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P82597 (MGLP_BAC25) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thermostable monoacylglycerol lipase

Short name=MGLP
Short name=bMGL
EC=3.1.1.23
OrganismBacillus sp. (strain H-257)
Taxonomic identifier129908 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes monoacylglycerols, with the highest activity occurring with 1-monolauroylglycerol. Ref.2

Catalytic activity

Hydrolyzes glycerol monoesters of long-chain fatty acids. Ref.2 Ref.3 Ref.4

Enzyme regulation

Not inhibited by cholate, but slightly inhibited by triton X-100 and deoxycholate. Completely inhibited by PMSF (phenylmethylsulfonyl fluoride) at a concentration of 200 µM. Ref.2 Ref.3

Subunit structure

Monomer. Ref.2 Ref.3

Miscellaneous

This lipase is not secreted extracellularly as other bacterial lipases. Ref.2

Sequence similarities

Belongs to the lipase/esterase LIP3/BchO family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6-8.

Temperature dependence:

Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
   Molecular functionHydrolase
Serine esterase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionacylglycerol lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 250249Thermostable monoacylglycerol lipase
PRO_0000207072

Sites

Active site971Nucleophile Ref.3 Ref.4
Active site1961Charge relay system Ref.3 Ref.4
Active site2261Charge relay system Ref.3 Ref.4
Binding site291Substrate; via amide nitrogen
Binding site981Substrate; via amide nitrogen
Site1451Important for substrate specificity

Experimental info

Mutagenesis1451I → G: 18% reduction in hydrolase activity for both 1-lauroylglycerol (1-LG) and 1-oleoylglycerol (1-OG). Ref.4
Mutagenesis1451I → S: 62% and 38% reduction in hydrolase activity for 1-oleoylglycerol and 1-lauroylglycerol, respectively. Ref.4
Mutagenesis1961D → N: Loss of enzyme activity. Ref.4

Secondary structure

.............................................. 250
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82597 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6D315EDF65A15AAE

FASTA25027,359
        10         20         30         40         50         60 
MSEQYPVLSG AEPFYAENGP VGVLLVHGFT GTPHSMRPLA EAYAKAGYTV CLPRLKGHGT 

        70         80         90        100        110        120 
HYEDMERTTF HDWVASVEEG YGWLKQRCQT IFVTGLSMGG TLTLYLAEHH PDICGIVPIN 

       130        140        150        160        170        180 
AAVDIPAIAA GMTGGGELPR YLDSIGSDLK NPDVKELAYE KTPTASLLQL ARLMAQTKAK 

       190        200        210        220        230        240 
LDRIVCPALI FVSDEDHVVP PGNADIIFQG ISSTEKEIVR LRNSYHVATL DYDQPMIIER 

       250 
SLEFFAKHAG 

« Hide

References

[1]"Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain H-257: molecular cloning, sequencing, and expression in Escherichia coli of the gene."
Kitaura S., Suzuki K., Imamura S.
J. Biochem. 129:397-402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257."
Imamura S., Kitaura S.
J. Biochem. 127:419-425(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
[3]"The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes."
Rengachari S., Bezerra G.A., Riegler-Berket L., Gruber C.C., Sturm C., Taschler U., Boeszoermenyi A., Dreveny I., Zimmermann R., Gruber K., Oberer M.
Biochim. Biophys. Acta 1821:1012-1021(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH INHIBITOR PMSF, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, ACTIVE SITE.
Strain: H-257.
[4]"Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase."
Rengachari S., Aschauer P., Schittmayer M., Mayer N., Gruber K., Breinbauer R., Birner-Gruenberger R., Dreveny I., Oberer M.
J. Biol. Chem. 288:31093-31104(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-196 IN COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, SITE, MUTAGENESIS OF ILE-145 AND ASP-196.
Strain: H-257.

Cross-references

Sequence databases

PIRJC7669.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RLIX-ray1.85A1-250[»]
3RM3X-ray1.20A1-250[»]
4KE6X-ray2.80A/B/C/D/E/F1-250[»]
4KE7X-ray1.70A/B1-250[»]
4KE8X-ray1.85A/B/C/D1-250[»]
4KE9X-ray2.20A/B/C/D3-250[»]
4KEAX-ray1.70A/B/C/D/E/F1-250[»]
ProteinModelPortalP82597.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR012354. Esterase_lipase.
[Graphical view]
PIRSFPIRSF017388. Esterase_lipase. 1 hit.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMGLP_BAC25
AccessionPrimary (citable) accession number: P82597
Secondary accession number(s): Q7M0R0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 45 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references