ID   BMGDS_TRIV2             Reviewed;         468 AA.
AC   Q3MB01;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Beta-monoglucosyldiacylglycerol synthase;
DE            Short=Beta-MGS;
DE            Short=MGlcDAG synthase;
DE            EC=2.4.1.336 {ECO:0000269|Ref.2};
DE   AltName: Full=UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase;
GN   OrderedLocusNames=Ava_2217;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 29413 / PCC 7937;
RA   Sato N., Murata M.;
RT   "Lipid biosynthesis in the blue-green alga (cyanobacterium), Anabaena
RT   variabilis III. UDPglucose:diacylglycerol glucosyltransferase activity in
RT   vitro.";
RL   Plant Cell Physiol. 23:1115-1120(1982).
CC   -!- FUNCTION: Glucosyltransferase involved in the biosynthesis of the non-
CC       bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which
CC       contributes to regulate the properties and stability of the membrane.
CC       Catalyzes the transfer of a glucosyl residue from UDP-Glc to
CC       diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl-
CC       DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only
CC       use UDP-Glc as sugar donor. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-
CC         3-O-(beta-D-glucopyranosyl)-sn-glycerol + H(+) + UDP;
CC         Xref=Rhea:RHEA:17285, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75799;
CC         EC=2.4.1.336; Evidence={ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 uM for UDP-Glc {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         The activity increases with temperature. {ECO:0000269|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; CP000117; ABA21835.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MB01; -.
DR   SMR; Q3MB01; -.
DR   STRING; 240292.Ava_2217; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABA21835; ABA21835; Ava_2217.
DR   KEGG; ava:Ava_2217; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_037834_0_0_3; -.
DR   OMA; RNRWAEG; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016758; F:hexosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046467; P:membrane lipid biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycerol metabolism; Glycosyltransferase;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..468
FT                   /note="Beta-monoglucosyldiacylglycerol synthase"
FT                   /id="PRO_0000425270"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  52844 MW;  C216E0694C4622F4 CRC64;
     MPANSWPDND SYKELDPLNS LLSEVSTTEE SVVETRDLSL PSRFQGRRGK AALVLTIVWS
     GTIALHLVSW GSIFILGLTT VLGIHALGVV FARPRHYQKE MQGSLPFVSI LVAAKNEEAV
     IAKLARNLCN LEYPNGQYEV WIIDDNSSDK TPHILAELAK EYDKLKVLRR SAQATGGKSG
     ALNQVLPLTQ GEIIAVFDAD AQVASDMLLH VVPLFQREKV GAVQVRKAIA NAKENFWTKG
     QMAEMSLDIW FQQQRTALGG IGELRGNGQF VRRQALDSCG GWNEETITDD LDLTFRLHLD
     KWDIECLFYP AVQEEGVTTA IALWHQRNRW AEGGYQRYLD YWDLILKNRM GTRKTWDMLM
     FMLTMYILPT AAIPDLLMAV VRHRPPMLGP VTGLSVTMSV VGMFAGLRRI RQEQKFQVHT
     PFVLLLQTMR GTLYMLHWLV VMSSTTARMS FRPKRLKWVK TVHTGSGE