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P07650

- TYPH_ECOLI

UniProt

P07650 - TYPH_ECOLI

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Protein
Thymidine phosphorylase
Gene
deoA, tpp, ttg, b4382, JW4345
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.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: EcoCyc
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:DEOA-MONOMER.
ECOL316407:JW4345-MONOMER.
MetaCyc:DEOA-MONOMER.
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: Chromosome, UP000000625: 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 phosphorylaseUniRule annotation
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP07650.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiFINGVRD.
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.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
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

MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD    50
MTMPERVSLT MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP 100
MVAACGGYIP MISGRGLGHT GGTLDKLESI PGFDIFPDDN RFREIIKDVG 150
VAIIGQTSSL APADKRFYAT RDITATVDSI PLITASILAK KLAEGLDALV 200
MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT DMNQVLASSA 250
GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL 300
QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF 350
VSEMDTRALG MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA 400
VIHAKDENNW QEAAKAVKAA IKLADKAPES TPTVYRRISE 440
Length:440
Mass (Da):47,207
Last modified:February 1, 1995 - v3
Checksum:i1DB3083C9275D2ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S56606.
RefSeqi NP_418799.1. NC_000913.3.
YP_492512.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AZY X-ray 3.00 A/B 2-440 [» ]
1OTP X-ray 2.80 A 2-440 [» ]
1TPT X-ray 2.80 A 2-440 [» ]
2TPT X-ray 2.60 A 2-440 [» ]
4EAD X-ray 1.50 A 2-440 [» ]
4EAF X-ray 1.55 A 2-440 [» ]
4LHM X-ray 1.52 A 2-440 [» ]
ProteinModelPortali P07650.
SMRi P07650. Positions 1-440.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-9426N.
IntActi P07650. 2 interactions.
STRINGi 511145.b4382.

Chemistry

BindingDBi P07650.
ChEMBLi CHEMBL3726.

Proteomic databases

PaxDbi P07650.
PRIDEi P07650.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77335 ; AAC77335 ; b4382 .
BAE78371 ; BAE78371 ; BAE78371 .
GeneIDi 12933785.
948901.
KEGGi ecj:Y75_p4266.
eco:b4382.
PATRICi 32124380. VBIEscCol129921_4530.

Organism-specific databases

EchoBASEi EB0215.
EcoGenei EG10219. deoA.

Phylogenomic databases

eggNOGi COG0213.
HOGENOMi HOG000047313.
KOi K00758.
OMAi FINGVRD.
OrthoDBi EOG61ZTGG.
PhylomeDBi P07650.

Enzyme and pathway databases

UniPathwayi UPA00578 ; UER00638 .
BioCyci EcoCyc:DEOA-MONOMER.
ECOL316407:JW4345-MONOMER.
MetaCyc:DEOA-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07650.
PROi P07650.

Gene expression databases

Genevestigatori P07650.

Family and domain databases

Gene3Di 3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPi MF_01628. Thymid_phosp.
InterProi IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013465. Thymidine_Pase.
[Graphical view ]
PANTHERi PTHR10515. PTHR10515. 1 hit.
Pfami PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000478. TP_PyNP. 1 hit.
SMARTi SM00941. PYNP_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsi TIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEi PS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1995) [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(2006) [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(1984) [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(1984) [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(1990) [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(1998) [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: April 1, 1988
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 143 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

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