CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002521
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thymidine phosphorylase 
Protein Synonyms/Alias
 TdRPase 
Gene Name
 deoA 
Gene Synonyms/Alias
 tpp; ttg; b4382; JW4345 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
73SGTVLDWKSLHLNGPacetylation[1]
147NRFREIIKDVGVAIIacetylation[1]
165SSLAPADKRFYATRDacetylation[1]
190ITASILAKKLAEGLDacetylation[1]
291LISGKLAKDDAEARAacetylation[1]
299DDAEARAKLQAVLDNacetylation[1]
308QAVLDNGKAAEVFGRacetylation[1]
332DFVENYAKYLPTAMLacetylation[1]
405PLAVIHAKDENNWQEacetylation[1]
415NNWQEAAKAVKAAIKacetylation[1]
426AAIKLADKAPESTPTacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 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. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Glycosyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 440 AA 
Protein Sequence
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT 60
MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYIP MISGRGLGHT 120
GGTLDKLESI PGFDIFPDDN RFREIIKDVG VAIIGQTSSL APADKRFYAT RDITATVDSI 180
PLITASILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT 240
DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL 300
QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF VSEMDTRALG 360
MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA VIHAKDENNW QEAAKAVKAA 420
IKLADKAPES TPTVYRRISE 440 
Gene Ontology
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004645; F:phosphorylase activity; IEA:InterPro.
 GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
 GO:0009032; F:thymidine phosphorylase activity; IEA:EC.
 GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
 GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. 
Interpro
 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. 
Pfam
 PF02885; Glycos_trans_3N
 PF00591; Glycos_transf_3
 PF07831; PYNP_C 
SMART
 SM00941; PYNP_C 
PROSITE
 PS00647; THYMID_PHOSPHORYLASE 
PRINTS