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Protein

Thymidine phosphorylase

Gene

deoA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. pyrimidine nucleobase metabolic process Source: InterPro
  3. thymidine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:DEOA-MONOMER.
ECOL316407:JW4345-MONOMER.
MetaCyc:DEOA-MONOMER.
BRENDAi2.4.2.4. 2026.
UniPathwayiUPA00578; UER00638.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine phosphorylase (EC:2.4.2.4)
Alternative name(s):
TdRPase
Gene namesi
Name:deoA
Synonyms:tpp, ttg
Ordered Locus Names:b4382, JW4345
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10219. deoA.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Thymidine phosphorylasePRO_0000059054Add
BLAST

Proteomic databases

PaxDbiP07650.
PRIDEiP07650.

Expressioni

Gene expression databases

GenevestigatoriP07650.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ygjKP425921EBI-909674,EBI-1121018

Protein-protein interaction databases

DIPiDIP-9426N.
IntActiP07650. 2 interactions.
STRINGi511145.b4382.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129Combined sources
Helixi19 – 3012Combined sources
Helixi36 – 4914Combined sources
Helixi53 – 6412Combined sources
Helixi73 – 753Combined sources
Beta strandi81 – 866Combined sources
Helixi94 – 10411Combined sources
Beta strandi108 – 1125Combined sources
Turni117 – 1193Combined sources
Helixi123 – 1275Combined sources
Helixi139 – 14911Combined sources
Beta strandi150 – 1545Combined sources
Helixi162 – 17110Combined sources
Turni172 – 1754Combined sources
Helixi180 – 19213Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi209 – 2135Combined sources
Helixi214 – 23017Combined sources
Beta strandi234 – 2418Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi250 – 2523Combined sources
Helixi253 – 26311Combined sources
Helixi270 – 28617Combined sources
Helixi293 – 30513Combined sources
Helixi308 – 31912Combined sources
Helixi326 – 3338Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi349 – 3546Combined sources
Helixi356 – 36510Combined sources
Turni366 – 3683Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi382 – 3854Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi399 – 4068Combined sources
Helixi407 – 42014Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi433 – 4386Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZYX-ray3.00A/B2-440[»]
1OTPX-ray2.80A2-440[»]
1TPTX-ray2.80A2-440[»]
2TPTX-ray2.60A2-440[»]
4EADX-ray1.50A2-440[»]
4EAFX-ray1.55A2-440[»]
4LHMX-ray1.52A2-440[»]
ProteinModelPortaliP07650.
SMRiP07650. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07650.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
InParanoidiP07650.
KOiK00758.
OMAiDWVVDAY.
OrthoDBiEOG61ZTGG.
PhylomeDBiP07650.

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.

P07650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD
60 70 80 90 100
MTMPERVSLT MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP
110 120 130 140 150
MVAACGGYIP MISGRGLGHT GGTLDKLESI PGFDIFPDDN RFREIIKDVG
160 170 180 190 200
VAIIGQTSSL APADKRFYAT RDITATVDSI PLITASILAK KLAEGLDALV
210 220 230 240 250
MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT DMNQVLASSA
260 270 280 290 300
GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL
310 320 330 340 350
QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF
360 370 380 390 400
VSEMDTRALG MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA
410 420 430 440
VIHAKDENNW QEAAKAVKAA IKLADKAPES TPTVYRRISE
Length:440
Mass (Da):47,207
Last modified:January 31, 1995 - v3
Checksum:i1DB3083C9275D2ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97278.1.
U00096 Genomic DNA. Translation: AAC77335.1.
AP009048 Genomic DNA. Translation: BAE78371.1.
X00742 Genomic DNA. Translation: CAA25324.1.
X03224 Genomic DNA. Translation: CAA26975.1.
PIRiS56606.
RefSeqiNP_418799.1. NC_000913.3.
YP_492512.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77335; AAC77335; b4382.
BAE78371; BAE78371; BAE78371.
GeneIDi12933785.
948901.
KEGGiecj:Y75_p4266.
eco:b4382.
PATRICi32124380. VBIEscCol129921_4530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97278.1.
U00096 Genomic DNA. Translation: AAC77335.1.
AP009048 Genomic DNA. Translation: BAE78371.1.
X00742 Genomic DNA. Translation: CAA25324.1.
X03224 Genomic DNA. Translation: CAA26975.1.
PIRiS56606.
RefSeqiNP_418799.1. NC_000913.3.
YP_492512.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZYX-ray3.00A/B2-440[»]
1OTPX-ray2.80A2-440[»]
1TPTX-ray2.80A2-440[»]
2TPTX-ray2.60A2-440[»]
4EADX-ray1.50A2-440[»]
4EAFX-ray1.55A2-440[»]
4LHMX-ray1.52A2-440[»]
ProteinModelPortaliP07650.
SMRiP07650. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9426N.
IntActiP07650. 2 interactions.
STRINGi511145.b4382.

Chemistry

BindingDBiP07650.
ChEMBLiCHEMBL3726.

Proteomic databases

PaxDbiP07650.
PRIDEiP07650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77335; AAC77335; b4382.
BAE78371; BAE78371; BAE78371.
GeneIDi12933785.
948901.
KEGGiecj:Y75_p4266.
eco:b4382.
PATRICi32124380. VBIEscCol129921_4530.

Organism-specific databases

EchoBASEiEB0215.
EcoGeneiEG10219. deoA.

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
InParanoidiP07650.
KOiK00758.
OMAiDWVVDAY.
OrthoDBiEOG61ZTGG.
PhylomeDBiP07650.

Enzyme and pathway databases

UniPathwayiUPA00578; UER00638.
BioCyciEcoCyc:DEOA-MONOMER.
ECOL316407:JW4345-MONOMER.
MetaCyc:DEOA-MONOMER.
BRENDAi2.4.2.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP07650.
PROiP07650.

Gene expression databases

GenevestigatoriP07650.

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

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The internal regulated promoter of the deo operon of Escherichia coli K-12."
    Valentin-Hansen P., Hammer K., Larsen J.E.L., Svendsen I.
    Nucleic Acids Res. 12:5211-5224(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-440.
    Strain: K12.
  5. "Structure and function of the intercistronic regulatory deoC-deoA element of Escherichia coli K-12."
    Valentin-Hansen P., Hammer-Jespersen K., Boetius F., Svendsen I.
    EMBO J. 3:179-183(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
  6. "Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8-A resolution."
    Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E.
    J. Biol. Chem. 265:14016-14022(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  7. "Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase."
    Pugmire M.J., Cook W.J., Jasanoff A., Walter M.R., Ealick S.E.
    J. Mol. Biol. 281:285-299(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiTYPH_ECOLI
AccessioniPrimary (citable) accession number: P07650
Secondary accession number(s): Q2M5T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1988
Last sequence update: January 31, 1995
Last modified: March 31, 2015
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.