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Protein

Thermostable monoacylglycerol lipase

Gene
N/A
Organism
Bacillus sp. (strain H-257)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei29Substrate; via amide nitrogen1
Active sitei97Nucleophile1
Binding sitei98Substrate; via amide nitrogen1
Sitei145Important for substrate specificity1
Active sitei196Charge relay system1
Active sitei226Charge relay system1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.23. 691.

Protein family/group databases

ESTHERibac25-mglp. CarbLipBact_2.

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)DescriptionActionsGraphical viewLength
Mutagenesisi145I → G: 18% reduction in hydrolase activity for both 1-lauroylglycerol (1-LG) and 1-oleoylglycerol (1-OG). 1 Publication1
Mutagenesisi145I → S: 62% and 38% reduction in hydrolase activity for 1-oleoylglycerol and 1-lauroylglycerol, respectively. 1 Publication1
Mutagenesisi196D → N: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002070722 – 250Thermostable monoacylglycerol lipaseAdd BLAST249

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 16Combined sources3
Beta strandi19 – 26Combined sources8
Helixi33 – 35Combined sources3
Helixi37 – 45Combined sources9
Beta strandi49 – 52Combined sources4
Beta strandi58 – 60Combined sources3
Helixi62 – 66Combined sources5
Helixi70 – 85Combined sources16
Beta strandi89 – 96Combined sources8
Helixi98 – 109Combined sources12
Beta strandi115 – 120Combined sources6
Helixi126 – 131Combined sources6
Beta strandi134 – 136Combined sources3
Beta strandi140 – 143Combined sources4
Beta strandi160 – 163Combined sources4
Helixi164 – 179Combined sources16
Helixi181 – 183Combined sources3
Beta strandi188 – 193Combined sources6
Beta strandi197 – 199Combined sources3
Helixi203 – 210Combined sources8
Beta strandi214 – 223Combined sources10
Helixi228 – 230Combined sources3
Helixi234 – 248Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4LHEX-ray1.96A/B1-250[»]
ProteinModelPortaliP82597.
SMRiP82597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lipase/esterase LIP3/BchO family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR012354. Esterase_lipase.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[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

« Hide

        10         20         30         40         50
MSEQYPVLSG AEPFYAENGP VGVLLVHGFT GTPHSMRPLA EAYAKAGYTV
60 70 80 90 100
CLPRLKGHGT HYEDMERTTF HDWVASVEEG YGWLKQRCQT IFVTGLSMGG
110 120 130 140 150
TLTLYLAEHH PDICGIVPIN AAVDIPAIAA GMTGGGELPR YLDSIGSDLK
160 170 180 190 200
NPDVKELAYE KTPTASLLQL ARLMAQTKAK LDRIVCPALI FVSDEDHVVP
210 220 230 240 250
PGNADIIFQG ISSTEKEIVR LRNSYHVATL DYDQPMIIER SLEFFAKHAG
Length:250
Mass (Da):27,359
Last modified:January 23, 2007 - v3
Checksum:i6D315EDF65A15AAE
GO

Sequence databases

PIRiJC7669.

Cross-referencesi

Sequence databases

PIRiJC7669.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4LHEX-ray1.96A/B1-250[»]
ProteinModelPortaliP82597.
SMRiP82597.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibac25-mglp. CarbLipBact_2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.23. 691.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR012354. Esterase_lipase.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
PIRSFiPIRSF017388. Esterase_lipase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 54 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.