ID   CNPD3_RHOE4             Reviewed;         301 AA.
AC   C1A2D8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable cyclic nucleotide phosphodiesterase RER_40650 {ECO:0000250|UniProtKB:P9WP65};
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:P9WP65};
GN   OrderedLocusNames=RER_40650;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008957; BAH34773.1; -; Genomic_DNA.
DR   RefSeq; WP_020908405.1; NC_012490.1.
DR   AlphaFoldDB; C1A2D8; -.
DR   SMR; C1A2D8; -.
DR   STRING; 234621.RER_40650; -.
DR   EnsemblBacteria; BAH34773; BAH34773; RER_40650.
DR   KEGG; rer:RER_40650; -.
DR   PATRIC; fig|234621.6.peg.4600; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_1_0_11; -.
DR   OMA; CAWLDQH; -.
DR   Proteomes; UP000002204; 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   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   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..301
FT                   /note="Probable cyclic nucleotide phosphodiesterase
FT                   RER_40650"
FT                   /id="PRO_0000413376"
FT   BINDING         20
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         22
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         22
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         61
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         95..96
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         207
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ   SEQUENCE   301 AA;  32343 MW;  BA8DC406C6774B8F CRC64;
     MSVRSAEYPR PKHFLVHLSD THLVAQGELY DAVDASTRLR EVLSGIVASG ARPDALIFTG
     DLTDQGHPDA YAELKAIVEP VAAEIDAQVI WAMGNHDDRS TFRSLLLGED ATDHPVDNVY
     DLDGLRVITL DSSVPGHHYG EISDRQLDWL RSELAVPAPD GTILALHHPP VPCIQDLAVL
     VELRDQSRLA DVLRGSDVRA ILAGHLHYST TATFAGIPVS VASSTCYTQD LNVEVGGQRG
     RDGAQGCNLV HVYDETIVHS VVPLGAHVTV GEPVDADEGA RRLSAAGIRI LESEKAGRSI
     V