ID   CNPD3_RUTMC             Reviewed;         234 AA.
AC   A1AWV4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Probable cyclic nucleotide phosphodiesterase Rmag_0669 {ECO:0000250|UniProtKB:P9WP65};
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:P9WP65};
GN   OrderedLocusNames=Rmag_0669;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthturnera.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q6XBH1};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000305}.
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DR   EMBL; CP000488; ABL02411.1; -; Genomic_DNA.
DR   RefSeq; WP_011738036.1; NC_008610.1.
DR   AlphaFoldDB; A1AWV4; -.
DR   SMR; A1AWV4; -.
DR   STRING; 413404.Rmag_0669; -.
DR   KEGG; rma:Rmag_0669; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_0_0_6; -.
DR   OrthoDB; 9784378at2; -.
DR   Proteomes; UP000002587; Chromosome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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   Hydrolase; Iron; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..234
FT                   /note="Probable cyclic nucleotide phosphodiesterase
FT                   Rmag_0669"
FT                   /id="PRO_0000413378"
FT   BINDING         11
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         13
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         13
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         49
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         49
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         49
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         79..80
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         186
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ   SEQUENCE   234 AA;  26547 MW;  75601DAEC907D5D5 CRC64;
     MMSHSFVQIS DCHIDNVEYA MGVNTHVNLK KIINKIINID TDALLISGDL THNGTITSYK
     TLQQILFPVQ IKLLVISGNH DIDNNLNTIF SKNLFSQFTL RKWEIISTNS VQTSKTSGFL
     TKNELKKLNF NLTQSIAKYI LIVLHHPIVP MNSTWDDSLS LENPKALFNV LDKYPKIQAI
     LFGHAHQAAE FSRLGVKIIS CPSTALQFNN ETRIGFNHYT LYDNGQLTID TQWI
//