AMGDS_ACHLA
ID AMGDS_ACHLA Reviewed; 398 AA.
AC Q93P60;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Alpha-monoglucosyldiacylglycerol synthase;
DE Short=Alpha-MGS;
DE Short=MGlcDAG synthase;
DE EC=2.4.1.337 {ECO:0000269|PubMed:11294844, ECO:0000269|PubMed:8995384};
DE AltName: Full=1,2-Diacylglycerol 3-glucosyltransferase;
DE AltName: Full=UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase;
GN Name=mgs; Synonyms=ALmgs;
OS Acholeplasma laidlawii.
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=2148;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=A-EF22;
RX PubMed=11294844; DOI=10.1074/jbc.m102576200;
RA Berg S., Edman M., Li L., Wikstrom M., Wieslander A.;
RT "Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from
RT Acholeplasma laidlawii membranes. Recognition of a large group of lipid
RT glycosyltransferases in eubacteria and archaea.";
RL J. Biol. Chem. 276:22056-22063(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=A-EF22;
RX PubMed=8995384; DOI=10.1074/jbc.272.2.929;
RA Karlsson O.P., Dahlqvist A., Vikstrom S., Wieslander A.;
RT "Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-
RT glucosyltransferase from membranes of Acholeplasma laidlawii.";
RL J. Biol. Chem. 272:929-936(1997).
RN [3]
RP PROTECTION AGAINST PROTEOLYTIC DIGESTION.
RC STRAIN=A-EF22;
RX PubMed=9368025; DOI=10.1074/jbc.272.47.29602;
RA Li L., Karlsson O.P., Wieslander A.;
RT "Activating amphiphiles cause a conformational change of the 1,2-
RT diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes
RT according to proteolytic digestion.";
RL J. Biol. Chem. 272:29602-29606(1997).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=A-EF22;
RX PubMed=12911309; DOI=10.1021/bi034360l;
RA Li L., Storm P., Karlsson O.P., Berg S., Wieslander A.;
RT "Irreversible binding and activity control of the 1,2-diacylglycerol 3-
RT glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer
RT surface.";
RL Biochemistry 42:9677-9686(2003).
RN [5]
RP STRUCTURE BY NMR OF 65-87.
RA Lind J., Barany-Wallje E., Ramo T., Wieslander A., Maler L.;
RT "Structure, position of and membrane-interaction of a putative membrane-
RT anchoring domain of alMGS.";
RL Submitted (MAR-2005) to the PDB data bank.
CC -!- FUNCTION: Glucosyltransferase involved in the biosynthesis of the non-
CC bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol. This is
CC a major component for maintaining a certain anionic lipid surface
CC charge density, for balancing the bilayer to non-bilayer phase
CC equilibria and for keeping a constant lipid bilayer spontaneous
CC curvature (curvature packing stress). Catalyzes the transfer of a
CC glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form
CC the corresponding alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-
CC glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor
CC and DAG is the preferred substrate. {ECO:0000269|PubMed:11294844,
CC ECO:0000269|PubMed:8995384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-
CC 3-O-(alpha-D-glucopyranosyl)-sn-glycerol + H(+) + UDP;
CC Xref=Rhea:RHEA:47612, ChEBI:CHEBI:15378, ChEBI:CHEBI:17670,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.337; Evidence={ECO:0000269|PubMed:11294844,
CC ECO:0000269|PubMed:8995384};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8995384};
CC -!- ACTIVITY REGULATION: Activated by the negatively charged lipids
CC phosphatidylglycerol (PG), cardiolipin (CL), dodecylphosphate-rac-
CC glycerol (PDG), 1,2-dioleoyl-phosphatidylglycerol (DOPG) and
CC phosphatidylserine (PS). {ECO:0000269|PubMed:11294844,
CC ECO:0000269|PubMed:8995384}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.37 mM for UDP-Glc (in the presence of DOPG at 31%)
CC {ECO:0000269|PubMed:8995384};
CC KM=0.39 mM for UDP-Glc (in the presence of DOPG at 20%)
CC {ECO:0000269|PubMed:8995384};
CC KM=0.44 mM for UDP-Glc (in the presence of DOPG at 25%)
CC {ECO:0000269|PubMed:8995384};
CC Vmax=3.18 nmol/h/mg enzyme (in the presence of DOPG at 31%)
CC {ECO:0000269|PubMed:8995384};
CC Vmax=2.06 nmol/h/mg enzyme (in the presence of DOPG at 25%)
CC {ECO:0000269|PubMed:8995384};
CC Vmax=0.55 nmol/h/mg enzyme (in the presence of DOPG at 20%)
CC {ECO:0000269|PubMed:8995384};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11294844,
CC ECO:0000305|PubMed:12911309}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11294844, ECO:0000305|PubMed:12911309}; Cytoplasmic
CC side {ECO:0000305|PubMed:11294844, ECO:0000305|PubMed:12911309}.
CC Note=The enzyme binds the membrane surface via electrostatic
CC association with anionic lipids and is accompanied by hydrophobic
CC interactions and by a conformational change induced by nonbilayer-prone
CC lipids. The enzyme is supposed to be located on the cytosolic side of
CC the membrane.
CC -!- MISCELLANEOUS: PG could also protect the enzyme from proteolytic
CC digestion of the proteinase K, possibly by orienting a lysine-rich face
CC toward the membrane. {ECO:0000305|PubMed:9368025}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AF349769; AAK38877.2; -; Genomic_DNA.
DR PDB; 1Z2T; NMR; -; A=65-87.
DR PDBsum; 1Z2T; -.
DR AlphaFoldDB; Q93P60; -.
DR BMRB; Q93P60; -.
DR SMR; Q93P60; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR BioCyc; MetaCyc:MON-19379; -.
DR BRENDA; 2.4.1.336; 64.
DR BRENDA; 2.4.1.337; 64.
DR EvolutionaryTrace; Q93P60; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell membrane;
KW Direct protein sequencing; Glycerol metabolism; Glycosyltransferase;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Transferase.
FT CHAIN 1..398
FT /note="Alpha-monoglucosyldiacylglycerol synthase"
FT /id="PRO_0000425272"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1Z2T"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1Z2T"
SQ SEQUENCE 398 AA; 45166 MW; 735790E9FDE75A07 CRC64;
MRIGIFSEAY LPLISGVVTS VVNLKEGLEA LGHEVYVITP IPSKDKFEND PSVIRIPGWV
IPRKSLKGFR LVLFVKRYVR KMRKLKLDVV HIHTEFSMGK LGLAVAKKER IPSVYTLHTS
YQDYTHYVSK LLTRFAPNAA KKLAGKINNQ YTKNCHMTIV PTKKIYDKMI RLKHDGEFTI
IPSGINLKPF YKSSYTSEQV QALKDKLGIR NDEFVAILVA RIAKEKSIGD LVEAFVEFYK
SYPNSRFIII GDGPDKPVLD KLIDSKKASK YINTLGFVKN AEVGLYYQIA DVFLNASTTE
TQGLTYVEAL AASLPIIVRY DDVFDAFVED GKNGIFFNKN EELVKHLIHI RQNPEILGTL
SKNAEISTKP YAKEVYAKSC ETLYLDLIDK NNKKLNKK
