PBDGT_MYCGE
ID PBDGT_MYCGE Reviewed; 341 AA.
AC Q9ZB73;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Processive diacylglycerol beta-glycosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Beta-diglycosyldiacylglycerol synthase;
DE Short=Beta-DGS;
DE Short=DGlyDAG synthase;
DE AltName: Full=Beta-monoglycosyldiacylglycerol synthase;
DE Short=Beta-MGS;
DE Short=MGlyDAG synthase;
DE AltName: Full=Glycosyl-beta-1,6-glycosyldiacylglycerol synthase;
DE AltName: Full=UDP-galactose:1,2-dioleoylglycerol 3-beta-D-galactosyltransferase;
DE AltName: Full=UDP-glucose:1,2-dioleoylglycerol 3-beta-D-glucosyltransferase;
GN OrderedLocusNames=MG335.2;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP IDENTIFICATION.
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=21835921; DOI=10.1074/jbc.m110.214148;
RA Andres E., Martinez N., Planas A.;
RT "Expression and characterization of a Mycoplasma genitalium
RT glycosyltransferase in membrane glycolipid biosynthesis: potential target
RT against mycoplasma infections.";
RL J. Biol. Chem. 286:35367-35379(2011).
CC -!- FUNCTION: Processive glycosyltransferase involved in the biosynthesis
CC of both the non-bilayer-prone beta-monoglycosyldiacylglycerol and the
CC bilayer-forming membrane lipid beta-diglycosyldiacylglycerol. These
CC components contribute to regulate the properties and stability of the
CC membrane. Catalyzes sequentially the transfers of glucosyl or
CC galactosyl residues from UDP-Glc or UDP-Gal to diacylglycerol (DAG)
CC acceptor to form the corresponding beta-glycosyl-DAG (3-O-(beta-D-
CC glycopyranosyl)-1,2-diacyl-sn-glycerol), which then acts as acceptor to
CC give beta-diglycosyl-DAG product (3-O-(beta-D-glycopyranosyl-beta-
CC (1->6)-D-glycopyranosyl)-1,2-diacyl-sn-glycerol). Dioleoylglycerol
CC (DOG) is a preferred sugar acceptor than 3-O-(beta-D-glucopyranosyl)-
CC 1,2-dioleoyl-sn-glycerol. {ECO:0000269|PubMed:21835921}.
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 Evidence={ECO:0000269|PubMed:21835921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-galactose = a 1,2-
CC diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+) + UDP;
CC Xref=Rhea:RHEA:14945, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC Evidence={ECO:0000269|PubMed:21835921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + UDP-
CC alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-
CC glycerol + H(+) + UDP; Xref=Rhea:RHEA:39031, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75799,
CC ChEBI:CHEBI:76264; Evidence={ECO:0000269|PubMed:21835921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-
CC D-galactose = a 1,2-diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:53748,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:87082;
CC Evidence={ECO:0000269|PubMed:21835921};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by the negatively charged lipid
CC dioleoylphosphatidylglycerol (DOPG) and inhibited by N-(n-
CC nonyl)deoxygalactonojirimycin (C9J). {ECO:0000269|PubMed:21835921}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for UDP-Glc (in the presence of beta-glucosyl-DOG as sugar
CC acceptor at pH 8 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:21835921};
CC KM=87 uM for UDP-Glc (in the presence of DOG as sugar acceptor at pH
CC 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
CC KM=90 uM for beta-glucosyl-DOG (in the presence of UDP-Gal as sugar
CC donor at pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
CC KM=234 uM for UDP-Gal (in the presence of DOG as sugar acceptor at pH
CC 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
CC KM=270 uM for DOG (in the presence of UDP-Gal as sugar donor at pH 8
CC and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
CC KM=479 uM for UDP-Gal (in the presence of beta-glucosyl-DOG as sugar
CC acceptor at pH 8 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:21835921};
CC Note=kcat is 0.27 sec(-1) for Glc transfer with DOG as sugar
CC acceptor. kcat is 1.10 sec(-1) for Gal transfer with DOG as sugar
CC acceptor. kcat is 0.004 sec(-1) for Glc transfer with beta-glucosyl-
CC DOG as sugar acceptor. kcat is 0.03 sec(-1) for Gal transfer with
CC beta-glucosyl-DOG as sugar acceptor.;
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21835921}.
CC -!- MISCELLANEOUS: The local lipid environment around the enzyme affects
CC both the extent of head group elongation and total amounts of
CC glycolipids produced. {ECO:0000305|PubMed:21835921}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; L43967; AAC71559.1; -; Genomic_DNA.
DR RefSeq; WP_010869439.1; NC_000908.2.
DR AlphaFoldDB; Q9ZB73; -.
DR SMR; Q9ZB73; -.
DR STRING; 243273.MG_517; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAC71559; AAC71559; MG_517.
DR KEGG; mge:MG_517; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_813338_0_0_14; -.
DR OMA; QDIPWTT; -.
DR OrthoDB; 865276at2; -.
DR BioCyc; MGEN243273:G1GJ2-419-MON; -.
DR BRENDA; 2.4.1.315; 3528.
DR SABIO-RK; Q9ZB73; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046509; F:1,2-diacylglycerol 3-beta-galactosyltransferase activity; IEA:RHEA.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycerol metabolism;
KW Glycosyltransferase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Membrane; Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="Processive diacylglycerol beta-glycosyltransferase"
FT /id="PRO_0000059245"
SQ SEQUENCE 341 AA; 40881 MW; 52D54E8F0A400DBF CRC64;
MDKLVSILVP CYKSKPFLKR FFNSLLKQDL NQAKIIFFND NVADETYEVL QKFKKEHNNL
AIEVYCDKQN EGIGKVRDKL VNLVTTPYFY FIDPDDCFNN KNVIKEIVES IKKEDFDLGV
LKSMVYLCFL KHDFIIKFLP LKGIFQGRVK LINNNNVNKL NYIKNNDQYI WNIVINTDFF
RKLNLTFESR LFEDIPIWYP MFFSSQKIVF IDVIGTNYFI RNDSLSTTIS APRYLNLIQC
YEKLYVNLSQ NGSLASFIDP NHKIEARFWR RQMFVWFALF SFEYFKKNFS ESKKILEKLF
VFLEKNGVYE RVFQTKNQGI YYIWVQRLKY FKHVLESKSD N
