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Processive diacylglycerol beta-glycosyltransferase (EC 2.4.1.-) (Beta-diglycosyldiacylglycerol synthase) (Beta-DGS) (DGlyDAG synthase) (Beta-monoglycosyldiacylglycerol synthase) (Beta-MGS) (MGlyDAG synthase) (Glycosyl-beta-1,6-glycosyldiacylglycerol synthase) (UDP-galactose:1,2-dioleoylglycerol 3-beta-D-galactosyltransferase) (UDP-glucose:1,2-dioleoylglycerol 3-beta-D-glucosyltransferase)

 PBDGT_MYCGE             Reviewed;         341 AA.
Q9ZB73;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-JUN-2017, entry version 84.
RecName: Full=Processive diacylglycerol beta-glycosyltransferase;
EC=2.4.1.-;
AltName: Full=Beta-diglycosyldiacylglycerol synthase;
Short=Beta-DGS;
Short=DGlyDAG synthase;
AltName: Full=Beta-monoglycosyldiacylglycerol synthase;
Short=Beta-MGS;
Short=MGlyDAG synthase;
AltName: Full=Glycosyl-beta-1,6-glycosyldiacylglycerol synthase;
AltName: Full=UDP-galactose:1,2-dioleoylglycerol 3-beta-D-galactosyltransferase;
AltName: Full=UDP-glucose:1,2-dioleoylglycerol 3-beta-D-glucosyltransferase;
OrderedLocusNames=MG335.2;
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=243273;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33530 / G-37 / NCTC 10195;
PubMed=7569993; DOI=10.1126/science.270.5235.397;
Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
"The minimal gene complement of Mycoplasma genitalium.";
Science 270:397-403(1995).
[2]
IDENTIFICATION.
Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=21835921; DOI=10.1074/jbc.M110.214148;
Andres E., Martinez N., Planas A.;
"Expression and characterization of a Mycoplasma genitalium
glycosyltransferase in membrane glycolipid biosynthesis: potential
target against mycoplasma infections.";
J. Biol. Chem. 286:35367-35379(2011).
-!- FUNCTION: Processive glycosyltransferase involved in the
biosynthesis of both the non-bilayer-prone beta-
monoglycosyldiacylglycerol and the bilayer-forming membrane lipid
beta-diglycosyldiacylglycerol. These components contribute to
regulate the properties and stability of the membrane. Catalyzes
sequentially the transfers of glucosyl or galactosyl residues from
UDP-Glc or UDP-Gal to diacylglycerol (DAG) acceptor to form the
corresponding beta-glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-
diacyl-sn-glycerol), which then acts as acceptor to give beta-
diglycosyl-DAG product (3-O-(beta-D-glycopyranosyl-beta-(1->6)-D-
glycopyranosyl)-1,2-diacyl-sn-glycerol). Dioleoylglycerol (DOG) is
a preferred sugar acceptor than 3-O-(beta-D-glucopyranosyl)-1,2-
dioleoyl-sn-glycerol. {ECO:0000269|PubMed:21835921}.
-!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-sn-glycerol = UDP +
1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:21835921}.
-!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP +
1,2-diacyl-3-O-(beta-D-galactopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:21835921}.
-!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-3-O-(beta-D-
glucopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D-
glucopyranosyl-(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:21835921}.
-!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-3-O-(beta-D-
galactopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D-
galactopyranosyl-(1->6)-O-beta-D-galactopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:21835921}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by the negatively charged lipid
dioleoylphosphatidylglycerol (DOPG) and inhibited by N-(n-
nonyl)deoxygalactonojirimycin (C9J).
{ECO:0000269|PubMed:21835921}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for UDP-Glc (in the presence of beta-glucosyl-DOG as
sugar acceptor at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:21835921};
KM=87 uM for UDP-Glc (in the presence of DOG as sugar acceptor
at pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
KM=90 uM for beta-glucosyl-DOG (in the presence of UDP-Gal as
sugar donor at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:21835921};
KM=234 uM for UDP-Gal (in the presence of DOG as sugar acceptor
at pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
KM=270 uM for DOG (in the presence of UDP-Gal as sugar donor at
pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921};
KM=479 uM for UDP-Gal (in the presence of beta-glucosyl-DOG as
sugar acceptor at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:21835921};
Note=Kcat is 0.27 sec(-1) for Glc transfer with DOG as sugar
acceptor. Kcat is 1.10 sec(-1) for Gal transfer with DOG as
sugar acceptor. Kcat is 0.004 sec(-1) for Glc transfer with
beta-glucosyl-DOG as sugar acceptor. Kcat is 0.03 sec(-1) for
Gal transfer with beta-glucosyl-DOG as sugar acceptor.;
-!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol
biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21835921}.
-!- MISCELLANEOUS: The local lipid environment around the enzyme
affects both the extent of head group elongation and total amounts
of glycolipids produced. {ECO:0000305|PubMed:21835921}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L43967; AAC71559.1; -; Genomic_DNA.
RefSeq; WP_010869439.1; NC_000908.2.
ProteinModelPortal; Q9ZB73; -.
SMR; Q9ZB73; -.
STRING; 243273.MgenG_010200003111; -.
CAZy; GT2; Glycosyltransferase Family 2.
EnsemblBacteria; AAC71559; AAC71559; MG_517.
KEGG; mge:MG_517; -.
eggNOG; COG0463; LUCA.
KO; K19004; -.
OMA; DQTPDNS; -.
OrthoDB; POG091H02KU; -.
BRENDA; 2.4.1.315; 3528.
UniPathway; UPA00894; -.
Proteomes; UP000000807; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IDA:UniProtKB.
GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF00535; Glycos_transf_2; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell membrane; Complete proteome;
Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis;
Lipid metabolism; Magnesium; Membrane; Reference proteome;
Transferase.
CHAIN 1 341 Processive diacylglycerol beta-
glycosyltransferase.
/FTId=PRO_0000059245.
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


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