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Protein

Thymidine phosphorylase

Gene

deoA

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.UniRule annotation

Catalytic activityi

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. pyrimidine-nucleoside phosphorylase activity Source: InterPro
  3. thymidine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyrimidine nucleobase metabolic process Source: InterPro
  2. thymidine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciCVIO243365:GHUD-3795-MONOMER.
UniPathwayiUPA00578; UER00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine phosphorylaseUniRule annotation (EC:2.4.2.4UniRule annotation)
Alternative name(s):
TdRPaseUniRule annotation
Gene namesi
Name:deoAUniRule annotation
Ordered Locus Names:CV_3700
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
ProteomesiUP000001424 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Thymidine phosphorylasePRO_0000059051Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243365.CV_3700.

Structurei

3D structure databases

ProteinModelPortaliQ7NRT0.
SMRiQ7NRT0. Positions 1-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiCGLAVPM.
OrthoDBiEOG61ZTGG.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPiMF_01628. Thymid_phosp.
InterProiIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR017872. Pyrmidine_PPase_CS.
IPR000053. Thymidine/pyrmidine_PPase.
IPR013465. Thymidine_Pase.
[Graphical view]
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7NRT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLPQEIIRK KRDNLTLSQQ EIQQFVAGIT DNSVADSQIA ALAMAIYFNG
60 70 80 90 100
MELEENVHLA LAMRDSGRRM HWKDLNLPGP IVDKHSTGGV GDVVSLMLGP
110 120 130 140 150
MVAACGGFVP MISGRGLGHT GGTLDKLSAV PGYNPFPEPE LFRKVVKDVG
160 170 180 190 200
VAIIGQTSDL APADRRFYAT RDVTATVESI ALITASILSK KLAAGLDVLV
210 220 230 240 250
MDVKAGSGAF MPTMQKSIEL AERIVKVGNG AGVATTALIT EMSQPLASTA
260 270 280 290 300
GNSIETREAV RYLKGDQRNP RLHEVTMALC AQMLIGGKLA ADEADARAKL
310 320 330 340 350
QAALDSGRAA EIFGRMVTAL GGPADFMEHY DRHLAPAPIM RPVYADRAGY
360 370 380 390 400
VGAMDTRGIG MAVCALGGGR RLATDVLDFR VGLSQFVELG QNIGKDTPLM
410 420 430 440
MIHAADEASF EDAARRVKAA IRIDEAAPSE LPLVYQIIRG E
Length:441
Mass (Da):47,055
Last modified:December 15, 2003 - v1
Checksum:iAB836251BC332CB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ61362.1.
RefSeqiNP_903370.1. NC_005085.1.
WP_011137247.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ61362; AAQ61362; CV_3700.
KEGGicvi:CV_3700.
PATRICi21442227. VBIChrVio67196_3629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ61362.1.
RefSeqiNP_903370.1. NC_005085.1.
WP_011137247.1. NC_005085.1.

3D structure databases

ProteinModelPortaliQ7NRT0.
SMRiQ7NRT0. Positions 1-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_3700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ61362; AAQ61362; CV_3700.
KEGGicvi:CV_3700.
PATRICi21442227. VBIChrVio67196_3629.

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiCGLAVPM.
OrthoDBiEOG61ZTGG.

Enzyme and pathway databases

UniPathwayiUPA00578; UER00638.
BioCyciCVIO243365:GHUD-3795-MONOMER.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPiMF_01628. Thymid_phosp.
InterProiIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR017872. Pyrmidine_PPase_CS.
IPR000053. Thymidine/pyrmidine_PPase.
IPR013465. Thymidine_Pase.
[Graphical view]
PANTHERiPTHR10515. PTHR10515. 1 hit.
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000478. TP_PyNP. 1 hit.
SMARTiSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsiTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEiPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Entry informationi

Entry nameiTYPH_CHRVO
AccessioniPrimary (citable) accession number: Q7NRT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 15, 2003
Last modified: April 29, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.