(data stored in SCRATCH zone)

SWISSPROT: C5BHJ3_EDWI9

ID   C5BHJ3_EDWI9            Unreviewed;       440 AA.
AC   C5BHJ3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01628, ECO:0000256|SAAS:SAAS00035308};
DE            EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_01628, ECO:0000256|SAAS:SAAS00035322};
DE   AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_01628};
GN   Name=deoA {ECO:0000256|HAMAP-Rule:MF_01628};
GN   OrderedLocusNames=NT01EI_0563 {ECO:0000313|EMBL:ACR67792.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67792.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis
CC       of pyrimidine nucleosides are involved in the degradation of these
CC       compounds and in their utilization as carbon and energy sources,
CC       or in the rescue of pyrimidine bases for nucleotide synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01628, ECO:0000256|SAAS:SAAS00035301}.
CC   -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy-
CC       alpha-D-ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01628,
CC       ECO:0000256|SAAS:SAAS00035315}.
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage
CC       pathway; dTMP from thymine: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01628, ECO:0000256|SAAS:SAAS00035314}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01628,
CC       ECO:0000256|SAAS:SAAS00353857}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|HAMAP-Rule:MF_01628,
CC       ECO:0000256|SAAS:SAAS00547054}.
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DR   EMBL; CP001600; ACR67792.1; -; Genomic_DNA.
DR   RefSeq; WP_015869992.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0563; -.
DR   EnsemblBacteria; ACR67792; ACR67792; NT01EI_0563.
DR   GeneID; 7960331; -.
DR   KEGG; eic:NT01EI_0563; -.
DR   PATRIC; fig|634503.3.peg.508; -.
DR   eggNOG; ENOG4105CMW; Bacteria.
DR   eggNOG; COG0213; LUCA.
DR   HOGENOM; HOG000047313; -.
DR   KO; K00758; -.
DR   OMA; VHSIGGV; -.
DR   OrthoDB; POG091H02BC; -.
DR   UniPathway; UPA00578; UER00638.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0004645; F:phosphorylase activity; IEA:InterPro.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0046104; P:thymidine metabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   HAMAP; MF_01628; Thymid_phosp; 1.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   InterPro; IPR013465; Thymidine_Pase.
DR   PANTHER; PTHR10515; PTHR10515; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02643; T_phosphoryl; 1.
DR   TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHJ3.
DR   SWISS-2DPAGE; C5BHJ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01628,
KW   ECO:0000256|SAAS:SAAS00031988, ECO:0000313|EMBL:ACR67792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01628,
KW   ECO:0000256|SAAS:SAAS00031989, ECO:0000313|EMBL:ACR67792.1}.
FT   DOMAIN      350    424       PYNP_C. {ECO:0000259|SMART:SM00941}.
SQ   SEQUENCE   440 AA;  46824 MW;  FD7E45C2952F42A8 CRC64;
     MFLAQEIIRK KRDGRALSEE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MSMPERVALT
     MAMRDSGTVL DWNSLNLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYVP MISGRGLGHT
     GGTLDKLESI PGFDIFPDDS RFRSIIADIG VAIIGQTSSL APADKRFYAT RDITATVDSI
     PLITASILAK KLAEGLDALV MDVKVGSGAF MPTFELSEAL AQAIVGVANG AGCRTTALLT
     DMNQVLASSA GNALEVREAV QFLTGKARNP RLFEVTMALC VEMLISGKLA ADQTEARSKL
     QAVLDNGRAA EIFGRMVAAQ GGPRDFVERY DHYLPQAVLC KPVFAEQAGI ITAMDTRALG
     MSVVGLGGGR RQASDSIDYS VGLTDMVRLG DSVDGQRPLA VVHARDEASW QQAAEAVRAA
     VTLGGCVPEP TPVVYRRITQ
//

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