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 02-SEP-2026, entry version 110. 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 Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasma pneumoniae). OC Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; 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 / Subtype 1; 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 + UDP + H(+); 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 + UDP + H(+); 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 + UDP + H(+); 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 + UDP + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00089; AAB96007.1; -; Genomic_DNA. DR PIR; S73685; S73685. 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 PaxDb; 272634-MPN_483; -. 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 OrthoDB; 9785185at2; -. DR BioCyc; MPNE272634:G1GJ3-791-MONOMER; -. 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:0008610; P:lipid biosynthetic process; IDA:UniProtKB. DR CDD; cd00761; Glyco_tranf_GTA_type; 1. DR FunFam; 3.90.550.10:FF:000323; Processive diacylglycerol beta-glycosyltransferase; 1. DR Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR22916; GLYCOSYLTRANSFERASE; 1. DR PANTHER; PTHR22916:SF51; GLYCOSYLTRANSFERASE EPSH-RELATED; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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 //