Q8YLG0 (CPDA_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
Short name=3',5'-cyclic AMP phosphodiesterase
Short name=cAMP phosphodiesterase
EC=3.1.4.17

Gene names

Name:	cpdA
Ordered Locus Names:	alr5338

Organism

Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Can also hydrolyze cGMP. Ref.2
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. Ref.2
Cofactor	Binds 2 metal cations per subunit Probable. Ref.2
Enzyme regulation	Activated by iron and manganese. Ref.2
Sequence similarities	Belongs to the cAMP phosphodiesterase class-III family.
Biophysicochemical properties	Kinetic parameters: KM=45 µM for cAMP Ref.2 Vmax=4.9 µmol/min/mg enzyme with cAMP as substrate Vmax=4.4 µmol/min/mg enzyme with cGMP as substrate

Ontologies

Keywords
Ligand	Metal-binding Nucleotide-binding cAMP
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 266	266	3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905		PRO_0000413371
Regions
	Nucleotide binding	86 – 87	2	cAMP By similarity
Sites
	Metal binding	14	1	Metal cation 1 By similarity
	Metal binding	16	1	Metal cation 1 By similarity
	Metal binding	56	1	Metal cation 1 By similarity
	Metal binding	56	1	Metal cation 2 By similarity
	Metal binding	86	1	Metal cation 2 By similarity
	Metal binding	155	1	Metal cation 2 By similarity
	Metal binding	194	1	Metal cation 2 By similarity
	Metal binding	196	1	Metal cation 1 By similarity
	Binding site	16	1	cAMP By similarity
	Binding site	56	1	cAMP By similarity
	Binding site	196	1	cAMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YLG0 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 46B3475509226736	FASTA	266	30,432
	10 20 30 40 50 60 MNEKLPISIA QITDIHLLAS ESQRLQGIST TESFLAVMKR LEELRPELDL LLMTGDLSDD 70 80 90 100 110 120 GTPESYENLQ HYLNSLQIAT YWLPGNHDCA IAMDKILNLG MVSRRKSFQR GNWNFILLNS 130 140 150 160 170 180 SVTDCVYGYL SATTLDWLDS ELKMLPNNPT LIALHHPPLS VNSAWIDRSC LQNSQELFAV 190 200 210 220 230 240 IDRYPQVKLV LFGHIHQEFR RQRHNVHYLG SPSTCYQFQS QSTTFAINQE LPGFRLLKLY 250 260 ADGTWTTKIE RVPYSLPIEP TVTVSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576.
[2]	"Biochemical properties of a cAMP phosphodiesterase in the cyanobacterium Anabaena sp. strain PCC 7120." Fujisawa T., Ohmori M. Microbes Environ. 20:92-96(2005) Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000019 Genomic DNA. Translation: BAB77037.1.
PIR	AB2473.
RefSeq	NP_489378.1. NC_003272.1.
3D structure databases
ProteinModelPortal	Q8YLG0.
ModBase	Search...
Protein-protein interaction databases
STRING	103690.alr5338.
Protocols and materials databases
DNASU	1108942.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB77037; BAB77037; BAB77037.
GeneID	1108942.
KEGG	ana:alr5338.
PATRIC	22781413. VBINosSp37423_6142.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1409.
HOGENOM	HOG000238351.
KO	K03651.
OMA	CAWLDQH.
ProtClustDB	CLSK896362.
Family and domain databases
HAMAP	MF_00905. cAMP_phophodiest_CpdA.
InterPro	IPR013622. Calcineurin-like_phos_C. IPR026575. cAMP_Pdiest_CpdA. IPR004843. Metallo_PEstase_dom. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
ProDom	PD587589. Calcineurin-like_phos_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

CPDA_NOSS1

Accession

Primary (citable) accession number: Q8YLG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program