ID Q31X00_SHIBS Unreviewed; 275 AA.
AC Q31X00;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
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=icc {ECO:0000313|EMBL:ABB67408.1};
GN Synonyms=cpdA {ECO:0000256|HAMAP-Rule:MF_00905};
GN OrderedLocusNames=SBO_2890 {ECO:0000313|EMBL:ABB67408.1};
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB67408.1, ECO:0000313|Proteomes:UP000007067};
RN [1] {ECO:0000313|EMBL:ABB67408.1, ECO:0000313|Proteomes:UP000007067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227 {ECO:0000313|EMBL:ABB67408.1,
RC ECO:0000313|Proteomes:UP000007067};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role
CC in modulating the intracellular concentration of cAMP, thereby
CC influencing cAMP-dependent processes. {ECO:0000256|HAMAP-
CC Rule:MF_00905}.
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; EC=3.1.4.53; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000256|ARBA:ARBA00025742, ECO:0000256|HAMAP-
CC Rule:MF_00905}.
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DR EMBL; CP000036; ABB67408.1; -; Genomic_DNA.
DR RefSeq; WP_000444747.1; NC_007613.1.
DR AlphaFoldDB; Q31X00; -.
DR SMR; Q31X00; -.
DR GeneID; 75203574; -.
DR KEGG; sbo:SBO_2890; -.
DR HOGENOM; CLU_070320_0_0_6; -.
DR Proteomes; UP000007067; 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_phosphodiest_CpdA; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR046379; cAMP_phosphodiest_CpdA.
DR InterPro; IPR026575; GpdQ/CpdA-like.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR42988:SF2; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CBUA0032-RELATED; 1.
DR PANTHER; PTHR42988; PHOSPHOHYDROLASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00905};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00905};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00905}.
FT DOMAIN 16..206
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 24
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 94..95
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 205
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
SQ SEQUENCE 275 AA; 30938 MW; 97696478536CFBF1 CRC64;
MESLLTLPLA GEARVRILQI TDTHLFAQKH EALLGVNTWE SYQAVLEAIR PHQHEFDLIV
ATGDLAQDQS SAAYQHFAEG IASFRAPCVW LPGNHDFQPA MYSALQDAGI SPAKRVFIGE
QWQILLLDSQ VFGVPHGELS EFQLEWLERK LADAPERHTL LLLHHHPLPA GCSWLDQHSL
RNAGELDTVL AKFPHVKYLL CGHIHQELDL DWNGRRLLAT PSTCVQFKPH CSNFTLDTIA
PGWRTLELHA DGTLTTEVHR LADTRFQPDT ASEGY
//
