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P82597

- MGLP_BAC25

UniProt

P82597 - MGLP_BAC25

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
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 – 971Nucleophile
    Binding sitei98 – 981Substrate; via amide nitrogen
    Sitei145 – 1451Important for substrate specificity
    Active sitei196 – 1961Charge relay system
    Active sitei226 – 2261Charge relay system

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: UniProtKB-EC

    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 lipasePRO_0000207072Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    250
    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.
    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.
    [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

    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: October 1, 2014
    This is version 46 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