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Protein

Mannosylglycerate synthase

Gene

mgs

Organism
Rhodothermus marinus (Rhodothermus obamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the stress protectant 2-O-alpha-D-mannosyl glycerate (MG) which is produced in response to growth at supraoptimal temperature and salinity, and protects several enzymes against inactivation by temperature, freeze-drying and osmotic stress. Catalyzes the condensation of alpha-GDP-D-mannose (GDP-Man) with D-glycerate to produce alpha-mannosyl-D-glycerate. It is specific for GDP-Man, but it can also use alpha-GDP-D-glucose (GDP-Glc), beta-GDP-D-fuctose, alpha-UDP-D-mannose and alpha-UDP-D-glucose as sugar donors. It is specific for D-glycerate, but it can also use D-lactate and glycolate as sugar acceptors. This reaction occurs with a net retention of anomeric configuration; the newly formed glycosidic linkage has the same alpha configuration as the sugar donor.3 Publications

Catalytic activityi

GDP-alpha-D-mannose + D-glycerate = GDP + 2-O-(alpha-D-mannopyranosyl)-D-glycerate.3 Publications

Cofactori

Mg2+1 Publication, Ca2+1 Publication, Mn2+1 Publication, Ni2+1 Publication, Co2+1 PublicationNote: Divalent cations such as magnesium, calcium and to a lesser extent manganese, nickel and cobalt.1 Publication

Enzyme regulationi

Inhibited by GDP.1 Publication

Kineticsi

Kcat is 6.5 sec(-1) for mannosylglycerate synthase activity with D-glycerate as sugar acceptor (in the presence of calcium ions at 65 degrees Celsius (PubMed:15951819)). Kcat is 6.1 sec(-1) for mannosylglycerate synthase activity with GDP-Man as sugar donor (in the presence of calcium ions at 65 degrees Celsius (PubMed:15951819)). Kcat is 1.9 sec(-1) for mannosylglycerate synthase activity with D-glycerate (PubMed:21288903). Kcat is 1.1 sec(-1) for mannosylglycerate synthase activity with GDP-Glc as sugar donor (in the presence of calcium ions at 65 degrees Celsius (PubMed:15951819)). Kcat is 1.02 sec(-1) for mannosylglycerate synthase activity with GDP-Man and D-glycerate as sugar donor and acceptor, respectively (in the presence of calcium ions at 25 degrees Celsius (PubMed:15951819)). Kcat is 0.63 sec(-1) for mannosylglycerate synthase activity with GDP-Glc as sugar donor (in the presence of calcium ions at 25 degrees Celsius (PubMed:15951819)).2 Publications

  1. KM=2.2 µM for D-glycerate3 Publications
  2. KM=3.1 µM for GDP-Man3 Publications
  3. KM=81.2 µM for GDP-Man (in the presence of calcium ions at 25 degrees Celsius)3 Publications
  4. KM=89.4 µM for GDP-Man (in the presence of calcium ions at 65 degrees Celsius)3 Publications
  5. KM=96.5 µM for D-glycerate (in the presence of calcium ions at 65 degrees Celsius)3 Publications
  6. KM=121.9 µM for D-glycerate (in the presence of calcium ions at 25 degrees Celsius)3 Publications
  7. KM=124.9 µM for GDP-Glc (in the presence of calcium ions at 25 degrees Celsius)3 Publications
  8. KM=138.6 µM for GDP-Glc (in the presence of calcium ions at 65 degrees Celsius)3 Publications
  9. KM=300 µM for GDP-Man (at 90 degrees Celsius)3 Publications
  10. KM=600 µM for D-glycerate (at 90 degrees Celsius (PubMed 10585410))3 Publications

    pH dependencei

    Optimum pH is between 5.5 and 7.3 Publications

    Temperature dependencei

    Optimum temperature is between 85 and 90 degrees Celsius. It is stable at high temperatures, however at 90 degrees Celsius the stability of the enzyme is only moderate and 50% of the activity is lost after 30 minutes incubation. At 65 degrees Celsius, the specific enzymatic activity is 5-fold lower than the maximum value.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351GDP-Man; via carbonyl oxygen
    Binding sitei66 – 661GDP-Man
    Binding sitei76 – 761GDP-Man
    Binding sitei100 – 1001GDP-Man
    Metal bindingi102 – 1021Divalent cation
    Binding sitei131 – 1311D-glycerate
    Binding sitei163 – 1631GDP-Man; via carbonyl oxygen
    Binding sitei192 – 1921GDP-Man
    Metal bindingi217 – 2171Divalent cation
    Binding sitei218 – 2181GDP-Man
    Binding sitei220 – 2201GDP-Man

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB
    • transferase activity, transferring hexosyl groups Source: UniProtKB

    GO - Biological processi

    • mannosylglycerate biosynthetic process Source: CACAO
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Calcium, Cobalt, Magnesium, Manganese, Metal-binding, Nickel

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13377.
    BRENDAi2.4.1.269. 5425.

    Protein family/group databases

    CAZyiGT78. Glycosyltransferase Family 78.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosylglycerate synthase (EC:2.4.1.2693 Publications)
    Short name:
    MGS
    Gene namesi
    Name:mgs
    OrganismiRhodothermus marinus (Rhodothermus obamensis)
    Taxonomic identifieri29549 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeRhodothermus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91K → A: The catalytic efficiency is almost one order of magnitude higher than wild-type enzyme for both substrates. The mutation has little effect on the affinity binding value for GDP-Man and D-glycerate. 1 Publication
    Mutagenesisi11 – 111E → A: Results in a modest increase in the catalytic efficiency coupled with a decrease in the affinity binding value for GDP-Man. 1 Publication
    Mutagenesisi37 – 371Y → A: Significant increase in catalytic efficiency. The mutation has little effect on the affinity binding value for GDP-Man, however it shows an 4-fold decrease in the affinity binding value for D-glycerate. 1 Publication
    Mutagenesisi66 – 661Q → A: Results in an increase in the catalytic efficiency (up to 72-fold) coupled with a decrease in the affinity binding for both D-glycerate and GDP-Man. 1 Publication
    Mutagenesisi76 – 761K → A: Results in a 3-fold increase in the catalytic efficiency coupled with a decrease in affinity binding for D-glycerate and GDP-Man of 15- and 3-fold, respectively. 1 Publication
    Mutagenesisi100 – 1001D → A: Completely inactive. 1 Publication
    Mutagenesisi102 – 1021D → A: Completely inactive. 1 Publication
    Mutagenesisi131 – 1311R → A: Completely inactive. 1 Publication
    Mutagenesisi135 – 1351D → A: Results in a extremely low affinity binding value for D-glycerate (5600-fold lower than wild-type) and displays a slight increase in the catalytic efficiency (2-fold) compared with wild-type enzyme. 1 Publication
    Mutagenesisi139 – 1391T → A: Results in a modest decrease in the catalytic efficiency coupled with a 1500-fold decrease in the affinity binding value for D-glycerate. The mutant is 500-fold less active when D-lactate, rather than D-glycerate, is the acceptor substrate. 1 Publication
    Mutagenesisi189 – 1891W → A: Results in a 3-fold increase in the catalytic efficiency coupled with a 7-fold decrease in the affinity binding for D-glycerate compared with the wild-type enzyme. It does not influence utilization of GDP-Man. 1 Publication
    Mutagenesisi192 – 1921D → A: Completely inactive. 1 Publication
    Mutagenesisi217 – 2171H → A: Displays a significant change in metal preference. This mutant is essentially inactive in the presence of calcium ions (specific activity 1000-fold lower than wild-type), whereas the catalytic efficiency value is 23-fold lower in the presence of magnesium ions. 1 Publication
    Mutagenesisi218 – 2181R → A: Results in a significant increase in the catalytic efficiency coupled with a decrease in the affinity binding value for GDP-Man. It has only a modest influence on the affinity binding value for D-glycerate. 1 Publication
    Mutagenesisi220 – 2201Y → A: Results in a 500-fold decrease in the affinity binding value for D-glycerate in the presence of saturating GDP-Man. 1 Publication
    Mutagenesisi220 – 2201Y → F: Results in a 1500-fold decrease in the affinity binding value for D-glycerate in the presence of saturating GDP-Man. 1 Publication
    Mutagenesisi229 – 2291M → A: Minor influence. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 397396Mannosylglycerate synthasePRO_0000429861Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60494N.
    STRINGi518766.Rmar_1220.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75Combined sources
    Helixi13 – 2513Combined sources
    Beta strandi31 – 388Combined sources
    Helixi41 – 5717Combined sources
    Beta strandi61 – 655Combined sources
    Beta strandi70 – 756Combined sources
    Helixi76 – 9015Combined sources
    Beta strandi94 – 985Combined sources
    Helixi108 – 11912Combined sources
    Beta strandi123 – 1286Combined sources
    Helixi137 – 1415Combined sources
    Helixi143 – 1508Combined sources
    Helixi156 – 1583Combined sources
    Beta strandi167 – 1704Combined sources
    Helixi171 – 1799Combined sources
    Helixi181 – 1844Combined sources
    Helixi191 – 20111Combined sources
    Beta strandi206 – 2105Combined sources
    Helixi223 – 2264Combined sources
    Helixi227 – 24014Combined sources
    Beta strandi251 – 2533Combined sources
    Helixi261 – 2644Combined sources
    Helixi271 – 2788Combined sources
    Helixi284 – 2896Combined sources
    Helixi290 – 2923Combined sources
    Helixi295 – 3039Combined sources
    Turni304 – 3063Combined sources
    Helixi315 – 32814Combined sources
    Helixi334 – 35421Combined sources
    Helixi356 – 3583Combined sources
    Helixi360 – 38021Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BO4X-ray1.95A/B/C/D/E/F1-397[»]
    2BO6X-ray2.45A/B1-397[»]
    2BO7X-ray2.95A/B/C/D/E/F/G/H/I/J1-397[»]
    2BO8X-ray2.80A/B/C/D/E/F/G/H/I/J1-397[»]
    2Y4JX-ray2.30A/B1-382[»]
    ProteinModelPortaliQ9RFR0.
    SMRiQ9RFR0. Positions 2-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9RFR0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 115GDP-Man binding
    Regioni100 – 1012GDP-Man binding
    Regioni136 – 1394D-glycerate binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 78 family.Curated

    Phylogenomic databases

    eggNOGiENOG410ZSHR. LUCA.
    OrthoDBiEOG6FJNC1.

    Family and domain databases

    InterProiIPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9RFR0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLVVFPFKH EHPEVLLHNV RVAAAHPRVH EVLCIGYERD QTYEAVERAA
    60 70 80 90 100
    PEISRATGTP VSVRLQERLG TLRPGKGDGM NTALRYFLEE TQWERIHFYD
    110 120 130 140 150
    ADITSFGPDW ITKAEEAADF GYGLVRHYFP RASTDAMITW MITRTGFALL
    160 170 180 190 200
    WPHTELSWIE QPLGGELLMR REVAAMLYED ERVRRRSDWG IDTLYTFVTV
    210 220 230 240 250
    QQGVSIYECY IPEGKAHRLY GGLDDLRTML VECFAAIQSL QHEVVGQPAI
    260 270 280 290 300
    HRQEHPHRVP VHIAERVGYD VEATLHRLMQ HWTPRQVELL ELFTTPVREG
    310 320 330 340 350
    LRTCQRRPAF NFMDEMAWAA TYHVLLEHFQ PGDPDWEELL FKLWTTRVLN
    360 370 380 390
    YTMTVALRGY DYAQQYLYRM LGRYRYQAAL ENGRGHPVPP RAALSTA
    Length:397
    Mass (Da):46,126
    Last modified:May 1, 2000 - v1
    Checksum:i10303BFBF298E6EC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF173987 Genomic DNA. Translation: AAF16905.1.

    Genome annotation databases

    PATRICi32316523. VBIRhoMar93821_1234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF173987 Genomic DNA. Translation: AAF16905.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BO4X-ray1.95A/B/C/D/E/F1-397[»]
    2BO6X-ray2.45A/B1-397[»]
    2BO7X-ray2.95A/B/C/D/E/F/G/H/I/J1-397[»]
    2BO8X-ray2.80A/B/C/D/E/F/G/H/I/J1-397[»]
    2Y4JX-ray2.30A/B1-382[»]
    ProteinModelPortaliQ9RFR0.
    SMRiQ9RFR0. Positions 2-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60494N.
    STRINGi518766.Rmar_1220.

    Protein family/group databases

    CAZyiGT78. Glycosyltransferase Family 78.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    PATRICi32316523. VBIRhoMar93821_1234.

    Phylogenomic databases

    eggNOGiENOG410ZSHR. LUCA.
    OrthoDBiEOG6FJNC1.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13377.
    BRENDAi2.4.1.269. 5425.

    Miscellaneous databases

    EvolutionaryTraceiQ9RFR0.

    Family and domain databases

    InterProiIPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase."
      Martins L.O., Empadinhas N., Marugg J.D., Miguel C., Ferreira C., da Costa M.S., Santos H.
      J. Biol. Chem. 274:35407-35414(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Strain: ATCC 43812 / R-10 / DSM 4252.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-11; ASP-100 AND ARG-131, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-9; TYR-37; GLN-66; LYS-76; ASP-102; ASP-135; THR-139; TRP-189; ASP-192; HIS-217; ARG-218; TYR-220 AND MET-229, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiMGS_RHOMR
    AccessioniPrimary (citable) accession number: Q9RFR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 9, 2014
    Last sequence update: May 1, 2000
    Last modified: March 16, 2016
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The biosynthesis of mannosylglycerate in R.marinus can proceed via an other alternative pathway, in wich a mannosyl-3-phosphoglycerate synthase catalyzes the conversion of GDP mannose and D-3-phosphoglycerate into a phosphorylated intermediate, which is subsequently converted to mannosylglycerate by the action of a mannosyl-3-phosphoglycerate phosphatase. A noticeable feature distinguishing the two enzymatic systems involved in the synthesis of MG is their dependence on salt; while the mannosylglycerate synthase reaction is salt-independent, addition of NaCl or KCl is required to achieve full activity of the mannosyl-3-phosphoglycerate synthase/phosphatase system (PubMed:10585410).1 Publication

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    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 one 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.