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Protein

Processive diacylglycerol beta-glycosyltransferase

Gene

MPN_483

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol.1 Publication
UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D-galactopyranosyl)-sn-glycerol.1 Publication
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.1 Publication
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.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by the negatively charged lipid phosphatidylglycerol (PG).1 Publication

GO - Molecular functioni

GO - Biological processi

  • glycerol metabolic process Source: UniProtKB-KW
  • membrane lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycerol metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMPNE272634:GJ6Z-524-MONOMER.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Processive diacylglycerol beta-glycosyltransferase (EC:2.4.1.-)
Alternative name(s):
Beta-monoglycosyldiacylglycerol synthase
Short name:
Beta-MGS
Short name:
MGlyDAG synthase
Diglycosyldiacylglycerol synthase
Short name:
Beta-DGS
Short name:
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
Gene namesi
Ordered Locus Names:MPN_483
ORF Names:MP359, P01_orf341
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000808 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Processive diacylglycerol beta-glycosyltransferasePRO_0000059246Add
BLAST

Proteomic databases

PaxDbiP75302.

Interactioni

Protein-protein interaction databases

IntActiP75302. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP75302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiCOG0463.
KOiK19004.
OMAiDQTPDNS.
OrthoDBiEOG6WQD5X.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P75302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKLISILVP CYQSQPFLDR FFKSLLKQDW NGVKVIFFND NKPDPTYEIL
60 70 80 90 100
KQFQQAHPQL AIEVHCGEKN VGVGGSRDQL INYVDTPYFY FVDPDDEFSD
110 120 130 140 150
PNCFKAIVET IQGENFDIAV LNSIVYLQML KNDFLIKHIP LKNIFQGKVK
160 170 180 190 200
LNPDNTVNHL HYIQNNDQYI WNIVINTAFF KALDLQFVNR FIEDIAVWFP
210 220 230 240 250
IMFKAQKVLW IDVNGVNYYL RPNSASTQKN SIKLLSFIEA YERLYFHLKK
260 270 280 290 300
VGKLADFIDP NNKIESRFWR RQAFIWFSFI NVSWMKAEFE QTKSVLQKLF
310 320 330 340
DFMEANGIYD RVFTNKHHGI YLLWVNRLKH FKKLVQAQPH L
Length:341
Mass (Da):40,415
Last modified:February 1, 1997 - v1
Checksum:iC209F50D714CB3D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96007.1.
PIRiS73685.
RefSeqiNP_110171.1. NC_000912.1.
WP_010874839.1. NC_000912.1.

Genome annotation databases

EnsemblBacteriaiAAB96007; AAB96007; MPN_483.
GeneIDi876759.
KEGGimpn:MPN483.
PATRICi20022390. VBIMycPne110_0522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96007.1.
PIRiS73685.
RefSeqiNP_110171.1. NC_000912.1.
WP_010874839.1. NC_000912.1.

3D structure databases

ProteinModelPortaliP75302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP75302. 3 interactions.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiP75302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB96007; AAB96007; MPN_483.
GeneIDi876759.
KEGGimpn:MPN483.
PATRICi20022390. VBIMycPne110_0522.

Phylogenomic databases

eggNOGiCOG0463.
KOiK19004.
OMAiDQTPDNS.
OrthoDBiEOG6WQD5X.

Enzyme and pathway databases

BioCyciMPNE272634:GJ6Z-524-MONOMER.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
    Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
    Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29342 / M129.
  2. "A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response."
    Klement M.L., Ojemyr L., Tagscherer K.E., Widmalm G., Wieslander A.
    Mol. Microbiol. 65:1444-1457(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
    Strain: ATCC 29342 / M129.

Entry informationi

Entry nameiPBDGT_MYCPN
AccessioniPrimary (citable) accession number: P75302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: July 22, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The local lipid environment around the enzyme affects both the extent of head group elongation and total amounts of glycolipids produced.1 Publication
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).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycoplasma pneumoniae
    Mycoplasma pneumoniae (strain M129): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.