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Q8MM62

- PDE6_DICDI

UniProt

Q8MM62 - PDE6_DICDI

Protein

cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B

Gene

pdeE

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Dual specificity cAMP and cGMP phosphodiesterase with marked preference for cyclic AMP, which is activated by cAMP and cGMP. Likely functions as a cAMP-stimulated cAMP-phosphodiesterase which may play a role in regulating the cAMP relay response.3 Publications

    Catalytic activityi

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

    Cofactori

    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.1 Publication

    Kineticsi

    cAMP/cGMP selectivity of 9.

    1. KM=200 µM for cAMP2 Publications
    2. KM=800 µM for cGMP2 Publications

    Vmax=650 nmol/min/mg enzyme with cAMP as substrate2 Publications

    Vmax=300 nmol/min/mg enzyme with cGMP as substrate2 Publications

    pH dependencei

    Optimum pH is 7.0.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi573 – 5731Divalent metal cationSequence Analysis
    Metal bindingi575 – 5751Divalent metal cationSequence Analysis
    Metal bindingi577 – 5771Divalent metal cationSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi783 – 930148cNMP 1Add
    BLAST
    Nucleotide bindingi946 – 1070125cNMP 2Add
    BLAST

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: dictyBase
    2. 3',5'-cyclic-GMP phosphodiesterase activity Source: dictyBase
    3. cAMP binding Source: UniProtKB-KW
    4. cGMP binding Source: UniProtKB-KW
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP catabolic process Source: dictyBase
    2. cGMP catabolic process Source: dictyBase

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cAMP-binding, cGMP, cGMP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (EC:3.1.4.35, EC:3.1.4.53)
    Alternative name(s):
    Cyclic GMP-binding protein B
    Phosphodiesterase 6
    Short name:
    DdPDE6
    Phosphodiesterase E
    Gene namesi
    Name:pdeE
    Synonyms:gbpB, pde6
    ORF Names:DDB_G0276027
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0276027. pdeE.

    Subcellular locationi

    Cytoplasmcytosol 2 Publications

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. intracellular Source: dictyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10961096cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase BPRO_0000353106Add
    BLAST

    Expressioni

    Developmental stagei

    Low expression during growth. Mainly expressed after 8-10 hours of starvation when cells are aggregating and in the multicellular stage.3 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0185220.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8MM62.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi214 – 2185Poly-Ser
    Compositional biasi241 – 2455Poly-Gln
    Compositional biasi457 – 4604Poly-Ser

    Domaini

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

    Sequence similaritiesi

    Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG70621.
    OMAiLSHINSC.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    3.60.15.10. 1 hit.
    InterProiIPR001279. Beta-lactamas-like.
    IPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 2 hits.
    [Graphical view]
    SMARTiSM00100. cNMP. 2 hits.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 3 hits.
    SSF56281. SSF56281. 1 hit.
    PROSITEiPS50042. CNMP_BINDING_3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8MM62-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSKYGDNII DFLRYLEKFV KSLTKDNKIE EFKTFDIKSL LYPRNKDYFG     50
    NLSKFLLAVI SARIGSNFIN EDDIFEISEL LKEFLGQELE HLPYLSYEEL 100
    YVEIVEQVGE INGTVSEIIE AITVTIDFLD TFEKVSQTID RSNEKQKLLA 150
    YLSAPVNQLD NSVSGVFNEN DYTDIQRFFT ELTNENNQSP DSNISILIND 200
    FQSLLNILES QQASSSSSKM IINDSPRTQQ RNGTTEQQKK QQQQQYLQKN 250
    KEPFYSKDKI MQVSGPSYVF TPSDCNVSIQ VGIPPDTLKR DQSICHFIVP 300
    HFLISKDVSL SEVEFPIFYN KFVQKGKTKV VIICTVEQKQ RIETILCESI 350
    FGPAPEHIYT DEEITIPDYK IDLLTERLAI DPRANDEKLD SYVIFKTFDT 400
    FGVVDIDLPS ASDPTKLINL RIRNTKGLIS FHEDYHVVQK QLHLKLQEQQ 450
    QDQQDKSSSS TTDKQMINTS GNRIILKNNT VSVIDSTIES QYVPVLPFGN 500
    DHEQVKKFKA PILGVTFLGV SHGLDFTHCS HTTGFIIWIN GSGVVVDPPV 550
    GNTTYLQTNG IYGKTVEHII LTHCHADHDS GILQKIIERN KVTLYTTKTI 600
    NESYMRKLKA LTGLPEQSLK NYYTWVPVTI GNKIKILGAE FEFDYSFHVI 650
    PTIRFKLEIY NKKISYSADT FYDLQKFKQL KDQGVLSKKR IERLKSFVFD 700
    ADMIIHESGV APIHTPMANL LELPSEIRKK IRVVHCSSSV DTKGEIIRPK 750
    EGLENTEIIK VDRKYKGVAE CIQIQTALNH CSVFSKLSPA EVQRVFFLCK 800
    KIWVKRNDVI IKKGSPSDMF YIILSGKVLV YENEYEPIKS TTSVGTVVTD 850
    TTTITTTVKT DAIKIPTIKL CAGETLGESA LQLDKNIDAS ATVIAETDVC 900
    LLVWKTMDLR TEFHSNLNTF ISKVHMDLSH INSCRDAIIR AFQHNITQHI 950
    NKEEVDSIAN GSKDVSFAHH QVIFNEGDTS DSMYIIKQGR VRIHSKKNKN 1000
    IIRYLNVGDF FGETAYRRSN EDSNFLPTRS FTATAIDPTI LLKLDIESIV 1050
    NPRIQNIIEQ KAKKNAEDNI RYHAYSPKIR TPRTPRKVYP IEGLSI 1096
    Length:1,096
    Mass (Da):124,924
    Last modified:October 1, 2002 - v1
    Checksum:i4F4F8CF199223782
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF481922 Genomic DNA. Translation: AAM34040.1.
    AY047364 Genomic DNA. Translation: AAL06060.1.
    AAFI02000014 Genomic DNA. Translation: EAL69313.1.
    RefSeqiXP_643272.1. XM_638180.1.

    Genome annotation databases

    EnsemblProtistsiDDB0185220; DDB0185220; DDB_G0276027.
    GeneIDi8620315.
    KEGGiddi:DDB_G0276027.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF481922 Genomic DNA. Translation: AAM34040.1 .
    AY047364 Genomic DNA. Translation: AAL06060.1 .
    AAFI02000014 Genomic DNA. Translation: EAL69313.1 .
    RefSeqi XP_643272.1. XM_638180.1.

    3D structure databases

    ProteinModelPortali Q8MM62.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0185220.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0185220 ; DDB0185220 ; DDB_G0276027 .
    GeneIDi 8620315.
    KEGGi ddi:DDB_G0276027.

    Organism-specific databases

    dictyBasei DDB_G0276027. pdeE.

    Phylogenomic databases

    eggNOGi NOG70621.
    OMAi LSHINSC.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    3.60.15.10. 1 hit.
    InterProi IPR001279. Beta-lactamas-like.
    IPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR014710. RmlC-like_jellyroll.
    [Graphical view ]
    Pfami PF00027. cNMP_binding. 2 hits.
    [Graphical view ]
    SMARTi SM00100. cNMP. 2 hits.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51206. SSF51206. 3 hits.
    SSF56281. SSF56281. 1 hit.
    PROSITEi PS50042. CNMP_BINDING_3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, COFACTOR.
    3. 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.
      , 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. "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: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE.
    6. "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, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE.
    7. "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.

    Entry informationi

    Entry nameiPDE6_DICDI
    AccessioniPrimary (citable) accession number: Q8MM62
    Secondary accession number(s): Q552E1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3