BMGDS_SYNY3
ID BMGDS_SYNY3 Reviewed; 479 AA.
AC P74165;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=sll1377;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
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).
RN [3]
RP FUNCTION, MUTAGENESIS OF ASP-147; ASP-200; ARG-329 AND ARG-331,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=19549521; DOI=10.1016/j.febslet.2009.06.033;
RA Shimojima M., Tsuchiya M., Ohta H.;
RT "Temperature-dependent hyper-activation of monoglucosyldiacylglycerol
RT synthase is post-translationally regulated in Synechocystis sp. PCC 6803.";
RL FEBS Lett. 583:2372-2376(2009).
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 ECO:0000269|PubMed:19549521}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC The activity increases with temperature.
CC {ECO:0000269|PubMed:19549521};
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; BA000022; BAA18254.1; -; Genomic_DNA.
DR PIR; S75693; S75693.
DR AlphaFoldDB; P74165; -.
DR SMR; P74165; -.
DR STRING; 1148.1653339; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; P74165; -.
DR EnsemblBacteria; BAA18254; BAA18254; BAA18254.
DR KEGG; syn:sll1377; -.
DR eggNOG; COG1215; Bacteria.
DR InParanoid; P74165; -.
DR OMA; RNRWAEG; -.
DR PhylomeDB; P74165; -.
DR BioCyc; MetaCyc:MON-19315; -.
DR BRENDA; 2.4.1.336; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 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..479
FT /note="Beta-monoglucosyldiacylglycerol synthase"
FT /id="PRO_0000425268"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 147
FT /note="D->Q: Significantly reduces the
FT monoglucosyldiacylglycerol synthase activity and blocks
FT temperature-dependent activation."
FT /evidence="ECO:0000269|PubMed:19549521"
FT MUTAGEN 200
FT /note="D->A: Significantly reduces the
FT monoglucosyldiacylglycerol synthase activity and blocks
FT temperature-dependent activation."
FT /evidence="ECO:0000269|PubMed:19549521"
FT MUTAGEN 329
FT /note="R->Q: Significantly reduces the
FT monoglucosyldiacylglycerol synthase activity and blocks
FT temperature-dependent activation."
FT /evidence="ECO:0000269|PubMed:19549521"
FT MUTAGEN 331
FT /note="R->A: Significantly reduces the
FT monoglucosyldiacylglycerol synthase activity and blocks
FT temperature-dependent activation."
FT /evidence="ECO:0000269|PubMed:19549521"
SQ SEQUENCE 479 AA; 54134 MW; C937345C6BE9EF6A CRC64;
MPQFPWKDND AELSPLEAFL AEWDDPEAEE EDFRNDFFRG SEGRRKKAAV MLMAIWTVVI
TLHYWVWGSW LVWALTGALS LQALRLMKAT PEEAPPLLTG DASTVPYPQV CLMVAAKNEE
AVIGKIVQQL CSLDYPGDRH EVWIVDDNST DRTPAILDQL RQQYPQLKVV RRGAGASGGK
SGALNEVLAQ TQGDIVGVFD ADANVPKDLL RRVVPYFASP TFGALQVRKA IANEAVNFWT
RGQGAEMALD AYFQQQRIVT GGIGELRGNG QFVARQALDA VGGWNEQTIT DDLDLTIRLH
LHQWKVGILV NPPVEEEGVT TAIALWHQRN RWAEGGYQRY LDYWRWICTQ PMGWKKKLDL
FSFLLMQYLL PTAAVPDLLM ALWQRRFPLL TPLSYLAIGF SCWGMYYGLK RLTPSEGESP
WQQMPALLAR TIGGTIYMFH WLIIMPAVTA RMAFRPKRLK WVKTVHGAAT EDALELKQS
