ID MGLP_BAC25 Reviewed; 250 AA. AC P82597; Q7M0R0; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 67. DE RecName: Full=Thermostable monoacylglycerol lipase; DE Short=MGLP; DE Short=bMGL; DE EC=3.1.1.23; OS Bacillus sp. (strain H-257). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=129908; RN [1] {ECO:0000312|PIR:JC7669} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11226879; DOI=10.1093/oxfordjournals.jbchem.a002870; RA Kitaura S., Suzuki K., Imamura S.; RT "Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain RT H-257: molecular cloning, sequencing, and expression in Escherichia coli of RT the gene."; RL J. Biochem. 129:397-402(2001). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND SUBUNIT. RX PubMed=10731713; DOI=10.1093/oxfordjournals.jbchem.a022623; RA Imamura S., Kitaura S.; RT "Purification and characterization of a monoacylglycerol lipase from the RT moderately thermophilic Bacillus sp. H-257."; RL J. Biochem. 127:419-425(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH RP INHIBITOR PMSF, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND RP ACTIVE SITE. RC STRAIN=H-257; RX PubMed=22561231; DOI=10.1016/j.bbalip.2012.04.006; RA Rengachari S., Bezerra G.A., Riegler-Berket L., Gruber C.C., Sturm C., RA Taschler U., Boeszoermenyi A., Dreveny I., Zimmermann R., Gruber K., RA Oberer M.; RT "The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals RT unexpected conservation of the cap architecture between bacterial and human RT enzymes."; RL Biochim. Biophys. Acta 1821:1012-1021(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-196 IN RP COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE RP SITE, SITE, AND MUTAGENESIS OF ILE-145 AND ASP-196. RC STRAIN=H-257; RX PubMed=24014019; DOI=10.1074/jbc.m113.491415; RA Rengachari S., Aschauer P., Schittmayer M., Mayer N., Gruber K., RA Breinbauer R., Birner-Gruenberger R., Dreveny I., Oberer M.; RT "Conformational plasticity and ligand binding of bacterial monoacylglycerol RT lipase."; RL J. Biol. Chem. 288:31093-31104(2013). CC -!- FUNCTION: Hydrolyzes monoacylglycerols, with the highest activity CC occurring with 1-monolauroylglycerol. {ECO:0000269|PubMed:10731713}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:10731713, CC ECO:0000269|PubMed:22561231, ECO:0000269|PubMed:24014019}; CC -!- ACTIVITY REGULATION: Not inhibited by cholate, but slightly inhibited CC by triton X-100 and deoxycholate. Completely inhibited by PMSF CC (phenylmethylsulfonyl fluoride) at a concentration of 200 uM. CC {ECO:0000269|PubMed:10731713, ECO:0000269|PubMed:22561231}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6-8.; CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius.; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10731713, CC ECO:0000269|PubMed:22561231}. CC -!- MISCELLANEOUS: This lipase is not secreted extracellularly as other CC bacterial lipases. {ECO:0000269|PubMed:10731713}. CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; JC7669; JC7669. DR PDB; 3RLI; X-ray; 1.85 A; A=1-250. DR PDB; 3RM3; X-ray; 1.20 A; A=1-250. DR PDB; 4KE6; X-ray; 2.80 A; A/B/C/D/E/F=1-250. DR PDB; 4KE7; X-ray; 1.70 A; A/B=1-250. DR PDB; 4KE8; X-ray; 1.85 A; A/B/C/D=1-250. DR PDB; 4KE9; X-ray; 2.20 A; A/B/C/D=3-250. DR PDB; 4KEA; X-ray; 1.70 A; A/B/C/D/E/F=1-250. DR PDB; 4LHE; X-ray; 1.96 A; A/B=1-250. DR PDBsum; 3RLI; -. DR PDBsum; 3RM3; -. DR PDBsum; 4KE6; -. DR PDBsum; 4KE7; -. DR PDBsum; 4KE8; -. DR PDBsum; 4KE9; -. DR PDBsum; 4KEA; -. DR PDBsum; 4LHE; -. DR AlphaFoldDB; P82597; -. DR SMR; P82597; -. DR ESTHER; bac25-mglp; CarbLipBact_2. DR BRENDA; 3.1.1.23; 691. DR GO; GO:0047372; F:acylglycerol lipase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR012354; Esterase_lipase. DR InterPro; IPR022742; Hydrolase_4. DR PANTHER; PTHR11614:SF121; CARBOXYLESTERASE; 1. DR PANTHER; PTHR11614; PHOSPHOLIPASE-RELATED; 1. DR Pfam; PF12146; Hydrolase_4; 1. DR PIRSF; PIRSF017388; Esterase_lipase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Hydrolase; Serine esterase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10731713" FT CHAIN 2..250 FT /note="Thermostable monoacylglycerol lipase" FT /id="PRO_0000207072" FT ACT_SITE 97 FT /note="Nucleophile" FT ACT_SITE 196 FT /note="Charge relay system" FT ACT_SITE 226 FT /note="Charge relay system" FT BINDING 29 FT /ligand="substrate" FT BINDING 98 FT /ligand="substrate" FT SITE 145 FT /note="Important for substrate specificity" FT MUTAGEN 145 FT /note="I->G: 18% reduction in hydrolase activity for both FT 1-lauroylglycerol (1-LG) and 1-oleoylglycerol (1-OG)." FT /evidence="ECO:0000269|PubMed:24014019" FT MUTAGEN 145 FT /note="I->S: 62% and 38% reduction in hydrolase activity FT for 1-oleoylglycerol and 1-lauroylglycerol, respectively." FT /evidence="ECO:0000269|PubMed:24014019" FT MUTAGEN 196 FT /note="D->N: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:24014019" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 19..26 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 33..35 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 37..45 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:4KEA" FT HELIX 62..66 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 70..85 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 89..96 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 115..120 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 126..131 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:4KEA" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 164..179 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 203..210 FT /evidence="ECO:0007829|PDB:3RM3" FT STRAND 214..223 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:3RM3" FT HELIX 234..248 FT /evidence="ECO:0007829|PDB:3RM3" SQ SEQUENCE 250 AA; 27359 MW; 6D315EDF65A15AAE CRC64; MSEQYPVLSG AEPFYAENGP VGVLLVHGFT GTPHSMRPLA EAYAKAGYTV CLPRLKGHGT HYEDMERTTF HDWVASVEEG YGWLKQRCQT IFVTGLSMGG TLTLYLAEHH PDICGIVPIN AAVDIPAIAA GMTGGGELPR YLDSIGSDLK NPDVKELAYE KTPTASLLQL ARLMAQTKAK LDRIVCPALI FVSDEDHVVP PGNADIIFQG ISSTEKEIVR LRNSYHVATL DYDQPMIIER SLEFFAKHAG //