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

 PBDGT_MYCPN             Reviewed;         341 AA.
P75302;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-FEB-2018, entry version 85.
RecName: Full=Processive diacylglycerol beta-glycosyltransferase;
EC=2.4.1.-;
AltName: Full=Beta-monoglycosyldiacylglycerol synthase;
Short=Beta-MGS;
Short=MGlyDAG synthase;
AltName: Full=Diglycosyldiacylglycerol synthase;
Short=Beta-DGS;
Short=DGlyDAG synthase;
AltName: Full=Glycosyl-beta-1,6-galactosyldiacylglycerol synthase;
AltName: Full=UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase;
AltName: Full=UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase;
OrderedLocusNames=MPN_483; ORFNames=MP359, P01_orf341;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
[2]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND SUBSTRATE
SPECIFICITY.
STRAIN=ATCC 29342 / M129;
PubMed=17697098; DOI=10.1111/j.1365-2958.2007.05865.x;
Klement M.L., Ojemyr L., Tagscherer K.E., Widmalm G., Wieslander A.;
"A processive lipid glycosyltransferase in the small human pathogen
Mycoplasma pneumoniae: involvement in host immune response.";
Mol. Microbiol. 65:1444-1457(2007).
-!- FUNCTION: Processive glycosyltransferase involved in the
biosynthesis of both the non-bilayer-prone beta-
monoglycosyldiacylglycerol and the bilayer-forming membrane lipid
glucosyl-galactosyldiacylglycerol and digalactosyl-diacylglycerol.
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).
Then, only beta-galactosyl-DAG (3-O-(beta-D-galactopyranosyl)-1,2-
diacyl-sn-glycerol) can act as acceptor to give the beta-glycosyl-
beta-galactosyl-DAG product (3-O-(beta-D-glycopyranosyl-(1->6)-D-
galactopyranosyl)-1,2-diacyl-sn-glycerol). It can also use alpha-
Gal-beta-Gal-DAG, ceramide (Cer) and beta-Gal-Cer as sugar
acceptors. The enzyme is supposed to be mainly a
galactosyltransferase, with higher glycosyltransferase activity
for the addition of the second glycosyl on beta-Gal-DAG as
acceptor. The main glycolipid produced in vivo is beta-Glc-beta-
Gal-DAG with a beta-1,6 linkage. {ECO:0000269|PubMed:17697098}.
-!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-sn-glycerol = UDP +
1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:17697098}.
-!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP +
1,2-diacyl-3-O-(beta-D-galactopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:17697098}.
-!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-3-O-(beta-D-
galactopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D-
glucopyranosyl-(1->6)-O-beta-D-galactopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:17697098}.
-!- 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:17697098}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by the negatively charged lipid
phosphatidylglycerol (PG). {ECO:0000269|PubMed:17697098}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- 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:17697098}.
-!- MISCELLANEOUS: Glycolipids such as beta-Gal-DAG, alpha-Gal-beta-
Gal-DAG, beta-Glc-beta-Gal-DAG and beta-Gal-Cer are highly
immunogenic and are reactive towards IgM antibodies. Glycolipids
with a terminal beta-Gal are more reactive than the ones with a
beta-Glc residue (PubMed:17697098). {ECO:0000305|PubMed:17697098}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
{ECO:0000305}.
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EMBL; U00089; AAB96007.1; -; Genomic_DNA.
PIR; S73685; S73685.
RefSeq; NP_110171.1; NC_000912.1.
RefSeq; WP_010874839.1; NC_000912.1.
ProteinModelPortal; P75302; -.
SMR; P75302; -.
IntAct; P75302; 3.
CAZy; GT2; Glycosyltransferase Family 2.
EnsemblBacteria; AAB96007; AAB96007; MPN_483.
GeneID; 876759; -.
KEGG; mpn:MPN483; -.
PATRIC; fig|272634.6.peg.522; -.
KO; K19004; -.
OMA; DQTPDNS; -.
BioCyc; MPNE272634:G1GJ3-791-MONOMER; -.
Proteomes; UP000000808; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
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_0000059246.
SEQUENCE 341 AA; 40415 MW; C209F50D714CB3D0 CRC64;
MNKLISILVP CYQSQPFLDR FFKSLLKQDW NGVKVIFFND NKPDPTYEIL KQFQQAHPQL
AIEVHCGEKN VGVGGSRDQL INYVDTPYFY FVDPDDEFSD PNCFKAIVET IQGENFDIAV
LNSIVYLQML KNDFLIKHIP LKNIFQGKVK LNPDNTVNHL HYIQNNDQYI WNIVINTAFF
KALDLQFVNR FIEDIAVWFP IMFKAQKVLW IDVNGVNYYL RPNSASTQKN SIKLLSFIEA
YERLYFHLKK VGKLADFIDP NNKIESRFWR RQAFIWFSFI NVSWMKAEFE QTKSVLQKLF
DFMEANGIYD RVFTNKHHGI YLLWVNRLKH FKKLVQAQPH L


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