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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Binding sitei35GDP-Man; via carbonyl oxygen1
    Binding sitei66GDP-Man1
    Binding sitei76GDP-Man1
    Binding sitei100GDP-Man1
    Metal bindingi102Divalent cation1
    Binding sitei131D-glycerate1
    Binding sitei163GDP-Man; via carbonyl oxygen1
    Binding sitei192GDP-Man1
    Metal bindingi217Divalent cation1
    Binding sitei218GDP-Man1
    Binding sitei220GDP-Man1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi9K → 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 Publication1
    Mutagenesisi11E → A: Results in a modest increase in the catalytic efficiency coupled with a decrease in the affinity binding value for GDP-Man. 1 Publication1
    Mutagenesisi37Y → 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 Publication1
    Mutagenesisi66Q → 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 Publication1
    Mutagenesisi76K → 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 Publication1
    Mutagenesisi100D → A: Completely inactive. 1 Publication1
    Mutagenesisi102D → A: Completely inactive. 1 Publication1
    Mutagenesisi131R → A: Completely inactive. 1 Publication1
    Mutagenesisi135D → 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 Publication1
    Mutagenesisi139T → 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 Publication1
    Mutagenesisi189W → 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 Publication1
    Mutagenesisi192D → A: Completely inactive. 1 Publication1
    Mutagenesisi217H → 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 Publication1
    Mutagenesisi218R → 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 Publication1
    Mutagenesisi220Y → A: Results in a 500-fold decrease in the affinity binding value for D-glycerate in the presence of saturating GDP-Man. 1 Publication1
    Mutagenesisi220Y → F: Results in a 1500-fold decrease in the affinity binding value for D-glycerate in the presence of saturating GDP-Man. 1 Publication1
    Mutagenesisi229M → A: Minor influence. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004298612 – 397Mannosylglycerate synthaseAdd BLAST396

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60494N.
    STRINGi518766.Rmar_1220.

    Structurei

    Secondary structure

    1397
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 7Combined sources5
    Helixi13 – 25Combined sources13
    Beta strandi31 – 38Combined sources8
    Helixi41 – 57Combined sources17
    Beta strandi61 – 65Combined sources5
    Beta strandi70 – 75Combined sources6
    Helixi76 – 90Combined sources15
    Beta strandi94 – 98Combined sources5
    Helixi108 – 119Combined sources12
    Beta strandi123 – 128Combined sources6
    Helixi137 – 141Combined sources5
    Helixi143 – 150Combined sources8
    Helixi156 – 158Combined sources3
    Beta strandi167 – 170Combined sources4
    Helixi171 – 179Combined sources9
    Helixi181 – 184Combined sources4
    Helixi191 – 201Combined sources11
    Beta strandi206 – 210Combined sources5
    Helixi223 – 226Combined sources4
    Helixi227 – 240Combined sources14
    Beta strandi251 – 253Combined sources3
    Helixi261 – 264Combined sources4
    Helixi271 – 278Combined sources8
    Helixi284 – 289Combined sources6
    Helixi290 – 292Combined sources3
    Helixi295 – 303Combined sources9
    Turni304 – 306Combined sources3
    Helixi315 – 328Combined sources14
    Helixi334 – 354Combined sources21
    Helixi356 – 358Combined sources3
    Helixi360 – 380Combined sources21

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9RFR0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni7 – 11GDP-Man binding5
    Regioni100 – 101GDP-Man binding2
    Regioni136 – 139D-glycerate binding4

    Sequence similaritiesi

    Belongs to the glycosyltransferase 78 family.Curated

    Phylogenomic databases

    eggNOGiENOG410ZSHR. LUCA.

    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
    PDB 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.
    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.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9RFR0.
    PROiQ9RFR0.

    Family and domain databases

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

    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: November 2, 2016
    This is version 70 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.