ID   CNPD3_NOSS1             Reviewed;         266 AA.
AC   Q8YLG0;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase alr5338 {ECO:0000305};
DE            EC=3.1.4.17 {ECO:0000269|Ref.2};
GN   OrderedLocusNames=alr5338;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   DOI=10.1264/jsme2.20.92;
RA   Fujisawa T., Ohmori M.;
RT   "Biochemical properties of a cAMP phosphodiesterase in the cyanobacterium
RT   Anabaena sp. strain PCC 7120.";
RL   Microbes Environ. 20:92-96(2005).
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. Can also hydrolyze cGMP.
CC       {ECO:0000269|Ref.2}.
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         Evidence={ECO:0000269|Ref.2};
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; Evidence={ECO:0000269|Ref.2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; Evidence={ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|Ref.2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|Ref.2};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- ACTIVITY REGULATION: Activated by iron and manganese.
CC       {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 uM for cAMP {ECO:0000269|Ref.2};
CC         Vmax=4.9 umol/min/mg enzyme with cAMP as substrate
CC         {ECO:0000269|Ref.2};
CC         Vmax=4.4 umol/min/mg enzyme with cGMP as substrate
CC         {ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000305}.
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DR   EMBL; BA000019; BAB77037.1; -; Genomic_DNA.
DR   PIR; AB2473; AB2473.
DR   RefSeq; WP_010999462.1; NZ_RSCN01000005.1.
DR   AlphaFoldDB; Q8YLG0; -.
DR   SMR; Q8YLG0; -.
DR   STRING; 103690.17134477; -.
DR   DNASU; 1108942; -.
DR   EnsemblBacteria; BAB77037; BAB77037; BAB77037.
DR   KEGG; ana:alr5338; -.
DR   eggNOG; COG1409; Bacteria.
DR   OMA; CAWLDQH; -.
DR   OrthoDB; 1242748at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd07402; MPP_GpdQ; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR026575; GpdQ/CpdA-like.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   cAMP; cGMP; Hydrolase; Iron; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..266
FT                   /note="3',5'-cyclic-nucleotide phosphodiesterase alr5338"
FT                   /id="PRO_0000413371"
FT   BINDING         14
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         16
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         16
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         56
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         86..87
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         155
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         196
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ   SEQUENCE   266 AA;  30432 MW;  46B3475509226736 CRC64;
     MNEKLPISIA QITDIHLLAS ESQRLQGIST TESFLAVMKR LEELRPELDL LLMTGDLSDD
     GTPESYENLQ HYLNSLQIAT YWLPGNHDCA IAMDKILNLG MVSRRKSFQR GNWNFILLNS
     SVTDCVYGYL SATTLDWLDS ELKMLPNNPT LIALHHPPLS VNSAWIDRSC LQNSQELFAV
     IDRYPQVKLV LFGHIHQEFR RQRHNVHYLG SPSTCYQFQS QSTTFAINQE LPGFRLLKLY
     ADGTWTTKIE RVPYSLPIEP TVTVSY