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P53052 (CPDB_YEREN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase

EC=3.1.3.6
EC=3.1.4.16
Gene names
Name:cpdB
OrganismYersinia enterocolitica
Taxonomic identifier630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate.

A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Divalent cations By similarity.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processnucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2',3'-cyclic-nucleotide 2'-phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3'-nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 6526282',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
PRO_0000000038

Regions

Region549 – 5557Substrate binding By similarity

Sites

Metal binding361Divalent metal cation 1 By similarity
Metal binding381Divalent metal cation 1 By similarity
Metal binding811Divalent metal cation 1 By similarity
Metal binding811Divalent metal cation 2 By similarity
Metal binding1211Divalent metal cation 2 By similarity
Metal binding2301Divalent metal cation 2 By similarity
Metal binding2621Divalent metal cation 2 By similarity
Metal binding2641Divalent metal cation 1 By similarity
Binding site4451Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P53052 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8781369575794E17

FASTA65271,492
        10         20         30         40         50         60 
MFKRPLTLSL LASLIALTTS TAQAATVDLR VLETTDLHSN MMDFDYYKDK PTEKFGLVRT 

        70         80         90        100        110        120 
ASLIEAARQQ ATNSVLVDNG DLIQGSPLGD YMAAKGLKAG EIHPVYKAMN TLDYAVGNIG 

       130        140        150        160        170        180 
NHEFNYGLDY LKKSLAGAKF PYVNANVIDV KTGKPLFQPY LIVDTPVKDR DGKNHNLRIG 

       190        200        210        220        230        240 
YIGFGPPQVM IWDKANLTGK VTVDDITETA KKWVPEMRKQ GANLVVAIPH SGLSSDPYKT 

       250        260        270        280        290        300 
MAENSVYYLS QVPGIDAIMF GHAHAVFPSK DFATIKGADI AQGTLNGIPA VMPGQWGDHL 

       310        320        330        340        350        360 
GVVDFVLNND QGQWQVTQAK AEARPIFDKA TQKSLAAENA NLMKVLAADH QGTRDFVSQP 

       370        380        390        400        410        420 
IGTASDNMYS YLSLIQDDPT VQIVNNAQRA YTEHFIQGDP DLADLPVLSA AAPFKAGGRK 

       430        440        450        460        470        480 
NDPASFVEVE KGELTFRNAA DLYLYPNTLV VVKASGADVK QWLECSAAQF NQIDVNSSKP 

       490        500        510        520        530        540 
QSLINWDSFR TYNFDVIDGV NYEIDVSQPA RYDGECALIN DKAERIKNLT FNGKPIDPQA 

       550        560        570        580        590        600 
TFLIGTNNYR AYSGKFAGTG DSHIAFASPD ENRAVLSAYI SAETKKHGQV TPQADNNWRL 

       610        620        630        640        650 
ATLNSQQPLD IRFETSPSTK AAEFIKQKAQ YPMKAMGTDE IGFAVFKIDL QK 

« Hide

References

[1]Truelzsch K.S.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 51871 / WA-314 / Serotype O:8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85742 Genomic DNA. Translation: CAA59745.1.
PIRS52695.

3D structure databases

ProteinModelPortalP53052.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.4.16. 6741.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR006294. Cyc_nuc_PDE_nucleotidase.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsTIGR01390. CycNucDiestase. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDB_YEREN
AccessionPrimary (citable) accession number: P53052
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families