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cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (EC 3.1.4.35) (EC 3.1.4.53) (Cyclic GMP-binding protein B) (Phosphodiesterase 6) (DdPDE6) (Phosphodiesterase E)

 PDE6_DICDI              Reviewed;        1096 AA.
Q8MM62; Q552E1;
25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
28-MAR-2018, entry version 91.
RecName: Full=cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B;
EC=3.1.4.35;
EC=3.1.4.53;
AltName: Full=Cyclic GMP-binding protein B;
AltName: Full=Phosphodiesterase 6;
Short=DdPDE6;
AltName: Full=Phosphodiesterase E;
Name=pdeE; Synonyms=gbpB, pde6; ORFNames=DDB_G0276027;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12011437; DOI=10.1073/pnas.102167299;
Goldberg J.M., Bosgraaf L., Van Haastert P.J.M., Smith J.L.;
"Identification of four candidate cGMP targets in Dictyostelium.";
Proc. Natl. Acad. Sci. U.S.A. 99:6749-6754(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
COFACTOR.
PubMed=12574165; DOI=10.1074/jbc.M209648200;
Meima M.E., Weening K.E., Schaap P.;
"Characterization of a cAMP-stimulated cAMP phosphodiesterase in
Dictyostelium discoideum.";
J. Biol. Chem. 278:14356-14362(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
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.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
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.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[5]
FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
DEVELOPMENTAL STAGE.
PubMed=12198158; DOI=10.1093/emboj/cdf438;
Bosgraaf L., Russcher H., Smith J.L., Wessels D., Soll D.R.,
Van Haastert P.J.M.;
"A novel cGMP signalling pathway mediating myosin phosphorylation and
chemotaxis in Dictyostelium.";
EMBO J. 21:4560-4570(2002).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
PubMed=12429832; DOI=10.1091/mbc.E02-05-0302;
Bosgraaf L., Russcher H., Snippe H., Bader S., Wind J.,
Van Haastert P.J.M.;
"Identification and characterization of two unusual cGMP-stimulated
phoshodiesterases in dictyostelium.";
Mol. Biol. Cell 13:3878-3889(2002).
[7]
SUBCELLULAR LOCATION.
PubMed=17040207; DOI=10.1042/BJ20061153;
Bader S., Kortholt A., Van Haastert P.J.M.;
"Seven Dictyostelium discoideum phosphodiesterases degrade three pools
of cAMP and cGMP.";
Biochem. J. 402:153-161(2007).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:12198158, ECO:0000269|PubMed:12429832,
ECO:0000269|PubMed:12574165}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12574165};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12574165};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12574165};
Note=Divalent metal cation. Can use Mn(2+) or, to a lower extent,
Mg(2+) or Zn(2+). Half-maximal activation occurs between 10 and
100 uM of Mn(2+) whereas maximal activation occurs with 10 mM of
Zn(2+) or Mg(2+). {ECO:0000269|PubMed:12574165};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=200 uM for cAMP {ECO:0000269|PubMed:12198158,
ECO:0000269|PubMed:12429832};
KM=800 uM for cGMP {ECO:0000269|PubMed:12198158,
ECO:0000269|PubMed:12429832};
Vmax=650 nmol/min/mg enzyme with cAMP as substrate
{ECO:0000269|PubMed:12198158, ECO:0000269|PubMed:12429832};
Vmax=300 nmol/min/mg enzyme with cGMP as substrate
{ECO:0000269|PubMed:12198158, ECO:0000269|PubMed:12429832};
Note=cAMP/cGMP selectivity of 9.;
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:12198158,
ECO:0000269|PubMed:12429832};
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000305|PubMed:12198158, ECO:0000305|PubMed:17040207}.
-!- DEVELOPMENTAL STAGE: Low expression during growth. Mainly
expressed after 8-10 hours of starvation when cells are
aggregating and in the multicellular stage.
{ECO:0000269|PubMed:12198158, ECO:0000269|PubMed:12429832,
ECO:0000269|PubMed:12574165}.
-!- DOMAIN: The beta lactamase-like domain catalyzes the hydrolysis of
cGMP. {ECO:0000250}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
cNMP phosphodiesterase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF481922; AAM34040.1; -; Genomic_DNA.
EMBL; AY047364; AAL06060.1; -; Genomic_DNA.
EMBL; AAFI02000014; EAL69313.1; -; Genomic_DNA.
RefSeq; XP_643272.1; XM_638180.1.
ProteinModelPortal; Q8MM62; -.
SMR; Q8MM62; -.
STRING; 44689.DDB0185220; -.
PaxDb; Q8MM62; -.
EnsemblProtists; EAL69313; EAL69313; DDB_G0276027.
GeneID; 8620315; -.
KEGG; ddi:DDB_G0276027; -.
dictyBase; DDB_G0276027; pdeE.
InParanoid; Q8MM62; -.
OMA; LSHINSC; -.
SABIO-RK; Q8MM62; -.
PRO; PR:Q8MM62; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; TAS:dictyBase.
GO; GO:0005622; C:intracellular; TAS:dictyBase.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:dictyBase.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IGI:dictyBase.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IMP:dictyBase.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:dictyBase.
GO; GO:0019934; P:cGMP-mediated signaling; IMP:dictyBase.
GO; GO:0072697; P:protein localization to cell cortex; IGI:dictyBase.
GO; GO:0061118; P:regulation of positive chemotaxis to cAMP; IMP:dictyBase.
CDD; cd00038; CAP_ED; 2.
Gene3D; 2.60.120.10; -; 2.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00100; cNMP; 2.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF51206; SSF51206; 3.
SUPFAM; SSF56281; SSF56281; 1.
PROSITE; PS50042; CNMP_BINDING_3; 2.
1: Evidence at protein level;
cAMP; cAMP-binding; cGMP; cGMP-binding; Complete proteome; Cytoplasm;
Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
Reference proteome; Repeat; Zinc.
CHAIN 1 1096 cAMP/cGMP-dependent 3',5'-cAMP/cGMP
phosphodiesterase B.
/FTId=PRO_0000353106.
NP_BIND 783 930 cNMP 1.
NP_BIND 946 1070 cNMP 2.
COMPBIAS 214 218 Poly-Ser.
COMPBIAS 241 245 Poly-Gln.
COMPBIAS 457 460 Poly-Ser.
METAL 573 573 Divalent metal cation. {ECO:0000255}.
METAL 575 575 Divalent metal cation. {ECO:0000255}.
METAL 577 577 Divalent metal cation. {ECO:0000255}.
SEQUENCE 1096 AA; 124924 MW; 4F4F8CF199223782 CRC64;
MNSKYGDNII DFLRYLEKFV KSLTKDNKIE EFKTFDIKSL LYPRNKDYFG NLSKFLLAVI
SARIGSNFIN EDDIFEISEL LKEFLGQELE HLPYLSYEEL YVEIVEQVGE INGTVSEIIE
AITVTIDFLD TFEKVSQTID RSNEKQKLLA YLSAPVNQLD NSVSGVFNEN DYTDIQRFFT
ELTNENNQSP DSNISILIND FQSLLNILES QQASSSSSKM IINDSPRTQQ RNGTTEQQKK
QQQQQYLQKN KEPFYSKDKI MQVSGPSYVF TPSDCNVSIQ VGIPPDTLKR DQSICHFIVP
HFLISKDVSL SEVEFPIFYN KFVQKGKTKV VIICTVEQKQ RIETILCESI FGPAPEHIYT
DEEITIPDYK IDLLTERLAI DPRANDEKLD SYVIFKTFDT FGVVDIDLPS ASDPTKLINL
RIRNTKGLIS FHEDYHVVQK QLHLKLQEQQ QDQQDKSSSS TTDKQMINTS GNRIILKNNT
VSVIDSTIES QYVPVLPFGN DHEQVKKFKA PILGVTFLGV SHGLDFTHCS HTTGFIIWIN
GSGVVVDPPV GNTTYLQTNG IYGKTVEHII LTHCHADHDS GILQKIIERN KVTLYTTKTI
NESYMRKLKA LTGLPEQSLK NYYTWVPVTI GNKIKILGAE FEFDYSFHVI PTIRFKLEIY
NKKISYSADT FYDLQKFKQL KDQGVLSKKR IERLKSFVFD ADMIIHESGV APIHTPMANL
LELPSEIRKK IRVVHCSSSV DTKGEIIRPK EGLENTEIIK VDRKYKGVAE CIQIQTALNH
CSVFSKLSPA EVQRVFFLCK KIWVKRNDVI IKKGSPSDMF YIILSGKVLV YENEYEPIKS
TTSVGTVVTD TTTITTTVKT DAIKIPTIKL CAGETLGESA LQLDKNIDAS ATVIAETDVC
LLVWKTMDLR TEFHSNLNTF ISKVHMDLSH INSCRDAIIR AFQHNITQHI NKEEVDSIAN
GSKDVSFAHH QVIFNEGDTS DSMYIIKQGR VRIHSKKNKN IIRYLNVGDF FGETAYRRSN
EDSNFLPTRS FTATAIDPTI LLKLDIESIV NPRIQNIIEQ KAKKNAEDNI RYHAYSPKIR
TPRTPRKVYP IEGLSI


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