P44685 (CPDA_HAEIN) 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
Synonyms:	icc
Ordered Locus Names:	HI_0399

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. May coordinate responses to nutritional stress, ensuring optimal competence development. Ref.2
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. HAMAP-Rule MF_00905
Cofactor	Binds 2 metal cations per subunit By similarity.
Disruption phenotype	Mutants show increased levels of cellular cAMP. Ref.2
Sequence similarities	Belongs to the cAMP phosphodiesterase class-III family.

Ontologies

Keywords
Ligand	Metal-binding Nucleotide-binding cAMP
Molecular function	Hydrolase
Technical term	Complete proteome Reference 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 – 274	274	3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905		PRO_0000084148
Regions
	Nucleotide binding	93 – 94	2	cAMP By similarity
Sites
	Metal binding	21	1	Metal cation 1 By similarity
	Metal binding	23	1	Metal cation 1 By similarity
	Metal binding	63	1	Metal cation 1 By similarity
	Metal binding	63	1	Metal cation 2 By similarity
	Metal binding	93	1	Metal cation 2 By similarity
	Metal binding	163	1	Metal cation 2 By similarity
	Metal binding	202	1	Metal cation 2 By similarity
	Metal binding	204	1	Metal cation 1 By similarity
	Binding site	23	1	cAMP By similarity
	Binding site	63	1	cAMP By similarity
	Binding site	204	1	cAMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44685 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A810BF2072CA4957	FASTA	274	31,556
	10 20 30 40 50 60 MKNTFVYQAE KPVIKLLQIT DPHLFKDESA ELLGVNTQAS FAQVLKEIQQ ENNEFDVILA 70 80 90 100 110 120 TGDLVQDSSD EGYIRFVEMM KPFNKPVFWI PGNHDFQPKM AEFLNQPPMN AAKHLLLGEH 130 140 150 160 170 180 WQALLLDSQV YGVPHGQLSQ HQLDLLKETL GKNPERYTLV VLHHHLLPTN SAWLDQHNLR 190 200 210 220 230 240 NSHELAEVLA PFTNVKAILY GHIHQEVNSE WNGYQVMATP ATCIQFKPDC QYFSLDTLQP 250 260 270 GWREIELHSD GSIRTEVKRI QQAEFFPNMQ EEGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"A 3',5' cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and optimizes competence in Haemophilus influenzae Rd." Macfadyen L.P., Ma C., Redfield R.J. J. Bacteriol. 180:4401-4405(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22058.1.
PIR	E64065.
RefSeq	NP_438561.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44685.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0399.
Protocols and materials databases
DNASU	949501.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22058; AAC22058; HI_0399.
GeneID	949501.
KEGG	hin:HI0399.
PATRIC	20189349. VBIHaeInf48452_0418.
Phylogenomic databases
eggNOG	COG1409.
KO	K03651.
OMA	CAWLDQH.
ProtClustDB	PRK11148.
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_HAEIN

Accession

Primary (citable) accession number: P44685

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program