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C9RR52 (CPDA_FIBSS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. 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:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Short name=3',5'-cyclic AMP phosphodiesterase
Short name=cAMP phosphodiesterase
EC=3.1.4.17
Gene names
Name:cpdA
Ordered Locus Names:Fisuc_1441, FSU_1912
OrganismFibrobacter succinogenes (strain ATCC 19169 / S85) [Complete proteome] [HAMAP]
Taxonomic identifier59374 [NCBI]
Taxonomic lineageBacteriaFibrobacteresFibrobacteralesFibrobacteraceaeFibrobacter

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes By similarity. HAMAP-Rule MF_00905

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. HAMAP-Rule MF_00905

Cofactor

Binds 2 metal cations per subunit By similarity. HAMAP-Rule MF_00905

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Sequence caution

The sequence ACX75038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   LigandcAMP
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2562563',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413368

Regions

Nucleotide binding89 – 902cAMP By similarity

Sites

Metal binding201Metal cation 1 By similarity
Metal binding221Metal cation 1 By similarity
Metal binding591Metal cation 1 By similarity
Metal binding591Metal cation 2 By similarity
Metal binding891Metal cation 2 By similarity
Metal binding1561Metal cation 2 By similarity
Metal binding1961Metal cation 2 By similarity
Metal binding1981Metal cation 1 By similarity
Binding site221cAMP By similarity
Binding site591cAMP By similarity
Binding site1981cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
C9RR52 [UniParc].

Last modified October 19, 2011. Version 2.
Checksum: 136B36E74CCA0D3A

FASTA25629,186
        10         20         30         40         50         60 
MYILRSCMEK KVLKIGQISD AHIGDDDRLV QDIDVRKNFL TAYNSESMKD LDLLVLSGDL 

        70         80         90        100        110        120 
ADNASTDAYS FIAGVIKDSK VPVCIIPGNH DNLEVMEKVF DLKDKVHNGK CYYRYDLDGR 

       130        140        150        160        170        180 
SIFFLDSADG TVSSDQLSWL EQETAKIDGE VLLFLHHPPC LCGHKFMDLR YSMKNIAEVQ 

       190        200        210        220        230        240 
ATLSKIKNLK HIFVGHYHSE MTIQLEDKTV YVTPSTQMQI DPNITVFCLS SAAPRWRLIE 

       250 
WGENFMETKV YFSNTP 

« Hide

References

[1]"Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J. expand/collapse author list , Stevenson D.M., Boyum J., Brumm P.I., Mead D.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19169 / S85.
[2]"Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85."
Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B., Russell J.B., Cann I.K.O., Mackie R.I., White B.A.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19169 / S85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001792 Genomic DNA. Translation: ACX75038.1. Different initiation.
CP002158 Genomic DNA. Translation: ADL25604.1.
RefSeqYP_003249520.1. NC_013410.1.
YP_005821847.1. NC_017448.1.

3D structure databases

ProteinModelPortalC9RR52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59374.Fisuc_1441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX75038; ACX75038; Fisuc_1441.
ADL25604; ADL25604; FSU_1912.
GeneID12433470.
8522047.
KEGGfsc:FSU_1912.
fsu:Fisuc_1441.
PATRIC32142651. VBIFibSuc28982_1412.
43021265. VBIFibSuc28982203727_1844.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
KOK03651.
OrthoDBEOG6QG8GQ.

Family and domain databases

HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR024654. Calcineurin-like_PHP_lpxH.
IPR026575. cAMP_Pdiest_CpdA.
[Graphical view]
PfamPF12850. Metallophos_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDA_FIBSS
AccessionPrimary (citable) accession number: C9RR52
Secondary accession number(s): D9SBF1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 24 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