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Q8MLZ3 (PDE5_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:
cGMP-dependent 3',5'-cGMP phosphodiesterase A

EC=3.1.4.35
Alternative name(s):
Cyclic GMP-binding protein A
Phosphodiesterase 5
Short name=DdPDE5
Phosphodiesterase D
Gene names
Name:pdeD
Synonyms:gbpA, pde5
ORF Names:DDB_G0274383
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length867 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphodiesterase specific for cGMP, which is activated by cGMP but not by cAMP. Involved in the degradation of intracellular cGMP. Ref.5

Catalytic activity

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactor

Divalent metal cation. Can use manganese and to a lower extent magnesium and zinc. Half-maximal activation occurs between 10 and 100 µM of manganese whereas maximal activation occurs with 10 mM of zinc or magnesium. Ref.2

Subcellular location

Cytoplasmcytosol Ref.2 Ref.5 Ref.8.

Developmental stage

Expressed during growth and development, with the highest level of expression during aggregation. Ref.2

Domain

The beta lactamase-like domain catalyzes the hydrolysis of cGMP.

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. cNMP phosphodiesterase family.

Contains 2 cyclic nucleotide-binding domains.

Biophysicochemical properties

Kinetic parameters:

cAMP/cGMP selectivity of 0.003.

KM=5.2 µM for cGMP Ref.5 Ref.7

Vmax=390 pmol/min/mg enzyme

pH dependence:

Optimum pH is 7.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 867867cGMP-dependent 3',5'-cGMP phosphodiesterase A
PRO_0000353105

Regions

Nucleotide binding607 – 721115cNMP 1
Nucleotide binding734 – 851118cNMP 2
Region357 – 503147Phosphodiesterase activity
Compositional bias124 – 1274Poly-Ser
Compositional bias142 – 1454Poly-Ser
Compositional bias151 – 1544Poly-Gln
Compositional bias155 – 1584Poly-Pro
Compositional bias178 – 1858Poly-His
Compositional bias189 – 1968Poly-Asn
Compositional bias200 – 2034Poly-Asn
Compositional bias209 – 22113Poly-Gln

Sites

Metal binding3991Divalent metal cation Potential
Metal binding4011Divalent metal cation Potential
Metal binding4031Divalent metal cation Potential

Sequences

Sequence LengthMass (Da)Tools
Q8MLZ3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E203EED614E6F386

FASTA86797,992
        10         20         30         40         50         60 
MMFSKRKSIR FNPEGDYTEL PRGGYVVPSK LGGIQFGVPP ETIKDSMALK IDVPTIYVFP 

        70         80         90        100        110        120 
EELWDRKTGI NAAEAEFPAY FNYFILKRKV SFVCTKEQEQ RIRIVFQETL LGPPEFNTGI 

       130        140        150        160        170        180 
IINSSSSTTD TSKTSPIKKQ TSSSSPPLSP QQQQPPPPLV KQPSQQQLEE LATMDTCHYH 

       190        200        210        220        230        240 
HHHHHQEVND NDNNNNTTTN NNNIEILEQQ QQQQQQQQQQ QDEDSTDVDE EFQKEFSSTF 

       250        260        270        280        290        300 
PRSEIPNLEK ECKYLRTFNS VDELFDFILF DDNGIAKLSD DVEIHFQEDQ SLFKVLQFEE 

       310        320        330        340        350        360 
TGKGNKVQTL VATIPSKILF PDMINSISTI NDNKIFDPPT FGITIIGSSH GFDPKKSTTG 

       370        380        390        400        410        420 
FVLWINKRGI MVDPPLNSSS FLQSQGVPTR MVDHIILTHC HADHDSGTFQ KLLEEYQITV 

       430        440        450        460        470        480 
VTTPTILGSF LRKYGALSNL STDLLRRLFI FRPVMIGEPM IISGAEFRFF YTIHTIPTIS 

       490        500        510        520        530        540 
FEVFYGGKSI FYSGDTCYDP NRIKDMNKRG IMKTSRMKFF LRPWNHTVVL HEAGVPPIHT 

       550        560        570        580        590        600 
PVSVLRALPD EVKNRLYLVH ISEHTLPAGS GLKIAKEGVA HTLSLDVMKS SHSEAVDILK 

       610        620        630        640        650        660 
LVESVDIFRS IPLTQACEIL QTATKRKYSQ GSVIIARDTE PDAFYVVASG VVCVNIGELK 

       670        680        690        700        710        720 
KNLIVGDYFG EMSLVMGGLR SANVQAVTDV EVLSFNKEDF LSITRNSTES IQFITRLWEM 

       730        740        750        760        770        780 
RNEKSWETMS LNSVFSRCTN SQKTAIQSIL VRELIKKDET LWCKGEEALF GCLVAEGSFV 

       790        800        810        820        830        840 
FKEDDSLESF SQGSFLGDIN AMTTQPPSIH KTTVVAKEES VIYKVLSQDL IKFFSNNPGI 

       850        860 
QLAFLDTIFV DALRDQVQQL VNSKLTY 

« Hide

References

« Hide 'large scale' references
[1]"A novel cGMP signalling pathway mediating myosin phosphorylation and chemotaxis in Dictyostelium."
Bosgraaf L., Russcher H., Smith J.L., Wessels D., Soll D.R., Van Haastert P.J.M.
EMBO J. 21:4560-4570(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of a novel type of cGMP phosphodiesterase that is defective in the chemotactic stmF mutants."
Meima M.E., Biondi R.M., Schaap P.
Mol. Biol. Cell 13:3870-3877(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, COFACTOR, DEVELOPMENTAL STAGE.
[3]"Sequence and analysis of chromosome 2 of Dictyostelium discoideum."
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A.
Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[4]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[5]"Identification and characterization of two unusual cGMP-stimulated phoshodiesterases in dictyostelium."
Bosgraaf L., Russcher H., Snippe H., Bader S., Wind J., Van Haastert P.J.M.
Mol. Biol. Cell 13:3878-3889(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Identification of four candidate cGMP targets in Dictyostelium."
Goldberg J.M., Bosgraaf L., Van Haastert P.J.M., Smith J.L.
Proc. Natl. Acad. Sci. U.S.A. 99:6749-6754(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Characterization of a cAMP-stimulated cAMP phosphodiesterase in Dictyostelium discoideum."
Meima M.E., Weening K.E., Schaap P.
J. Biol. Chem. 278:14356-14362(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Seven Dictyostelium discoideum phosphodiesterases degrade three pools of cAMP and cGMP."
Bader S., Kortholt A., Van Haastert P.J.M.
Biochem. J. 402:153-161(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF481921 Genomic DNA. Translation: AAM34039.1.
AY047363 Genomic DNA. Translation: AAL06059.1.
AAFI02000012 Genomic DNA. Translation: EAL70084.1.
RefSeqXP_644314.1. XM_639222.1.

3D structure databases

ProteinModelPortalQ8MLZ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0185054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0185054; DDB0185054; DDB_G0274383.
GeneID8619742.
KEGGddi:DDB_G0274383.

Organism-specific databases

dictyBaseDDB_G0274383. pdeD.

Phylogenomic databases

eggNOGNOG70621.
OMAETIKDSM.
PhylomeDBQ8MLZ3.

Enzyme and pathway databases

BRENDA3.1.4.35. 1939.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 2 hits.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 2 hits.
SSF56281. SSF56281. 1 hit.
PROSITEPS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDE5_DICDI
AccessionPrimary (citable) accession number: Q8MLZ3
Secondary accession number(s): Q554K9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase