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P44685 (CPDA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:icc
Ordered Locus Names:HI_0399
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length274 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. May coordinate responses to nutritional stress, ensuring optimal competence development. Ref.2

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

Disruption phenotype

Mutants show increased levels of cellular cAMP. Ref.2

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2742743',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000084148

Regions

Nucleotide binding93 – 942cAMP By similarity

Sites

Metal binding211Metal cation 1 By similarity
Metal binding231Metal cation 1 By similarity
Metal binding631Metal cation 1 By similarity
Metal binding631Metal cation 2 By similarity
Metal binding931Metal cation 2 By similarity
Metal binding1631Metal cation 2 By similarity
Metal binding2021Metal cation 2 By similarity
Metal binding2041Metal cation 1 By similarity
Binding site231cAMP By similarity
Binding site631cAMP By similarity
Binding site2041cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P44685 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A810BF2072CA4957

FASTA27431,556
        10         20         30         40         50         60 
MKNTFVYQAE KPVIKLLQIT DPHLFKDESA ELLGVNTQAS FAQVLKEIQQ ENNEFDVILA 

        70         80         90        100        110        120 
TGDLVQDSSD EGYIRFVEMM KPFNKPVFWI PGNHDFQPKM AEFLNQPPMN AAKHLLLGEH 

       130        140        150        160        170        180 
WQALLLDSQV YGVPHGQLSQ HQLDLLKETL GKNPERYTLV VLHHHLLPTN SAWLDQHNLR 

       190        200        210        220        230        240 
NSHELAEVLA PFTNVKAILY GHIHQEVNSE WNGYQVMATP ATCIQFKPDC QYFSLDTLQP 

       250        260        270 
GWREIELHSD GSIRTEVKRI QQAEFFPNMQ EEGY 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"A 3',5' cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and optimizes competence in Haemophilus influenzae Rd."
Macfadyen L.P., Ma C., Redfield R.J.
J. Bacteriol. 180:4401-4405(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22058.1.
PIRE64065.
RefSeqNP_438561.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0399.

Protocols and materials databases

DNASU949501.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22058; AAC22058; HI_0399.
GeneID949501.
KEGGhin:HI0399.
PATRIC20189349. VBIHaeInf48452_0418.

Phylogenomic databases

eggNOGCOG1409.
KOK03651.
OMAWREIELH.
OrthoDBEOG6QG8GQ.
PhylomeDBP44685.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR013622. Calcineurin-like_phos_C.
IPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProDomPD587589. Calcineurin-like_phos_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCPDA_HAEIN
AccessionPrimary (citable) accession number: P44685
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 84 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names