ID   CNPD3_COXBU             Reviewed;         248 AA.
AC   Q839Z9;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable cyclic nucleotide phosphodiesterase CBUA0032 {ECO:0000250|UniProtKB:P9WP65};
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:P9WP65};
GN   OrderedLocusNames=CBUA0032;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OG   Plasmid pQpH1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016829; AAO91608.1; -; Genomic_DNA.
DR   RefSeq; NP_819048.1; NC_004704.1.
DR   RefSeq; WP_011109651.1; NC_004704.2.
DR   AlphaFoldDB; Q839Z9; -.
DR   SMR; Q839Z9; -.
DR   STRING; 227377.CBUA0032; -.
DR   EnsemblBacteria; AAO91608; AAO91608; CBUA0032.
DR   GeneID; 1207862; -.
DR   KEGG; cbu:CBUA0032; -.
DR   PATRIC; fig|227377.7.peg.2122; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_0_0_6; -.
DR   OMA; GHVHNDY; -.
DR   Proteomes; UP000002671; Plasmid pQpH1.
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   GO; GO:0042545; P:cell wall modification; IBA:GO_Central.
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; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..248
FT                   /note="Probable cyclic nucleotide phosphodiesterase
FT                   CBUA0032"
FT                   /id="PRO_0000413366"
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         15
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         15
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         52
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         52
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         52
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         82..83
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         82
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         193
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ   SEQUENCE   248 AA;  29002 MW;  D37DD91AAE70BEB6 CRC64;
     MEDNCIKIAQ VSDLHLTSEN CETSRGRYSN AMNVFSAISL SGQHDMIFIT GDISDDYTEN
     SYKQLLEMLK KLTCRVFVIP GNHDDVNLMN KIIPEKYLFS PETVTSFNTF DFLFVNTVVN
     GEIHGLLTDQ DLSLFQNHLE NSGNKKKCII MHHNPIPLNR KIYDKYMLLN YQDFLRIICL
     YDNVKLVIFG HVHNDYTISY RQTLFSSAPA TCYQIKKFES DIIIEEKYGY KNYFLFEEFI
     ETNCIWIK