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InterPro: IPR002168 Lipase, GDXG, active site

Protein matchesHelp
UniProtKB
Matches:
1601 proteins
AccessionHelp IPR002168 Lipase_GDXG_AS
TypeHelp Active_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR013094 Alpha/beta hydrolase fold-3
IPR017157 Arylacetamide deacetylase
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0016787 hydrolase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

These enzymes contain a Ser-centred consensus sequence and a conserved His-Gly dipeptide found in most lipase amino-terminal domains. These sequences are involved in the lipase active site conformation since substitution of the conserved Ser or His residues by Ala and Gln, respectively, results in the loss of both lipase and esterase activities [1].

Structural linksHelp
CATH: 3.40.50.1820
Database linksHelp
PDBe-motif: PS01173 , PS01174
Enzyme: EC:3.1.1
PROSITE doc: PDOC00903
Blocks: IPB002168

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002168 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P22760 Arylacetamide deacetylase

P54310 Hormone-sensitive lipase

Q6L545 Gibberellin receptor GID1

Q8ZRA1 Acetyl esterase

Q9MAA7 Probable gibberellin receptor GID1L1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013094 Alpha/beta hydrolase fold-3
IPR017157 Arylacetamide deacetylase
IPR002168 Lipase, GDXG, active site
IPR010468 Hormone-sensitive lipase, N-terminal
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Feller G, Thiry M, Gerday C.
Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues.
DNA Cell Biol. 10 381-8 1991 [PubMed: 1907455]

Additional ReadingHelp
Byun JS, Rhee JK, Kim ND, Yoon J, Kim DU, Koh E, Oh JW, Cho HS.
Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties.
BMC Struct. Biol. 7 2007 47 [PubMed: 17625021]
http://dx.doi.org/10.1186/1472-6807-7-47
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InterPro 23.1