ID   CPDP_ALIFS              Reviewed;         330 AA.
AC   Q56686;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase;
DE            Short=3':5'-CNP;
DE            Short=PDEase;
DE            EC=3.1.4.17;
DE   Flags: Precursor;
GN   Name=cpdP;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-1;
RX   PubMed=8393003; DOI=10.1128/jb.175.15.4615-4624.1993;
RA   Dunlap P.V., Callahan S.M.;
RT   "Characterization of a periplasmic 3':5'-cyclic nucleotide
RT   phosphodiesterase gene, cpdP, from the marine symbiotic bacterium Vibrio
RT   fischeri.";
RL   J. Bacteriol. 175:4615-4624(1993).
CC   -!- FUNCTION: Seems to allow the organism to grow on cAMP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-II
CC       family. {ECO:0000305}.
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DR   EMBL; L11527; AAA27513.1; -; Genomic_DNA.
DR   PIR; A40602; A40602.
DR   AlphaFoldDB; Q56686; -.
DR   SMR; Q56686; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:InterPro.
DR   CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR024225; cAMP-PdiesteraseII_CS.
DR   InterPro; IPR000396; Pdiesterase2.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR28283; PTHR28283; 2.
DR   Pfam; PF02112; PDEase_II; 1.
DR   PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
DR   PRINTS; PR00388; PDIESTERASE2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS00607; PDEASE_II; 1.
PE   3: Inferred from homology;
KW   cAMP; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..330
FT                   /note="3',5'-cyclic-nucleotide phosphodiesterase"
FT                   /id="PRO_0000023354"
SQ   SEQUENCE   330 AA;  36089 MW;  B87127EE2CE213D4 CRC64;
     MFKNKLAVLF TCLSVFSFSA QSGSFDTVTL GSKGGIQDGN LTAFLIKSEA DSNFVMLDAG
     SVVNGLIVSE QKGAFKDITV PDSSPYTKVG YLLKDRIKGY FISHAHLDHV AGLIISSPDD
     SKKPIYGLAA TNKDLMKNYF NWSAWPNFGN KGEGFKLNKY NYVDLQPGVW SPVAETTMSV
     VSLPLSHSGG QSTVFILKDS EGDVFAYFGD TGPDEVEKSS AMRTAWSVLA PFVKQGKLKG
     IIIEVSFTNE TPDKSLFGHL TPNWLVKELS VLEDMNGKGS LKDLNVAISH IKYSLKNSED
     PKVIIKKQLV EVNDLGVNFI FPEQGDSLQF