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Information on EC 3.1.4.52 - cyclic-guanylate-specific phosphodiesterase

for references in articles please use BRENDA:EC3.1.4.52
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EC Tree
IUBMB Comments
Requires Mg2+ or Mn2+ for activity and is inhibited by Ca2+ and Zn2+. Contains a heme unit. This enzyme linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65, diguanylate cyclase and an allosteric activator of EC 2.4.1.12, cellulose synthase (UDP-forming), rendering it inactive . It is the balance between these two enzymes that determines the cellular level of c-di-GMP .
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UNIPROT: Q6MM30
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hd-gyp, c-di-gmp phosphodiesterase, phosphodiesterase a, blrp1, putative uncharacterized protein, pa4781, cyclic di-gmp phosphodiesterase, c-di-gmp-specific phosphodiesterase, pde-a, pa4108, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclic-di-GMP phosphodiesterase
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SYSTEMATIC NAME
IUBMB Comments
cyclic bis(3->5')diguanylate 3-guanylylhydrolase
Requires Mg2+ or Mn2+ for activity and is inhibited by Ca2+ and Zn2+. Contains a heme unit. This enzyme linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65, diguanylate cyclase and an allosteric activator of EC 2.4.1.12, cellulose synthase (UDP-forming), rendering it inactive [1]. It is the balance between these two enzymes that determines the cellular level of c-di-GMP [1].
CAS REGISTRY NUMBER
COMMENTARY hide
338732-46-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the fold and active site of the HD-GYP domain are different from those of EAL proteins, and restricted access to the active-site cleft is indicative of a different mode of activity regulation. The region encompassing the GYP motif has a novel conformation and is surface exposed and available for complexation with binding partners, including GGDEF proteins. Structure of the GYP motif and structure-function relationship. Mechanistic implications for HD-GYP family proteins
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q6MM30_BDEBA
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
308
0
34791
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging-drop method at 18°C using 0.001 ml of protein solution mixed with an equal volume of reservoir solution, varying conditions using 0.1 M bis-Tris, pH 5.5, 0.2-0.4 M ammonium acetate, 25% w/v PEG 3350, with or without 20% v/v DMSO or 2.1 M DL-malic acid, pH 7.0, X-ray diffraction structure determination and analysis at 2.5 A resolution
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence comparisons, comparative transcriptional profiling of Bd1817 expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lovering, A.L.; Capeness, M.J.; Lambert, C.; Hobley, L.; Sockett, R.E.
The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases
mBio
2
e00163
2011
Bdellovibrio bacteriovorus (Q6MM30), Bdellovibrio bacteriovorus
Manually annotated by BRENDA team