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Alpha-monoglucosyldiacylglycerol synthase (Alpha-MGS) (MGlcDAG synthase) (EC 2.4.1.337) (1,2-Diacylglycerol 3-glucosyltransferase) (UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase)

 AMGDS_ACHLA             Reviewed;         398 AA.
Q93P60;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-JUL-2017, entry version 47.
RecName: Full=Alpha-monoglucosyldiacylglycerol synthase;
Short=Alpha-MGS;
Short=MGlcDAG synthase;
EC=2.4.1.337 {ECO:0000269|PubMed:11294844, ECO:0000269|PubMed:8995384};
AltName: Full=1,2-Diacylglycerol 3-glucosyltransferase;
AltName: Full=UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase;
Name=mgs; Synonyms=ALmgs;
Acholeplasma laidlawii.
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=2148;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, FUNCTION,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
STRAIN=A-EF22;
PubMed=11294844; DOI=10.1074/jbc.M102576200;
Berg S., Edman M., Li L., Wikstrom M., Wieslander A.;
"Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase
from Acholeplasma laidlawii membranes. Recognition of a large group of
lipid glycosyltransferases in eubacteria and archaea.";
J. Biol. Chem. 276:22056-22063(2001).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
ENZYME REGULATION, AND SUBSTRATE SPECIFICITY.
STRAIN=A-EF22;
PubMed=8995384; DOI=10.1074/jbc.272.2.929;
Karlsson O.P., Dahlqvist A., Vikstrom S., Wieslander A.;
"Lipid dependence and basic kinetics of the purified 1,2-
diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma
laidlawii.";
J. Biol. Chem. 272:929-936(1997).
[3]
PROTECTION AGAINST PROTEOLYTIC DIGESTION.
STRAIN=A-EF22;
PubMed=9368025; DOI=10.1074/jbc.272.47.29602;
Li L., Karlsson O.P., Wieslander A.;
"Activating amphiphiles cause a conformational change of the 1,2-
diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii
membranes according to proteolytic digestion.";
J. Biol. Chem. 272:29602-29606(1997).
[4]
SUBCELLULAR LOCATION.
STRAIN=A-EF22;
PubMed=12911309; DOI=10.1021/bi034360l;
Li L., Storm P., Karlsson O.P., Berg S., Wieslander A.;
"Irreversible binding and activity control of the 1,2-diacylglycerol
3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid
bilayer surface.";
Biochemistry 42:9677-9686(2003).
[5]
STRUCTURE BY NMR OF 65-87.
Lind J., Barany-Wallje E., Ramo T., Wieslander A., Maler L.;
"Structure, position of and membrane-interaction of a putative
membrane-anchoring domain of alMGS.";
Submitted (MAR-2005) to the PDB data bank.
-!- FUNCTION: Glucosyltransferase involved in the biosynthesis of the
non-bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol.
This is a major component for maintaining a certain anionic lipid
surface charge density, for balancing the bilayer to non-bilayer
phase equilibria and for keeping a constant lipid bilayer
spontaneous curvature (curvature packing stress). Catalyzes the
transfer of a glucosyl residue from UDP-Glc to diacylglycerol
(DAG) acceptor to form the corresponding alpha-glucosyl-DAG (1,2-
diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol). It can only use
UDP-Glc as sugar donor and DAG is the preferred substrate.
{ECO:0000269|PubMed:11294844, ECO:0000269|PubMed:8995384}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
= UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:11294844, ECO:0000269|PubMed:8995384}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8995384};
-!- ENZYME REGULATION: Activated by the negatively charged lipids
phosphatidylglycerol (PG), cardiolipin (CL), dodecylphosphate-rac-
glycerol (PDG), 1,2-dioleoyl-phosphatidylglycerol (DOPG) and
phosphatidylserine (PS). {ECO:0000269|PubMed:11294844,
ECO:0000269|PubMed:8995384}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.37 mM for UDP-Glc (in the presence of DOPG at 31%)
{ECO:0000269|PubMed:8995384};
KM=0.39 mM for UDP-Glc (in the presence of DOPG at 20%)
{ECO:0000269|PubMed:8995384};
KM=0.44 mM for UDP-Glc (in the presence of DOPG at 25%)
{ECO:0000269|PubMed:8995384};
Vmax=3.18 nmol/h/mg enzyme (in the presence of DOPG at 31%)
{ECO:0000269|PubMed:8995384};
Vmax=2.06 nmol/h/mg enzyme (in the presence of DOPG at 25%)
{ECO:0000269|PubMed:8995384};
Vmax=0.55 nmol/h/mg enzyme (in the presence of DOPG at 20%)
{ECO:0000269|PubMed:8995384};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11294844,
ECO:0000305|PubMed:12911309}; Peripheral membrane protein
{ECO:0000305|PubMed:11294844, ECO:0000305|PubMed:12911309};
Cytoplasmic side {ECO:0000305|PubMed:11294844,
ECO:0000305|PubMed:12911309}. Note=The enzyme binds the membrane
surface via electrostatic association with anionic lipids and is
accompanied by hydrophobic interactions and by a conformational
change induced by nonbilayer-prone lipids. The enzyme is supposed
to be located on the cytosolic side of the membrane.
-!- MISCELLANEOUS: PG could also protect the enzyme from proteolytic
digestion of the proteinase K, possibly by orienting a lysine-rich
face toward the membrane. {ECO:0000305|PubMed:9368025}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
Glycosyltransferase 4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF349769; AAK38877.2; -; Genomic_DNA.
PDB; 1Z2T; NMR; -; A=65-87.
PDBsum; 1Z2T; -.
ProteinModelPortal; Q93P60; -.
SMR; Q93P60; -.
CAZy; GT4; Glycosyltransferase Family 4.
eggNOG; ENOG4107V8I; Bacteria.
eggNOG; COG0438; LUCA.
BioCyc; MetaCyc:MONOMER-19379; -.
EvolutionaryTrace; Q93P60; -.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IDA:UniProtKB.
GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR028098; Glyco_trans_4-like_N.
Pfam; PF13439; Glyco_transf_4; 1.
Pfam; PF00534; Glycos_transf_1; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cell membrane;
Direct protein sequencing; Glycerol metabolism; Glycosyltransferase;
Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
Transferase.
CHAIN 1 398 Alpha-monoglucosyldiacylglycerol
synthase.
/FTId=PRO_0000425272.
HELIX 71 78 {ECO:0000244|PDB:1Z2T}.
HELIX 80 83 {ECO:0000244|PDB:1Z2T}.
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


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