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A7ZVS5

- TYPH_ECO24

UniProt

A7ZVS5 - TYPH_ECO24

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Protein

Thymidine phosphorylase

Gene

deoA

Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed - 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-EC

GO - Biological processi

  1. pyrimidine nucleobase metabolic process Source: InterPro
  2. pyrimidine nucleoside metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciECOL331111:GH7P-4960-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:EcE24377A_4981
OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
Taxonomic identifieri331111 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001122: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Thymidine phosphorylasePRO_1000069659Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi331111.EcE24377A_4981.

Structurei

3D structure databases

ProteinModelPortaliA7ZVS5.
SMRiA7ZVS5. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0213.
HOGENOMiHOG000047313.
KOiK00758.
OMAiFINGVRD.
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.
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.

A7ZVS5-1 [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
VIHAKDENSW QEAAKAVKAA IKLADKAPES TPTVYRRISE
Length:440
Mass (Da):47,180
Last modified:October 23, 2007 - v1
Checksum:iB3BDF83C9275D2F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV17407.1.
RefSeqiYP_001465904.1. NC_009801.1.

Genome annotation databases

EnsemblBacteriaiABV17407; ABV17407; EcE24377A_4981.
GeneIDi5588086.
KEGGiecw:EcE24377A_4981.
PATRICi18299217. VBIEscCol31211_5175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV17407.1 .
RefSeqi YP_001465904.1. NC_009801.1.

3D structure databases

ProteinModelPortali A7ZVS5.
SMRi A7ZVS5. Positions 1-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331111.EcE24377A_4981.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV17407 ; ABV17407 ; EcE24377A_4981 .
GeneIDi 5588086.
KEGGi ecw:EcE24377A_4981.
PATRICi 18299217. VBIEscCol31211_5175.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00578 ; UER00638 .
BioCyci ECOL331111:GH7P-4960-MONOMER.

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

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E24377A / ETEC.

Entry informationi

Entry nameiTYPH_ECO24
AccessioniPrimary (citable) accession number: A7ZVS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: October 1, 2014
This is version 49 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

Documents

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

External Data

Dasty 3