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P26265 (CPDB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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
Ordered Locus Names:STM4403
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length647 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.

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 6476282',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
PRO_0000000036

Regions

Region544 – 5507Substrate binding By similarity

Sites

Metal binding311Divalent metal cation 1 By similarity
Metal binding331Divalent metal cation 1 By similarity
Metal binding761Divalent metal cation 1 By similarity
Metal binding761Divalent metal cation 2 By similarity
Metal binding1161Divalent metal cation 2 By similarity
Metal binding2251Divalent metal cation 2 By similarity
Metal binding2571Divalent metal cation 2 By similarity
Metal binding2591Divalent metal cation 1 By similarity
Binding site4401Substrate By similarity

Experimental info

Sequence conflict511G → A in CAA37956. Ref.2
Sequence conflict84 – 896GDYMAA → RLYGG in CAA37956. Ref.2
Sequence conflict96 – 983DVH → GIQ in CAA37956. Ref.2
Sequence conflict1331A → G in CAA37956. Ref.2
Sequence conflict1741I → N in CAA37956. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26265 [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: E9F7FE7D6681DB34

FASTA64770,517
        10         20         30         40         50         60 
MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIH 

        70         80         90        100        110        120 
AARNEVKNSV LVDNGDLIQG SPLGDYMAAK GLKDGDVHPV YKALNTLDYA VGNLGNHEFN 

       130        140        150        160        170        180 
YGLDYLHNAL AGAKFPYVNA NIIDVKTQKP LFTPYLIKET SVIDKDGNPQ TLKIGYIGFV 

       190        200        210        220        230        240 
PPQIMIWDKA NLSGKVTVND ITETARKYVP EMREKGADIV VVIAHSGLSA DPYHSMAENS 

       250        260        270        280        290        300 
VYYLSEVPGV DAIMFGHAHA VFPGKDFADI KGADIAKGTL NGIPAVMPGM WGDHLGVVDL 

       310        320        330        340        350        360 
VLNNDSGKWQ VTQAKAEARP IYDAAAKKSL AAEDSKLVGI LKADHDATRE FVSKPIGKSA 

       370        380        390        400        410        420 
DNMYSYLALV QDDPTVQVVN NAQKAYVEHF IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS 

       430        440        450        460        470        480 
FVEVEKGQLT FRNAADLYLY PNTLVVVKAS GKEVKEWLEC SAGQFNQIDI HSNKPQSLIN 

       490        500        510        520        530        540 
WDGFRTYNFD VIDGVNYQID VSQPARYDGE CQMVNPQAER IKNLTFNGKP VDPNATFLVA 

       550        560        570        580        590        600 
TNNYRAYGGK FAGTGDSHIA FASPDENRAV LAAWIGAESK RAGEIHPAAD NNWRLAPIHS 

       610        620        630        640 
DTALDIRFET SPGDKAAAFI KAKGQYPMKK VAVDDIGFAI YQVDLSK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
Strain: LT2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL23223.1.
X54009 Genomic DNA. Translation: CAA37956.1.
PIRS11915.
RefSeqNP_463264.1. NC_003197.1.

3D structure databases

ProteinModelPortalP26265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4403.

Proteomic databases

PaxDbP26265.
PRIDEP26265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23223; AAL23223; STM4403.
GeneID1255929.
KEGGstm:STM4403.
PATRIC32387729. VBISalEnt20916_4628.

Phylogenomic databases

eggNOGCOG0737.
HOGENOMHOG000248800.
KOK01119.
OMAMVWDKAN.
OrthoDBEOG696BW0.
ProtClustDBPRK09420.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4435-MONOMER.

Family and domain databases

Gene3D3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR006294. Cyc_nuc_PDE_nucleotidase.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 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_SALTY
AccessionPrimary (citable) accession number: P26265
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 13, 2001
Last modified: April 16, 2014
This is version 114 of the entry and version 2 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