ID F9T647_9VIBR Unreviewed; 273 AA.
AC F9T647;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000256|HAMAP-Rule:MF_00905};
DE Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE Short=cAMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE EC=3.1.4.53 {ECO:0000256|HAMAP-Rule:MF_00905};
GN Name=cpdA {ECO:0000256|HAMAP-Rule:MF_00905};
GN ORFNames=IX91_12495 {ECO:0000313|EMBL:AIW14989.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW14989.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW14989.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW14989.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role
CC in modulating the intracellular concentration of cAMP, thereby
CC influencing cAMP-dependent processes. {ECO:0000256|HAMAP-
CC Rule:MF_00905}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000256|ARBA:ARBA00025742, ECO:0000256|HAMAP-
CC Rule:MF_00905}.
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DR EMBL; CP009354; AIW14989.1; -; Genomic_DNA.
DR RefSeq; WP_004744980.1; NZ_CP009354.1.
DR AlphaFoldDB; F9T647; -.
DR STRING; 1051646.IX91_12495; -.
DR KEGG; vtu:IX91_12495; -.
DR PATRIC; fig|1051646.9.peg.2464; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_070320_0_0_6; -.
DR Proteomes; UP000030071; Chromosome 1.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd07402; MPP_GpdQ; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR HAMAP; MF_00905; cAMP_phosphodiest_CpdA; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR046379; cAMP_phosphodiest_CpdA.
DR InterPro; IPR026575; GpdQ/CpdA-like.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR42988:SF2; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CBUA0032-RELATED; 1.
DR PANTHER; PTHR42988; PHOSPHOHYDROLASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00905};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00905};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00905}.
FT DOMAIN 14..204
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 20
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 22
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 62
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 92..93
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 203
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
SQ SEQUENCE 273 AA; 30576 MW; 6EE67F3C56116031 CRC64;
MKVTSSSSNS DSIKLLQITD THLFEPVDGS LLSVNTLDSF NAVVAAIVEE NQSFDAVIST
GDISQDHTAE SYQRFERGIA PLKNTCFWLP GNHDFKPSMS SVLPSTQIKQ VEHVLLGEHW
QMVLLDSQVV GVPHGRLSDQ QLALLEDKLS QYPERNTLVL LHHHPILVGS RWLDQHTLKD
AHHFWEVVEK HSNVKAVLCG HVHQDMNVLH QGVRVMATPS TCVQFKPNSD DFALDTLSPG
WRELELHSDG QLTTQVKRLP YGSFQPDFNS AGY
//
