PBDGT_MYCPN
ID PBDGT_MYCPN Reviewed; 341 AA.
AC P75302;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Processive diacylglycerol beta-glycosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Beta-monoglycosyldiacylglycerol synthase;
DE Short=Beta-MGS;
DE Short=MGlyDAG synthase;
DE AltName: Full=Diglycosyldiacylglycerol synthase;
DE Short=Beta-DGS;
DE Short=DGlyDAG synthase;
DE AltName: Full=Glycosyl-beta-1,6-galactosyldiacylglycerol synthase;
DE AltName: Full=UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase;
DE AltName: Full=UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase;
GN OrderedLocusNames=MPN_483; ORFNames=MP359, P01_orf341;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=17697098; DOI=10.1111/j.1365-2958.2007.05865.x;
RA Klement M.L., Ojemyr L., Tagscherer K.E., Widmalm G., Wieslander A.;
RT "A processive lipid glycosyltransferase in the small human pathogen
RT Mycoplasma pneumoniae: involvement in host immune response.";
RL Mol. Microbiol. 65:1444-1457(2007).
CC -!- FUNCTION: Processive glycosyltransferase involved in the biosynthesis
CC of both the non-bilayer-prone beta-monoglycosyldiacylglycerol and the
CC bilayer-forming membrane lipid glucosyl-galactosyldiacylglycerol and
CC digalactosyl-diacylglycerol. These components contribute to regulate
CC the properties and stability of the membrane. Catalyzes sequentially
CC the transfers of glucosyl or galactosyl residues from UDP-Glc or UDP-
CC Gal to diacylglycerol (DAG) acceptor to form the corresponding beta-
CC glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-diacyl-sn-glycerol).
CC Then, only beta-galactosyl-DAG (3-O-(beta-D-galactopyranosyl)-1,2-
CC diacyl-sn-glycerol) can act as acceptor to give the beta-glycosyl-beta-
CC galactosyl-DAG product (3-O-(beta-D-glycopyranosyl-(1->6)-D-
CC galactopyranosyl)-1,2-diacyl-sn-glycerol). It can also use alpha-Gal-
CC beta-Gal-DAG, ceramide (Cer) and beta-Gal-Cer as sugar acceptors. The
CC enzyme is supposed to be mainly a galactosyltransferase, with higher
CC glycosyltransferase activity for the addition of the second glycosyl on
CC beta-Gal-DAG as acceptor. The main glycolipid produced in vivo is beta-
CC Glc-beta-Gal-DAG with a beta-1,6 linkage.
CC {ECO:0000269|PubMed:17697098}.
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:17697098};
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:17697098};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-
CC D-glucose = a 1,2-diacyl-3-O-[beta-D-glucopyranosyl-(1->6)-beta-D-
CC galactopyranosyl]-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:53752,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:137667;
CC Evidence={ECO:0000269|PubMed:17697098};
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:17697098};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by the negatively charged lipid
CC phosphatidylglycerol (PG). {ECO:0000269|PubMed:17697098}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
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:17697098}.
CC -!- MISCELLANEOUS: Glycolipids such as beta-Gal-DAG, alpha-Gal-beta-Gal-
CC DAG, beta-Glc-beta-Gal-DAG and beta-Gal-Cer are highly immunogenic and
CC are reactive towards IgM antibodies. Glycolipids with a terminal beta-
CC Gal are more reactive than the ones with a beta-Glc residue
CC (PubMed:17697098). {ECO:0000305|PubMed:17697098}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; U00089; AAB96007.1; -; Genomic_DNA.
DR PIR; S73685; S73685.
DR RefSeq; NP_110171.1; NC_000912.1.
DR RefSeq; WP_010874839.1; NC_000912.1.
DR AlphaFoldDB; P75302; -.
DR SMR; P75302; -.
DR IntAct; P75302; 3.
DR STRING; 272634.MPN_483; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAB96007; AAB96007; MPN_483.
DR GeneID; 66608844; -.
DR KEGG; mpn:MPN_483; -.
DR PATRIC; fig|272634.6.peg.522; -.
DR HOGENOM; CLU_813338_0_0_14; -.
DR OMA; QDIPWTT; -.
DR BioCyc; MPNE272634:G1GJ3-791-MON; -.
DR Proteomes; UP000000808; 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: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_0000059246"
SQ 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
