CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004495
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoribosyl 1,2-cyclic phosphodiesterase 
Protein Synonyms/Alias
 Phosphoribosyl cyclic phosphodiesterase 
Gene Name
 phnP 
Gene Synonyms/Alias
 b4092; JW4053 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
171DTAGLPEKTLKFLRNacetylation[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
 Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate. 
Sequence Annotation
 METAL 21 21 Zinc.
 METAL 23 23 Zinc.
 METAL 26 26 Zinc.
 METAL 76 76 Manganese 1; via tele nitrogen.
 METAL 78 78 Manganese 1; via pros nitrogen.
 METAL 80 80 Manganese 2.
 METAL 81 81 Manganese 2; via tele nitrogen.
 METAL 143 143 Manganese 1; via tele nitrogen.
 METAL 164 164 Manganese 1.
 METAL 164 164 Manganese 2.
 METAL 222 222 Manganese 2; via tele nitrogen.
 METAL 225 225 Zinc; via pros nitrogen.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Manganese; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 252 AA 
Protein Sequence
MSLTLTLTGT GGAQGVPAWG CECAACARAR RSPQYRRQPC SGVVKFNDAI TLIDAGLHDL 60
ADRWSPGSFQ QFLLTHYHMD HVQGLFPLRW GVGDPIPVYG PPDEQGCDDL FKHPGLLDFS 120
HTVEPFVVFD LQGLQVTPLP LNHSKLTFGY LLETAHSRVA WLSDTAGLPE KTLKFLRNNQ 180
PQVMVMDCSH PPRADAPRNH CDLNTVLALN QVIRSPRVIL THISHQFDAW LMENALPSGF 240
EVGFDGMEIG VA 252 
Gene Ontology
 GO:0030145; F:manganese ion binding; IDA:EcoCyc.
 GO:0008081; F:phosphoric diester hydrolase activity; IDA:EcoCyc.
 GO:0019700; P:organic phosphonate catabolic process; IMP:EcoCyc. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR017693; Phosphonate_metab_PhnP. 
Pfam
  
SMART
 SM00849; Lactamase_B 
PROSITE
  
PRINTS