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RHOMR:MGS
Contents
| Species (Taxon ID) | Rhodothermus marinus (Rhodothermus obamensis). (29549) | |
| Gene Name(s) | mgs | |
| Protein Name(s) | Mannosylglycerate synthase | |
| External Links | ||
| UniProt | Q9RFR0 | |
| EMBL | AF173987 | |
| RefSeq | YP_003290498.1 | |
| PDB | 2BO4 2BO6 2BO7 2BO8 2Y4J | |
| PDBsum | 2BO4 2BO6 2BO7 2BO8 2Y4J | |
| ProteinModelPortal | Q9RFR0 | |
| SMR | Q9RFR0 | |
| DIP | DIP-60494N | |
| CAZy | GT78 | |
| GeneID | 8567867 | |
| KEGG | rmr:Rmar_1220 | |
| PATRIC | 32316523 | |
| OrthoDB | EOG6FJNC1 | |
| BioCyc | MetaCyc:MONOMER-13377 | |
| EvolutionaryTrace | Q9RFR0 | |
| GO | GO:0046872 GO:0051479 | |
| InterPro | IPR029044 | |
| SUPFAM | SSF53448 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0051479 |
mannosylglycerate biosynthetic process |
ECO:0000314 |
P |
Table 2 shows the activity of the native and recombinant enzymes and their ability to utilize substrates in the mannosylglycerate biosynthetic pathway. The native enzyme was obtained by electroelution and had a specific activity of 70mmol/min/mg of protein. The substrates used to determine the specificity of Mgs were GDP mannose, ADP mannose, UDP mannose,mannose 1-phosphate, and mannose 6-phosphate as sugar donors,and D-glycerate,L-glycerate, and D-3-P-glycerate as sugar acceptors. GDP glucose, UDP glucose, and ADP glucose were tested as sugar donors, and glycerol 3-phosphate, glucose 6-phosphate,glucose 1-phosphate, and glucose as sugar acceptors in an effort to also identify the ability of Mgs to catalyze the synthesis of other glycosylconjugates. Mgs was specific for GDP mannose and D-glycerate and had an absolute stereospecificity for D-glycerate. UDP mannose and GDP mannose were the only sugar nucleotides used by the enzyme. UDP mannose was used very little, less than 3% of that of GDP mannose. NaCl and KCl (50-500 mM concentrations) had no effect on enzyme activity. However, Mg2+ was required for optimal activity shown by the 2.5-fold lower activity in absence of the cation. |
complete | |||||
|
involved_in |
GO:0051479 |
mannosylglycerate biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016758 |
transferase activity, transferring hexosyl groups |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0102921 |
mannosylglycerate synthase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Martins, LO et al. (1999) Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase. J. Biol. Chem. 274 35407-14 PubMed GONUTS page
- ↑ 2.0 2.1 Nielsen, MM et al. (2011) Substrate and metal ion promiscuity in mannosylglycerate synthase. J. Biol. Chem. 286 15155-64 PubMed GONUTS page
- ↑ Flint, J et al. (2005) Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat. Struct. Mol. Biol. 12 608-14 PubMed GONUTS page
