CNPD3_MYCTO
ID CNPD3_MYCTO Reviewed; 318 AA.
AC P9WP64; L0T7J7; O06629; Q7D993;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=cAMP/cGMP dual specificity phosphodiesterase MT0825 {ECO:0000250|UniProtKB:P9WP65};
DE EC=3.1.4.16 {ECO:0000250|UniProtKB:P9WP65};
DE EC=3.1.4.17 {ECO:0000250|UniProtKB:P9WP65};
DE AltName: Full=2',3'-cyclic-nucleotide phosphodiesterase {ECO:0000250|UniProtKB:P9WP65};
DE AltName: Full=3',5'-cyclic-nucleotide phosphodiesterase {ECO:0000250|UniProtKB:P9WP65};
GN Name=icc {ECO:0000312|EMBL:AAK45067.1};
GN OrderedLocusNames=MT0825 {ECO:0000312|EMBL:AAK45067.1};
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity
CC for the second messengers cAMP and cGMP.
CC {ECO:0000250|UniProtKB:P9WP65}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000250|UniProtKB:P9WP65};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cyclophospho-AMP + H2O = 3'-AMP + H(+);
CC Xref=Rhea:RHEA:27886, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:60879, ChEBI:CHEBI:60880; EC=3.1.4.16;
CC Evidence={ECO:0000250|UniProtKB:P9WP65};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cyclophospho-GMP + H2O = 3'-GMP + H(+);
CC Xref=Rhea:RHEA:27858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:60732, ChEBI:CHEBI:60837; EC=3.1.4.16;
CC Evidence={ECO:0000250|UniProtKB:P9WP65};
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:0000250|UniProtKB:P9WP65};
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:0000250|UniProtKB:P9WP65};
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:0000250|UniProtKB:P9WP65};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P9WP65};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:P9WP65};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WP65};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P9WP65};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WP65}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WP65}. Cell
CC membrane {ECO:0000250|UniProtKB:P9WP65}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P9WP65}. Cell envelope
CC {ECO:0000250|UniProtKB:P9WP65}. Note=The C-terminal extension (CTE) is
CC necessary for the localization to the cell wall and cell envelope.
CC {ECO:0000250|UniProtKB:P9WP65}.
CC -!- DOMAIN: The C-terminal extension (CTE) is used to better adjust the
CC substrates into the active sites and mediates in vivo subcellular
CC localization of the protein. {ECO:0000250|UniProtKB:P9WP65}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK45067.1; -; Genomic_DNA.
DR PIR; F70536; F70536.
DR RefSeq; WP_003404120.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WP64; -.
DR SMR; P9WP64; -.
DR EnsemblBacteria; AAK45067; AAK45067; MT0825.
DR KEGG; mtc:MT0825; -.
DR HOGENOM; CLU_070320_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:RHEA.
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 3: Inferred from homology;
KW cAMP; Cell membrane; Cell wall; cGMP; Cytoplasm; Hydrolase; Iron;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Secreted.
FT CHAIN 1..318
FT /note="cAMP/cGMP dual specificity phosphodiesterase MT0825"
FT /id="PRO_0000427006"
FT REGION 278..318
FT /note="C-terminal extension"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 23
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 23
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 63
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 97..98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 207
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 209
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
SQ SEQUENCE 318 AA; 34233 MW; 7C1B683C5E375B3F CRC64;
MHRLRAAEHP RPDYVLLHIS DTHLIGGDRR LYGAVDADDR LGELLEQLNQ SGLRPDAIVF
TGDLADKGEP AAYRKLRGLV EPFAAQLGAE LVWVMGNHDD RAELRKFLLD EAPSMAPLDR
VCMIDGLRII VLDTSVPGHH HGEIRASQLG WLAEELATPA PDGTILALHH PPIPSVLDMA
VTVELRDQAA LGRVLRGTDV RAILAGHLHY STNATFVGIP VSVASATCYT QDLTVAAGGT
RGRDGAQGCN LVHVYPDTVV HSVIPLGGGE TVGTFVSPGQ ARRKIAESGI FIEPSRRDSL
FKHPPMVLTS SAPRSPVD
