MGH1_SELML
ID MGH1_SELML Reviewed; 488 AA.
AC D8QTR2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Mannosylglycerate hydrolase MGH1 {ECO:0000305};
DE EC=3.2.1.170 {ECO:0000269|PubMed:23179444};
GN Name=MGH {ECO:0000303|PubMed:23179444};
GN ORFNames=SELMODRAFT_437793 {ECO:0000312|EMBL:EFJ37158.1};
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: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG)
CC to D-glycerate and D-mannose (PubMed:23179444). Can also hydrolyze
CC alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency
CC (PubMed:23179444). {ECO:0000269|PubMed:23179444}.
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:0000269|PubMed:23179444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58457;
CC Evidence={ECO:0000269|PubMed:23179444};
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:0000269|PubMed:23179444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32060;
CC Evidence={ECO:0000269|PubMed:23179444};
CC -!- ACTIVITY REGULATION: Activity is not dependent on divalent cations, but
CC it is enhanced by Mn(2+). {ECO:0000269|PubMed:23179444}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.8 mM for 2-O-(alpha-D-mannosyl)-glycerate (at 40 degrees
CC Celsius) {ECO:0000269|PubMed:23179444};
CC KM=5.9 mM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at 40 degrees
CC Celsius) {ECO:0000269|PubMed:23179444};
CC Vmax=40.5 umol/min/mg enzyme with 2-O-(alpha-D-mannosyl)-glycerate as
CC substrate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444};
CC Vmax=7.3 umol/min/mg enzyme with 2-O-(alpha-D-glucopyranosyl)-D-
CC glycerate as substrate (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:23179444};
CC pH dependence:
CC Optimum pH is 6.0-6.50. {ECO:0000269|PubMed:23179444};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:23179444};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; GL377566; EFJ37158.1; -; Genomic_DNA.
DR RefSeq; XP_002961898.1; XM_002961852.1.
DR AlphaFoldDB; D8QTR2; -.
DR SMR; D8QTR2; -.
DR PRIDE; D8QTR2; -.
DR EnsemblPlants; EFJ37158; EFJ37158; SELMODRAFT_437793.
DR GeneID; 9656922; -.
DR Gramene; EFJ37158; EFJ37158; SELMODRAFT_437793.
DR KEGG; smo:SELMODRAFT_437793; -.
DR eggNOG; ENOG502S06X; Eukaryota.
DR HOGENOM; CLU_015270_1_0_1; -.
DR InParanoid; D8QTR2; -.
DR OMA; NSPRWDS; -.
DR OrthoDB; 942740at2759; -.
DR BioCyc; MetaCyc:MON-18220; -.
DR BRENDA; 3.2.1.208; 9844.
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:0102547; F:glucosylglycerate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102546; F:mannosylglycerate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0051478; P:mannosylglycerate metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..488
FT /note="Mannosylglycerate hydrolase MGH1"
FT /id="PRO_0000451956"
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; A8CE8C137B6E1590 CRC64;
MAGPVRCLPP VVEATSIPHA PPVISKEVSE IVNNMLSVAI PAAAAASAQD QRFASQFRCG
PEFTTMKAQA LEACRKILAE NDQGGYTIPA KGLYPYQWNW DSALVSLGLA EMEEERAWEE
LDRLMSAQWE DGMVPHIVFH KPSSTYFPGP EIWGSPDKPR NTTGITQPPV AAISVRRLLE
EAKDKALALA MARKLFPKLL AWHRWFYRAR DPEGTGLVAT IHPWETGMDN SPAWDEALAR
VPIDDIPPYV RRDLGHVDAK MRPQKAEYDR YLTLLYRFRA LDYDEAKLYY ETPFRVTDLC
TNCILHKANE DLLWLAGATG ACTDESEIRG WTARANVAFD TLFDVEAGLY RCKDQLTGQF
LPAATSAGFL PLFAGVASGE KASAVARTLG RWLDDVAYGI PSCDPRDPQF EALRYWRGPV
WLIVNWMVSE GLKRYGYGEL AQRVERDSYE LVKNGGIFEY YCPLTGMGAG GGCFSWTAAM
CLAWLFKT
