P08331 (CPDB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 118.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase EC=3.1.3.6 EC=3.1.4.16 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 647 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2',3'-cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to the corresponding nucleoside and phosphate. Ref.1 |
| Catalytic activity | Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate. Ref.1 A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. Ref.1 |
| Cofactor | Divalent cations By similarity. |
| Subcellular location | |
| Miscellaneous | Two kinetically distinguishable active sites for the two substrates (2',3'-cyclic nucleotides and 3'-nucleotides) have been identified. |
| Sequence similarities | Belongs to the 5'-nucleotidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological process | nucleotide catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Inferred from electronic annotation. Source: EC 3'-nucleotidase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.6 | ||||||
| Chain | 20 – 647 | 628 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase | PRO_0000000035 | |||||
Regions | |||||||||
| Region | 544 – 550 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 31 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 33 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 76 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 76 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 116 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 225 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 257 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 259 | 1 | Divalent metal cation 1 By similarity | ||||||
| Binding site | 440 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 316 | 1 | A → G in AAA23597. Ref.1 | ||||||
| Sequence conflict | 528 – 552 | 25 | GKPID…GGKFA → ASRLIRTPCSWLPPITIALT GQIC in AAA23597. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and sequence analysis of the gene (cpdB) encoding periplasmic 2',3'-cyclic phosphodiesterase." Liu J., Burns D.M., Beacham I.R. J. Bacteriol. 165:1002-1010(1986) [PubMed: 3005231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. |
| [2] | "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: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Transcription and regulation of the cpdB gene in Escherichia coli K12 and Salmonella typhimurium LT2: evidence for modulation of constitutive promoters by cyclic AMP-CRP complex." Liu J., Beacham I.R. Mol. Gen. Genet. 222:161-165(1990) [PubMed: 2172762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. Strain: K12. |
| [6] | "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-31. Strain: K12 / EMG2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M13464 Genomic DNA. Translation: AAA23597.1. U14003 Genomic DNA. Translation: AAA97109.1. U00096 Genomic DNA. Translation: AAC77170.1. AP009048 Genomic DNA. Translation: BAE78214.1. X54008 Genomic DNA. Translation: CAA37954.1. |
| PIR | ESECPC. H65232. |
| RefSeq | NP_418634.1. NC_000913.2. |
3D structure databases | |
| ProteinModelPortal | P08331. |
| SMR | P08331. Positions 19-354. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-9311N. |
| IntAct | P08331. 2 interactions. |
| MINT | MINT-1228170. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000003401; EBESCP00000003401; EBESCG00000002787. EBESCT00000014549; EBESCP00000013840; EBESCG00000013610. |
| GeneID | 948729. |
| GenomeReviews | Gene locus JW4171 in contig AP009048_GR. Gene locus b4213 in contig U00096_GR. |
| KEGG | ecj:JW4171. eco:b4213. |
| PATRIC | 32124001. VBIEscCol129921_4345. |
Organism-specific databases | |
| EchoBASE | EB0158. |
| EcoGene | EG10160. cpdB. |
Phylogenomic databases | |
| eggNOG | COG0737. |
| GeneTree | EBGT00050000009523. |
| HOGENOM | HBG510269. |
| OMA | DHDATRE. |
| ProtClustDB | PRK09420. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:CPDB-MONOMER. MetaCyc:CPDB-MONOMER. |
Gene expression databases | |
| Genevestigator | P08331. |
Family and domain databases | |
| InterPro | IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR006294. Cyc_nuc_PDE_nucleotidase. IPR004843. Metallo_PEstase_dom. [Graphical view] |
| Gene3D | G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit. |
| KO | K01119. |
| PANTHER | PTHR11575. 5_nucleotidase. 1 hit. |
| Pfam | PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view] |
| PRINTS | PR01607. APYRASEFAMLY. |
| SUPFAM | SSF55816. 5'-Nucleotdase_C. 1 hit. |
| TIGRFAMs | TIGR01390. CycNucDiestase. 1 hit. |
| PROSITE | PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CPDB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P08331 Secondary accession number(s): Q2M692 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

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