ID MGDG_SPIOL Reviewed; 522 AA. AC Q9SM44; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 08-NOV-2023, entry version 59. DE RecName: Full=Monogalactosyldiacylglycerol synthase, chloroplastic; DE Short=SoMGD1; DE EC=2.4.1.46; DE AltName: Full=MGDG synthase type A; DE Flags: Precursor; GN Name=MGD A; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=10518794; DOI=10.1046/j.1432-1327.1999.00801.x; RA Miege C., Marechal E., Shimojima M., Awai K., Block M.A., Ohta H., RA Takamiya K., Douce R., Joyard J.; RT "Biochemical and topological properties of type A MGDG synthase, a spinach RT chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic RT and eukaryotic MGDG."; RL Eur. J. Biochem. 265:990-1001(1999). RN [2] RP CHARACTERIZATION. RX PubMed=8119920; DOI=10.1016/s0021-9258(17)37531-2; RA Marechal E., Block M.A., Joyard J., Douce R.; RT "Kinetic properties of monogalactosyldiacylglycerol synthase from spinach RT chloroplast envelope membranes."; RL J. Biol. Chem. 269:5788-5798(1994). RN [3] RP CHARACTERIZATION, AND ACTIVITY REGULATION. RX PubMed=7890698; DOI=10.1074/jbc.270.11.5714; RA Marechal E., Miege C., Block M.A., Douce R., Joyard J.; RT "The catalytic site of monogalactosyldiacylglycerol synthase from spinach RT chloroplast envelope membranes. Biochemical analysis of the structure and RT of the metal content."; RL J. Biol. Chem. 270:5714-5722(1995). RN [4] RP BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF RP TRP-171; GLU-173; TRP-177; HIS-240; HIS-245; CYS-284; CYS-286; RP 343-GLY--GLY-347; GLU-346; CYS-378; ARG-380; PHE-402; CYS-415; LYS-419; RP GLU-427; GLU-445 AND ASN-448. RX PubMed=16009708; DOI=10.1074/jbc.m505622200; RA Botte C., Jeanneau C., Snajdrova L., Bastien O., Imberty A., Breton C., RA Marechal E.; RT "Molecular modeling and site-directed mutagenesis of plant chloroplast RT monogalactosyldiacylglycerol synthase reveal critical residues for RT activity."; RL J. Biol. Chem. 280:34691-34701(2005). CC -!- FUNCTION: Involved in the synthesis of the major structural component CC of photosynthetic membranes. The 1,2-diacylglycerol substrate CC preference is 18:2/18:2 > 18:0/18:1 > 18:1/18:1 > 18:1/16:0 > 16:0/18:2 CC > 18:3/18:3 > 16:0/18:1 > 16:0/16:0 > 18:0/18:0. CC {ECO:0000269|PubMed:10518794}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-galactose = a 1,2- CC diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+) + UDP; CC Xref=Rhea:RHEA:14945, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, CC ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.46; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC -!- ACTIVITY REGULATION: Inhibited by ortho-phenanthroline and UDP CC (competitive inhibitor relatively to UDP-Gal only) and inactivated by CC citraconic anhydride, tert-butoxycarbonyl-L-methionine CC hydrosuccinimidyl ester (SLR) and N-ethylmaleimide (NEM). CC {ECO:0000269|PubMed:10518794, ECO:0000269|PubMed:7890698}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.65 mM for UDP-Gal {ECO:0000269|PubMed:16009708}; CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane CC {ECO:0000269|PubMed:10518794}. CC -!- DOMAIN: The C-terminal domain (308-483) is involved in UDP-Gal binding CC while the N-terminal domains (131-307) is involved in dyacylglycerol CC binding. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ249607; CAB56218.1; -; mRNA. DR AlphaFoldDB; Q9SM44; -. DR SMR; Q9SM44; -. DR CAZy; GT28; Glycosyltransferase Family 28. DR KEGG; ag:CAB56218; -. DR OrthoDB; 101156at2759; -. DR BRENDA; 2.4.1.46; 5812. DR SABIO-RK; Q9SM44; -. DR Proteomes; UP001155700; Unplaced. DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046509; F:1,2-diacylglycerol 3-beta-galactosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro. DR CDD; cd17507; GT28_Beta-DGS-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR InterPro; IPR009695; Diacylglyc_glucosyltr_N. DR InterPro; IPR007235; Glyco_trans_28_C. DR PANTHER; PTHR43025; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE; 1. DR PANTHER; PTHR43025:SF3; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE 1, CHLOROPLASTIC; 1. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR Pfam; PF06925; MGDG_synth; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 1: Evidence at protein level; KW Chloroplast; Glycosyltransferase; Membrane; Plastid; KW Plastid inner membrane; Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..98 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 99..522 FT /note="Monogalactosyldiacylglycerol synthase, FT chloroplastic" FT /id="PRO_5000065674" FT SITE 422 FT /note="Substrate specificity for galactose" FT MUTAGEN 171 FT /note="W->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 173 FT /note="E->N: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 177 FT /note="W->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 240 FT /note="H->A: Total loss of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 245 FT /note="H->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 284 FT /note="C->A: No effect." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 286 FT /note="C->A: No effect." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 343..347 FT /note="Missing: Total loss of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 346 FT /note="E->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 378 FT /note="C->A: 25% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 380 FT /note="R->E: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 402 FT /note="F->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 415 FT /note="C->A: No effect." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 419 FT /note="K->A: Total loss of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 427 FT /note="E->A: Total loss of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 445 FT /note="E->A: Total loss of activity." FT /evidence="ECO:0000269|PubMed:16009708" FT MUTAGEN 448 FT /note="N->A: 90% reduction of activity." FT /evidence="ECO:0000269|PubMed:16009708" SQ SEQUENCE 522 AA; 57511 MW; 02E2B929732551A7 CRC64; MSHPSTVTSE PSNLLDFVPK LGNFVLNSSL HGNNSNGYSS FSSNSVHFGG LATQNRYKFV NSLSFSKEGS NLKRILSDFN RVIRLHCDRI PLGFSSIGLN SGESNGVSDN GHGVLEDVRV PVNAVEPESP KRVLILMSDT GGGHRASAEA IKAAFNEEFG DDYQVFVTDL WSEHTPWPFN QLPRSYNFLV KHGPLWKMMY YGTSPRVIHQ SNFAATSVFI AREVARGLMK YQPDIIISVH PLMQHVPLRI LRGRGLLEKI VFTTVVTDLS TCHPTWFHKL VTRCYCPSNE VAKRATKAGL QPSQIKVYGL PVRPSFVRSV RPKNELRKEL GMDEHLPAVL LMGGGEGMGP IEATARALGN ALYDANLGEP TGQLLVICGR NKKLAGKLSS IDWKIPVQVK GFVTKIEECM GACDCIITKA GPGTIAEAMI RGLPIILNDY IAGQEAGNVP YVIENGIGKY LKSPKEIAKT VSQWFGPKAN ELQIMSQNAL KHARPDAVFK IVHDLDELVR QKIFVRQYSC AA //