ID TYPH_CHRVO Reviewed; 441 AA.
AC Q7NRT0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 01-MAY-2013, entry version 75.
DE RecName: Full=Thymidine phosphorylase;
DE EC=2.4.2.4;
DE AltName: Full=TdRPase;
GN Name=deoA; OrderedLocusNames=CV_3700;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 /
OS NBRC 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC NCTC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M.,
RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S.,
RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A.,
RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M.,
RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O.,
RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L.,
RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A.,
RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P.,
RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S.,
RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M.,
RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C.,
RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O.,
RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P.,
RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E.,
RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N.,
RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C.,
RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L.,
RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T.,
RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy-
CC alpha-D-ribose 1-phosphate.
CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage
CC pathway; dTMP from thymine: step 1/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family.
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DR EMBL; AE016825; AAQ61362.1; -; Genomic_DNA.
DR RefSeq; NP_903370.1; NC_005085.1.
DR ProteinModelPortal; Q7NRT0; -.
DR SMR; Q7NRT0; 1-438.
DR STRING; 243365.CV_3700; -.
DR EnsemblBacteria; AAQ61362; AAQ61362; CV_3700.
DR GeneID; 2548212; -.
DR KEGG; cvi:CV_3700; -.
DR PATRIC; 21442227; VBIChrVio67196_3629.
DR eggNOG; COG0213; -.
DR HOGENOM; HOG000047313; -.
DR KO; K00758; -.
DR OMA; LMAIYFR; -.
DR ProtClustDB; PRK05820; -.
DR BioCyc; CVIO243365:GHUD-3699-MONOMER; -.
DR UniPathway; UPA00578; UER00638.
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:HAMAP.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0046104; P:thymidine metabolic process; IEA:HAMAP.
DR Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.90.1170.30; -; 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; IPR000053; Pyrmidine_PPase.
DR InterPro; IPR017872; Pyrmidine_PPase_CS.
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; Glyco_trans_3; 1.
DR SUPFAM; SSF52418; Glyco_trans_3; 1.
DR SUPFAM; SSF54680; PYNP_C; 1.
DR TIGRFAMs; TIGR02643; T_phosphoryl; 1.
DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycosyltransferase; Transferase.
FT CHAIN 1 441 Thymidine phosphorylase.
FT /FTId=PRO_0000059051.
SQ SEQUENCE 441 AA; 47055 MW; AB836251BC332CB6 CRC64;
MFLPQEIIRK KRDNLTLSQQ EIQQFVAGIT DNSVADSQIA ALAMAIYFNG MELEENVHLA
LAMRDSGRRM HWKDLNLPGP IVDKHSTGGV GDVVSLMLGP MVAACGGFVP MISGRGLGHT
GGTLDKLSAV PGYNPFPEPE LFRKVVKDVG VAIIGQTSDL APADRRFYAT RDVTATVESI
ALITASILSK KLAAGLDVLV MDVKAGSGAF MPTMQKSIEL AERIVKVGNG AGVATTALIT
EMSQPLASTA GNSIETREAV RYLKGDQRNP RLHEVTMALC AQMLIGGKLA ADEADARAKL
QAALDSGRAA EIFGRMVTAL GGPADFMEHY DRHLAPAPIM RPVYADRAGY VGAMDTRGIG
MAVCALGGGR RLATDVLDFR VGLSQFVELG QNIGKDTPLM MIHAADEASF EDAARRVKAA
IRIDEAAPSE LPLVYQIIRG E
//
