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P82597

- MGLP_BAC25

UniProt

P82597 - MGLP_BAC25

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Protein
Thermostable monoacylglycerol lipase
Gene
N/A
Organism
Bacillus sp. (strain H-257)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Hydrolyzes glycerol monoesters of long-chain fatty acids.3 Publications

Enzyme regulationi

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.2 Publications

pH dependencei

Optimum pH is 6-8.

Temperature dependencei

Optimum temperature is 75 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate; via amide nitrogen
Active sitei97 – 971Nucleophile2 Publications
Binding sitei98 – 981Substrate; via amide nitrogen
Sitei145 – 1451Important for substrate specificity
Active sitei196 – 1961Charge relay system2 Publications
Active sitei226 – 2261Charge relay system2 Publications

GO - Molecular functioni

  1. acylglycerol lipase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Names & Taxonomyi

Protein namesi
Recommended name:
Thermostable monoacylglycerol lipase (EC:3.1.1.23)
Short name:
MGLP
Short name:
bMGL
OrganismiBacillus sp. (strain H-257)
Taxonomic identifieri129908 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451I → G: 18% reduction in hydrolase activity for both 1-lauroylglycerol (1-LG) and 1-oleoylglycerol (1-OG). 1 Publication
Mutagenesisi145 – 1451I → S: 62% and 38% reduction in hydrolase activity for 1-oleoylglycerol and 1-lauroylglycerol, respectively. 1 Publication
Mutagenesisi196 – 1961D → N: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 250249Thermostable monoacylglycerol lipase
PRO_0000207072Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163
Beta strandi19 – 268
Helixi33 – 353
Helixi37 – 459
Beta strandi49 – 524
Beta strandi58 – 603
Helixi62 – 665
Helixi70 – 8516
Beta strandi89 – 968
Helixi98 – 10912
Beta strandi115 – 1206
Helixi126 – 1316
Beta strandi134 – 1363
Beta strandi140 – 1434
Beta strandi160 – 1634
Helixi164 – 17916
Helixi181 – 1833
Beta strandi188 – 1936
Beta strandi197 – 1993
Helixi203 – 2108
Beta strandi214 – 22310
Helixi228 – 2303
Helixi234 – 24815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP82597.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR012354. Esterase_lipase.
[Graphical view]
PIRSFiPIRSF017388. Esterase_lipase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P82597-1 [UniParc]FASTAAdd to Basket

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MSEQYPVLSG AEPFYAENGP VGVLLVHGFT GTPHSMRPLA EAYAKAGYTV    50
CLPRLKGHGT HYEDMERTTF HDWVASVEEG YGWLKQRCQT IFVTGLSMGG 100
TLTLYLAEHH PDICGIVPIN AAVDIPAIAA GMTGGGELPR YLDSIGSDLK 150
NPDVKELAYE KTPTASLLQL ARLMAQTKAK LDRIVCPALI FVSDEDHVVP 200
PGNADIIFQG ISSTEKEIVR LRNSYHVATL DYDQPMIIER SLEFFAKHAG 250
Length:250
Mass (Da):27,359
Last modified:January 23, 2007 - v3
Checksum:i6D315EDF65A15AAE
GO

Sequence databases

PIRiJC7669.

Cross-referencesi

Sequence databases

PIRi JC7669.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3RLI X-ray 1.85 A 1-250 [» ]
3RM3 X-ray 1.20 A 1-250 [» ]
4KE6 X-ray 2.80 A/B/C/D/E/F 1-250 [» ]
4KE7 X-ray 1.70 A/B 1-250 [» ]
4KE8 X-ray 1.85 A/B/C/D 1-250 [» ]
4KE9 X-ray 2.20 A/B/C/D 3-250 [» ]
4KEA X-ray 1.70 A/B/C/D/E/F 1-250 [» ]
ProteinModelPortali P82597.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR012354. Esterase_lipase.
[Graphical view ]
PIRSFi PIRSF017388. Esterase_lipase. 1 hit.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiMGLP_BAC25
AccessioniPrimary (citable) accession number: P82597
Secondary accession number(s): Q7M0R0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This lipase is not secreted extracellularly as other bacterial lipases.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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