Q9KL18 · CGAP3_VIBCH

Function

function

Phosphodiesterase (PDE) that catalyzes the hydrolysis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP), leading to linear 5'-pApG (PubMed:25837739, PubMed:30365951).
Counteracts the function of the 3'3'-cGAMP synthase DncV, and is involved in the modulation of intracellular 3'3'-cGAMP levels. Enhances bacterial chemotaxis and inhibits intestinal colonization in vivo. Thus exerts a crucial role in regulating bacterial infectivity through catalyzing 3'3'-cGAMP degradation. Is specific for 3'3'-cGAMP since it cannot degrade other cGAMP linkage isomers (3'2'-, 2'3'-, and 2'2'-cGAMPs); is also able to hydrolyze c-di-GMP but not c-di-AMP (PubMed:25837739).

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Requires a divalent metal cation for activity. Likely has a bi-nuclear metal center. Has the highest enzyme activity with Mn2+, and when incubated with Ni2+, its activity is about 60% lower than that observed with Mn2+.

pH Dependence

Optimum pH is 10.0.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site317a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site318a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site318a divalent metal cation 2 (UniProtKB | ChEBI)
Active site321Proton donor
Binding site346a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site370a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site371a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site399a divalent metal cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functioncyclic-nucleotide phosphodiesterase activity
Molecular Functionmetal ion binding
Biological Processcyclic nucleotide catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3'3'-cGAMP-specific phosphodiesterase 3
  • EC number
  • Short names
    3'3'-cGAMP PDE 3
    ; V-cGAP3

Gene names

    • Ordered locus names
      VC_A0931

Organism names

Accessions

  • Primary accession
    Q9KL18

Proteomes

Phenotypes & Variants

Disruption phenotype

Significant increase in the ability to colonize the small intestine compared to the wild-type strain. No defect in biofilm formation. Enforced DncV expression in mutant cells lacking this gene causes an enhanced inhibition of chemotaxis. The double mutant lacking both VC_A0681 and VC_A0931 shows enhanced bacterial infectivity, and the triple one (VC_A0681, VC_A0210 and VC_A0931) has the highest infectivity, which demonstrates that V-cGAPs play non-redundant roles in cGAMP degradation.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis13Large decrease in enzymatic activity.
Mutagenesis17Large decrease in enzymatic activity.
Mutagenesis21Large decrease in enzymatic activity.
Mutagenesis317-318Loss of enzymatic activity.
Mutagenesis321Almost loss of activity.

Miscellaneous

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004353541-4603'3'-cGAMP-specific phosphodiesterase 3

Expression

Induction

Expression is up-regulated by 3'3'-cGAMP production (at both mRNA and protein levels).

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-189HD
Domain260-455HD-GYP

Domain

Consists of two tandem domains of about 15% identity and similar three-dimensional topology that interact to form a pseudo-dimeric structure. The N-terminal domain (residues 1-258) plays an important regulatory role in facilitating the catalytic function of the C-terminal domain (residues 259-460). The N-terminal domain alone does not show any activity. The C-terminal domain alone is much less active comparing to the full-length protein. The full-length protein is 13 times more active than the C-terminal domain alone.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    51,291
  • Last updated
    2000-10-01 v1
  • Checksum
    E160C15151DC3D2F
MSVAQNTFPLSELMISLTTALDMTEGQPPEHCIRCCWIGMHIGMQLELSEPELHDLFFTLLLKDAGCSSNAARICELYATDDLTFKRRYKTVGTSLSSVINFIVKNTGSEQSWTERILTTIDILKNGNDYAQELIQTRCTRGADVARELRFSEAVAQGIHSLDEHWNGQGRPEQRKGEAIPLFSRIALLAQVFDVFQMEHSIEEALQEIMARSGVWFDPKLVEVVEQLVENPRFLSGLKATDISQRVMNLPPAQAHLPLDDAYLECIVTAFGKIVDAKSPYTAGHSERVAVYTDLIARQLAISDADRIWLRRAALLHDIGKLGVSNAILDKPGKLDEAEWRAVQAHAAYTEQILYKLSPFKTLARMAGAHHEKLDGTGYPRGVNGDEISLMTRIITTADIFDALSAERPYRAAMPIDKALAIMEENLHTAIDPECFAALKKALNLLPDEYTQLPHSSDKT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE003853
EMBL· GenBank· DDBJ
AAF96828.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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