BMGDS_NOSS1
ID BMGDS_NOSS1 Reviewed; 468 AA.
AC Q8YMK0;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Beta-monoglucosyldiacylglycerol synthase;
DE Short=Beta-MGS;
DE Short=MGlcDAG synthase;
DE EC=2.4.1.336 {ECO:0000269|PubMed:16714404};
DE AltName: Full=UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase;
GN OrderedLocusNames=all4933;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=16714404; DOI=10.1104/pp.106.082859;
RA Awai K., Kakimoto T., Awai C., Kaneko T., Nakamura Y., Takamiya K.,
RA Wada H., Ohta H.;
RT "Comparative genomic analysis revealed a gene for
RT monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane
RT lipid synthesis in cyanobacteria.";
RL Plant Physiol. 141:1120-1127(2006).
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. Two types of DAG (dipalmitoyl-DAG (DPDAG)
CC and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors,
CC but OPDAG is preferred. {ECO:0000269|PubMed:16714404}.
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|PubMed:16714404};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16714404};
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; BA000019; BAB76632.1; -; Genomic_DNA.
DR PIR; AE2422; AE2422.
DR RefSeq; WP_010999059.1; NZ_RSCN01000018.1.
DR AlphaFoldDB; Q8YMK0; -.
DR SMR; Q8YMK0; -.
DR STRING; 103690.17134071; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; BAB76632; BAB76632; BAB76632.
DR KEGG; ana:all4933; -.
DR eggNOG; COG1215; Bacteria.
DR OMA; RNRWAEG; -.
DR OrthoDB; 724641at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA: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; IDA: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;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..468
FT /note="Beta-monoglucosyldiacylglycerol synthase"
FT /id="PRO_0000425269"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 468 AA; 52828 MW; CEF120EA6E2530BE CRC64;
MPANSWPDND SYKELDPLNS LLSDVSTTEE SVVETRDLSL PSRFQGRRGK AALVLTIVWS
GTIALHLVSW GSIFILGLTT VLGIHALGVV FARPRHYQKE IQGSLPFVSI LVAAKNEEAV
IAKLAKNLCN LEYPNGQYEV WIIDDNSTDK TPHILAELAK EYDKLKVLRR SAQATGGKSG
ALNQVLPLTQ GEIIAVFDAD AQVASDMLLH VVPLFQREKV GAVQVRKAIA NAKENFWTKG
QMAEMSLDIW FQQQRTALGG IGELRGNGQF VRRQALDSCG GWNEETITDD LDLTFRLHLD
KWDIECLFYP AVQEEGVTTA IALWHQRNRW AEGGYQRYLD YWDLILKNRM GTRKTWDMLM
FMLTMYILPT AAIPDLLMAL TRHRPPMLGP VTGLSVTMSV VGMFAGLRRI RQEQKFQVHT
PFVLLLQTMR GTLYMLHWLV VMSSTTARMS FRPKRLKWVK TVHTGTGE