MGS_SELML
ID MGS_SELML Reviewed; 422 AA.
AC D8S5L4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Mannosylglycerate synthase {ECO:0000303|PubMed:23179444};
DE EC=2.4.1.269 {ECO:0000269|PubMed:23179444};
GN Name=MGS {ECO:0000303|PubMed:23179444};
GN Synonyms=GT78A1 {ECO:0000312|EMBL:EFJ20192.1};
GN ORFNames=SELMODRAFT_452917 {ECO:0000312|EMBL:EFJ20192.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23179444; DOI=10.1007/s00425-012-1808-6;
RA Nobre A., Empadinhas N., Nobre M.F., Lourenco E.C., Maycock C.,
RA Ventura M.R., Mingote A., da Costa M.S.;
RT "The plant Selaginella moellendorffii possesses enzymes for synthesis and
RT hydrolysis of the compatible solutes mannosylglycerate and
RT glucosylglycerate.";
RL Planta 237:891-901(2013).
CC -!- FUNCTION: Involved in the biosynthesis of the compatible solute alpha-
CC D-mannosyl-glycerate (MG) (PubMed:23179444). Catalyzes the condensation
CC of GDP-alpha-D-mannose (GDP-Man) with D-glycerate to produce alpha-D-
CC mannosyl-glycerate (PubMed:23179444). Can also use GDP-alpha-D-glucose
CC (GDP-Glc) as sugar donor to produce alpha-D-glucopyranosyl-glycerate
CC (GG) (PubMed:23179444). {ECO:0000269|PubMed:23179444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + GDP-alpha-D-mannose = (2R)-2-O-(alpha-D-
CC mannosyl)-glycerate + GDP + H(+); Xref=Rhea:RHEA:30639,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:57541, ChEBI:CHEBI:58189; EC=2.4.1.269;
CC Evidence={ECO:0000269|PubMed:23179444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30640;
CC Evidence={ECO:0000269|PubMed:23179444};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + GDP-alpha-D-glucose = (2R)-2-O-(alpha-D-
CC glucopyranosyl)-glycerate + GDP + H(+); Xref=Rhea:RHEA:65940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:62230, ChEBI:CHEBI:62510;
CC Evidence={ECO:0000269|PubMed:23179444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65941;
CC Evidence={ECO:0000269|PubMed:23179444};
CC -!- ACTIVITY REGULATION: Activity is not dependent on divalent cations, but
CC it is enhanced by Mg(2+). {ECO:0000269|PubMed:23179444}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for GDP-alpha-D-mannose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23179444};
CC KM=4.4 mM for D-glycerate (with GDP-alpha-D-mannose as cosubstrate
CC and at 50 degrees Celsius) {ECO:0000269|PubMed:23179444};
CC KM=1.0 mM for GDP-alpha-D-glucose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23179444};
CC KM=3.4 mM for D-glycerate (with GDP-alpha-D-glucose as cosubstrate
CC and at 50 degrees Celsius) {ECO:0000269|PubMed:23179444};
CC Vmax=9.5 umol/min/mg enzyme with GDP-alpha-D-mannose as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:23179444};
CC Vmax=10.9 umol/min/mg enzyme with D-glycerate as substrate (with GDP-
CC alpha-D-mannose as cosubstrate and at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23179444};
CC Vmax=8.0 umol/min/mg enzyme with GDP-alpha-D-glucose as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:23179444};
CC Vmax=11.0 umol/min/mg enzyme with D-glycerate as substrate (with GDP-
CC alpha-D-glucose as cosubstrate and at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23179444};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:23179444};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:23179444};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 78 family.
CC {ECO:0000305}.
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DR EMBL; GL377603; EFJ20192.1; -; Genomic_DNA.
DR RefSeq; XP_002978745.1; XM_002978699.1.
DR AlphaFoldDB; D8S5L4; -.
DR SMR; D8S5L4; -.
DR PRIDE; D8S5L4; -.
DR EnsemblPlants; EFJ20192; EFJ20192; SELMODRAFT_452917.
DR GeneID; 9658694; -.
DR Gramene; EFJ20192; EFJ20192; SELMODRAFT_452917.
DR KEGG; smo:SELMODRAFT_452917; -.
DR eggNOG; ENOG502SJKF; Eukaryota.
DR HOGENOM; CLU_694216_0_0_1; -.
DR InParanoid; D8S5L4; -.
DR OMA; RSSTDAM; -.
DR OrthoDB; 836280at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0102921; F:mannosylglycerate synthase activity; IDA:UniProtKB.
DR GO; GO:0051479; P:mannosylglycerate biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 2.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..422
FT /note="Mannosylglycerate synthase"
FT /id="PRO_0000451955"
FT BINDING 7..11
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 66
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 77
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 101..102
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 101
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 132
FT /ligand="(R)-glycerate"
FT /ligand_id="ChEBI:CHEBI:16659"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 137..140
FT /ligand="(R)-glycerate"
FT /ligand_id="ChEBI:CHEBI:16659"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 164
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 193
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
FT BINDING 221
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT /evidence="ECO:0000250|UniProtKB:Q9RFR0"
SQ SEQUENCE 422 AA; 47867 MW; 1A37F864201A376A CRC64;
MSLVCFPFKE EDVAVVVRNV ECAAAHPRVS TVLCVGYSKG ETWCAIEAKR PSIESSTGKR
IILLQQKRIG VSLRSGKGDG MNTALAYFLD HTELKRIHFY DSDIVSFSAD WITKAERQAD
LDFDVVRHYF PRSSTDAMIT WFVTKIGFCL LWPKTVLPFI EQPLGGELLL TRKAAEALYT
DHRVRGQSDW GIDTLYTFIM VQKGLHLAEV YIPEGKVHAL YSGLRDLRTM LVECFSAMQS
LKDEAVPLNE GTHRMEYTRP VPELVKQKVG YDVEKTLKLL RSNWTQGQRD LLQKHFDPAL
AKGLLNASEW PTWGFADEEA WVAAYRTLLV HFEKGDEDWE ELLFKIWVSR VLNHTMRHSL
RGYDAALDAL RSLIWETQHQ SAMLSKSAAA NHHIVSGHSA SEALPRTAGQ LREKRMDAAC
AV
