(data stored in ACNUC7421 zone)

SWISSPROT: C3MF66_SINFN

ID   C3MF66_SINFN            Unreviewed;       268 AA.
AC   C3MF66;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000256|HAMAP-Rule:MF_00905};
DE            Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE            Short=cAMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE            EC=3.1.4.53 {ECO:0000256|HAMAP-Rule:MF_00905};
GN   Name=cpdA {ECO:0000256|HAMAP-Rule:MF_00905};
GN   OrderedLocusNames=NGR_c01000 {ECO:0000313|EMBL:ACP23903.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23903.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23903.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory
CC       role in modulating the intracellular concentration of cAMP,
CC       thereby influencing cAMP-dependent processes. {ECO:0000256|HAMAP-
CC       Rule:MF_00905}.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00905}.
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC       Note=Binds 2 metal cations per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00905};
CC   -!- SIMILARITY: Belongs to the cAMP phosphodiesterase class-III
CC       family. {ECO:0000256|HAMAP-Rule:MF_00905}.
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DR   EMBL; CP001389; ACP23903.1; -; Genomic_DNA.
DR   RefSeq; WP_012706688.1; NC_012587.1.
DR   RefSeq; YP_002824656.1; NC_012587.1.
DR   ProteinModelPortal; C3MF66; -.
DR   STRING; 394.NGR_c01000; -.
DR   EnsemblBacteria; ACP23903; ACP23903; NGR_c01000.
DR   GeneID; 7790679; -.
DR   KEGG; rhi:NGR_c01000; -.
DR   PATRIC; fig|394.7.peg.2894; -.
DR   eggNOG; ENOG4108X4D; Bacteria.
DR   eggNOG; COG1409; LUCA.
DR   HOGENOM; HOG000238352; -.
DR   KO; K03651; -.
DR   OMA; AAPNHEG; -.
DR   OrthoDB; POG091H05L5; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP.
DR   CDD; cd07402; MPP_GpdQ; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_00905; cAMP_phophodiest_CpdA; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR026575; cAMP_Pdiest_CpdA.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MF66.
DR   SWISS-2DPAGE; C3MF66.
KW   cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        3    201       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   NP_BIND      80     81       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   METAL         9      9       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        11     11       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        50     50       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        50     50       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        80     80       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       159    159       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       198    198       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       200    200       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   BINDING      11     11       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING      50     50       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING     200    200       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
SQ   SEQUENCE   268 AA;  29884 MW;  075E71890BE55EEB CRC64;
     MTKFIIFTDL HMVPEGMSII GIDPYRRLAA GIQHVNRYHA DADRVIFAGD LAHGADRASY
     ERLKALLGEL DPPAAIMIGN HDRREAFLEV FDEAATDASG FVQQVIDFAD CRAILLDTLF
     APPYDYPVSH AGYLCDRRLA WLDRQLASAA DRPVLIFMHH PPHITGFIGI DMFRLINEED
     FYGLVRRHGN VRHIFAGHVH RTISGSSRGI PFSVFKSPVH QQPMPFDIPD ASLSVDEPAA
     YGIALVTRDG VLVHTEDYEI AKRDAAVA
//

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