MGH2_SELML
ID MGH2_SELML Reviewed; 488 AA.
AC D8T3S4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Mannosylglycerate hydrolase MGH2 {ECO:0000305};
DE EC=3.2.1.170 {ECO:0000250|UniProtKB:D8QTR2};
GN ORFNames=SELMODRAFT_447962 {ECO:0000312|EMBL:EFJ08650.1};
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG)
CC to D-glycerate and D-mannose. Can also hydrolyze alpha-D-
CC glucopyranosyl-glycerate (GG)with lower efficiency.
CC {ECO:0000250|UniProtKB:D8QTR2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate +
CC D-mannose; Xref=Rhea:RHEA:58456, ChEBI:CHEBI:4208, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16659, ChEBI:CHEBI:57541; EC=3.2.1.170;
CC Evidence={ECO:0000250|UniProtKB:D8QTR2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58457;
CC Evidence={ECO:0000250|UniProtKB:D8QTR2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-
CC glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510;
CC Evidence={ECO:0000250|UniProtKB:D8QTR2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32060;
CC Evidence={ECO:0000250|UniProtKB:D8QTR2};
CC -!- ACTIVITY REGULATION: Activity is not dependent on divalent cations, but
CC it is enhanced by Mn(2+). {ECO:0000250|UniProtKB:D8QTR2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; GL377671; EFJ08650.1; -; Genomic_DNA.
DR RefSeq; XP_002990235.1; XM_002990189.1.
DR AlphaFoldDB; D8T3S4; -.
DR SMR; D8T3S4; -.
DR PRIDE; D8T3S4; -.
DR EnsemblPlants; EFJ08650; EFJ08650; SELMODRAFT_447962.
DR GeneID; 9630789; -.
DR Gramene; EFJ08650; EFJ08650; SELMODRAFT_447962.
DR KEGG; smo:SELMODRAFT_447962; -.
DR eggNOG; ENOG502S06X; Eukaryota.
DR HOGENOM; CLU_015270_1_0_1; -.
DR InParanoid; D8T3S4; -.
DR OMA; SGICEYY; -.
DR OrthoDB; 942740at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..488
FT /note="Mannosylglycerate hydrolase MGH2"
FT /id="PRO_0000451957"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT ACT_SITE 459
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
FT BINDING 415..416
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K5BDL0"
SQ SEQUENCE 488 AA; 54528 MW; 66E3030AB17373AC CRC64;
MAGPVRCLPP VVEATSIPHA PPVISKEVSE IVNNMLSVAI PAAAAASAQD QRFASQFRCG
PEFATMKAQA LEACRKILAE NDQGGYTIPA KGLYPYQWNW DSALVSLGLA EMEEERAWEE
LDRLMSAQWE DGMVPHIVFH KPSSTYFPGP EIWGSPDKPR NSTGITQPPV AAISVRRLLE
EAKDKALALA MARKLFPKLL AWHRWFYRAR DPEGTGLVAT IHPWETGMDN SPAWDEALAR
VPIDDIPPYV RRDLGHVDAK MRPQKAEYDR YLTLLYRFRA LDYDEAKLYY ETPFRVTDLC
TNCILHKANE DLLWLAGATG ACTDESEIRG WTARANVAFD TLFDVEAGLY RCKDQLTGQF
LPAATSAGFL PLFAGVASGE KASAVARTLG RWLDDVAYGI PSCDPRDPWF EALRYWRGPV
WLIVNWMVSE GLKRYGYGEL AQRVERDSYE LVKNGGIFEY YCPLTGMGAG GGCFSWTAAM
CLAWLFKS
