(data stored in ACNUC7421 zone)

SWISSPROT: C5B6Y1_EDWI9

ID   C5B6Y1_EDWI9            Unreviewed;       275 AA.
AC   C5B6Y1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
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=NT01EI_0200 {ECO:0000313|EMBL:ACR67443.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67443.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67443.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67443.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+);
CC         Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53;
CC         Evidence={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; CP001600; ACR67443.1; -; Genomic_DNA.
DR   RefSeq; WP_015869654.1; NC_012779.2.
DR   EnsemblBacteria; ACR67443; ACR67443; NT01EI_0200.
DR   GeneID; 7958788; -.
DR   KEGG; eic:NT01EI_0200; -.
DR   PATRIC; fig|634503.3.peg.177; -.
DR   eggNOG; ENOG41070EG; Bacteria.
DR   eggNOG; COG1409; LUCA.
DR   HOGENOM; HOG000238351; -.
DR   KO; K03651; -.
DR   OMA; CAWLDQH; -.
DR   OrthoDB; 1242748at2; -.
DR   BioCyc; EICT634503:G1GVC-189-MONOMER; -.
DR   Proteomes; UP000001485; Chromosome.
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   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; IPR013622; CpdA_C.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   ProDom; PD587589; Calcineurin-like_phos_C; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B6Y1.
DR   SWISS-2DPAGE; C5B6Y1.
KW   cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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:UP000001485}.
FT   DOMAIN       16    206       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   NP_BIND      94     95       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   METAL        22     22       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        24     24       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        64     64       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        64     64       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        94     94       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       164    164       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       203    203       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       205    205       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   BINDING      24     24       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING      64     64       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING     205    205       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
SQ   SEQUENCE   275 AA;  30679 MW;  B735EA0C8C15A890 CRC64;
     MESLFHLAVA SGAPVRLLQI TDTHLFAGQQ ETLLGVNTYR SYQAVLAAIR AEAHPFDLIV
     ATGDLAQDHS AAAYRHFAAG VAELHRPCLW LPGNHDFQPA MVDALAQAGV HANKRALLGE
     CWQIVLLDSQ VVGVPHGELS DYQLEWLELT LASEPQRHTM LLLHHHPQPS GCTWLDQHSL
     RNAHALDEIL RRYPQVNTLV CGHIHQELDL DWNGRRLLAT PSTCVQFKPL CTNFTIDTIS
     PGWRYLTLYP DGRVTTAVHR LASSEFRPDL DADGY
//

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