIQ TLMSNSYNIQ EVLKTADLVI GAVLIPGHRA
     PTLVSKEMVS GMPFHSVIVD VAIDQGGIFE TTNKVTTHDN PTYIKENVVH YAVANMPGAV
     PQTATYALSN ATMEYVNLLA NNDLISLLKD NLALRRGLNT YNGKLTIEAV AIDLDLPYFP
     VNTALEA
//
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