ID   MGDG1_ARATH             Reviewed;         533 AA.
AC   O81770; Q3E9T1; Q9MU68; W8Q2X7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Monogalactosyldiacylglycerol synthase 1, chloroplastic {ECO:0000305};
DE            Short=AtMGD1 {ECO:0000303|PubMed:11553816};
DE            EC=2.4.1.46 {ECO:0000269|PubMed:20023301, ECO:0000269|PubMed:26935252};
DE   AltName: Full=MGDG synthase type A {ECO:0000303|PubMed:11553816};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2797 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=MGD1 {ECO:0000303|PubMed:10869420};
GN   Synonyms=EMB2797 {ECO:0000305}, MGDA {ECO:0000303|PubMed:11553816};
GN   OrderedLocusNames=At4g31780 {ECO:0000312|Araport:AT4G31780};
GN   ORFNames=F28M20.30 {ECO:0000312|EMBL:CAA19745.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=10869420; DOI=10.1073/pnas.100132197;
RA   Jarvis P., Doermann P., Peto C.A., Lutes J., Benning C., Chory J.;
RT   "Galactolipid deficiency and abnormal chloroplast development in the
RT   Arabidopsis MGD synthase 1 mutant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:8175-8179(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11553816; DOI=10.1073/pnas.181331498;
RA   Awai K., Marechal E., Block M.A., Brun D., Masuda T., Shimada H.,
RA   Takamiya K., Ohta H., Joyard J.;
RT   "Two types of MGDG synthase genes, found widely in both 16:3 and 18:3
RT   plants, differentially mediate galactolipid syntheses in photosynthetic and
RT   nonphotosynthetic tissues in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10960-10965(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP   NOMENCLATURE.
RX   PubMed=11171188; DOI=10.1042/bst0280732;
RA   Marechal E., Awai K., Block M.A., Brun D., Masuda T., Shimada H.,
RA   Takamiya K., Ohta H., Joyard J.;
RT   "The multigenic family of monogalactosyl diacylglycerol synthases.";
RL   Biochem. Soc. Trans. 28:732-738(2000).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION BY LIGHT AND CYTOKININ.
RX   PubMed=14730084; DOI=10.1104/pp.103.032656;
RA   Kobayashi K., Awai K., Takamiya K., Ohta H.;
RT   "Arabidopsis type B monogalactosyldiacylglycerol synthase genes are
RT   expressed during pollen tube growth and induced by phosphate starvation.";
RL   Plant Physiol. 134:640-648(2004).
RN   [9]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=17940034; DOI=10.1073/pnas.0704680104;
RA   Kobayashi K., Kondo M., Fukuda H., Nishimura M., Ohta H.;
RT   "Galactolipid synthesis in chloroplast inner envelope is essential for
RT   proper thylakoid biogenesis, photosynthesis, and embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:17216-17221(2007).
RN   [10]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-150;
RP   HIS-155; THR-186; PRO-189; HIS-251; ARG-260; TRP-287 AND GLU-456.
RX   PubMed=20023301; DOI=10.1074/jbc.m109.071928;
RA   Dubots E., Audry M., Yamaryo Y., Bastien O., Ohta H., Breton C.,
RA   Marechal E., Block M.A.;
RT   "Activation of the chloroplast monogalactosyldiacylglycerol synthase MGD1
RT   by phosphatidic acid and phosphatidylglycerol.";
RL   J. Biol. Chem. 285:6003-6011(2010).
RN   [11]
RP   ACTIVITY REGULATION.
RX   PubMed=21946275; DOI=10.1038/nchembio.658;
RA   Botte C.Y., Deligny M., Roccia A., Bonneau A.L., Saidani N., Hardre H.,
RA   Aci S., Yamaryo-Botte Y., Jouhet J., Dubots E., Loizeau K., Bastien O.,
RA   Brehelin L., Joyard J., Cintrat J.C., Falconet D., Block M.A., Rousseau B.,
RA   Lopez R., Marechal E.;
RT   "Chemical inhibitors of monogalactosyldiacylglycerol synthases in
RT   Arabidopsis thaliana.";
RL   Nat. Chem. Biol. 7:834-842(2011).
RN   [12]
RP   FUNCTION.
RX   PubMed=25253888; DOI=10.1104/pp.114.250050;
RA   Fujii S., Kobayashi K., Nakamura Y., Wada H.;
RT   "Inducible knockdown of MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE1 reveals
RT   roles of galactolipids in organelle differentiation in Arabidopsis
RT   cotyledons.";
RL   Plant Physiol. 166:1436-1449(2014).
RN   [13]
RP   PHOSPHATIDYLGLYCEROL-BINDING.
RX   PubMed=32100029; DOI=10.1093/glycob/cwz106;
RA   Nitenberg M., Makshakova O., Rocha J., Perez S., Marechal E., Block M.A.,
RA   Girard-Egrot A., Breton C.;
RT   "Mechanism of activation of plant monogalactosyldiacylglycerol synthase 1
RT   (MGD1) by phosphatidylglycerol.";
RL   Glycobiology 30:396-406(2020).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 137-533 IN COMPLEX WITH UDP,
RP   CATALYTIC ACTIVITY, REGION, AND MUTAGENESIS OF 192-GLN--SER-214; ASP-279;
RP   LYS-430; PRO-433; THR-435; GLN-455 AND GLU-456.
RX   PubMed=26935252; DOI=10.1111/tpj.13129;
RA   Rocha J., Sarkis J., Thomas A., Pitou L., Radzimanowski J., Audry M.,
RA   Chazalet V., de Sanctis D., Palcic M.M., Block M.A., Girard-Egrot A.,
RA   Marechal E., Breton C.;
RT   "Structural insights and membrane binding properties of MGD1, the major
RT   galactolipid synthase in plants.";
RL   Plant J. 85:622-633(2016).
CC   -!- FUNCTION: Involved in the synthesis of the major structural component
CC       of photosynthetic membranes. Required for proper thylakoid membrane
CC       biogenesis. Does not discriminate between prokaryotic (18:1/16:0) or
CC       eukaryotic (18:2/18:2) 1,2-diacylglycerol species, but operates with
CC       some preference for the prokaryotic one. Is responsible for most
CC       galactolipid synthesis in chloroplasts (PubMed:10869420,
CC       PubMed:11171188, PubMed:11553816, PubMed:17940034). Required for the
CC       formation of thylakoid membranes and functional photosynthetic electron
CC       transport during cotyledons greening in young seedlings
CC       (PubMed:25253888). May link galactolipid synthesis with the coordinated
CC       transcriptional regulation of chloroplasts and other organelles during
CC       cotyledon greening (PubMed:25253888). {ECO:0000269|PubMed:10869420,
CC       ECO:0000269|PubMed:11171188, ECO:0000269|PubMed:11553816,
CC       ECO:0000269|PubMed:17940034, ECO:0000269|PubMed:25253888}.
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         Evidence={ECO:0000269|PubMed:20023301, ECO:0000269|PubMed:26935252};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14946;
CC         Evidence={ECO:0000269|PubMed:20023301, ECO:0000269|PubMed:26935252};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycerol + UDP-alpha-D-
CC         galactose = 1,2-di-(9Z,12Z-octadecadienoyl)-3-beta-D-galactosyl-sn-
CC         glycerol + H(+) + UDP; Xref=Rhea:RHEA:48492, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:77127,
CC         ChEBI:CHEBI:90506; Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48493;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + UDP-alpha-D-
CC         galactose = 1-(9Z-octadecenoyl)-2-hexadecanoyl-3-beta-D-galactosyl-
CC         sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:48496, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:75447,
CC         ChEBI:CHEBI:90507; Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48497;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + UDP-alpha-D-galactose =
CC         1,2-di-(9Z-octadecenoyl)-3-beta-D-galactosyl-sn-glycerol + H(+) +
CC         UDP; Xref=Rhea:RHEA:48480, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:63775, ChEBI:CHEBI:66914;
CC         Evidence={ECO:0000269|PubMed:20023301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48481;
CC         Evidence={ECO:0000269|PubMed:20023301};
CC   -!- ACTIVITY REGULATION: Activated by phosphatidate (PA) and
CC       phosphatidylglycerol (PG) (PubMed:20023301). Inhibited by galvestine-1
CC       (PubMed:21946275). {ECO:0000269|PubMed:20023301,
CC       ECO:0000269|PubMed:21946275}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000305|PubMed:11171188, ECO:0000305|PubMed:11553816}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O81770-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O81770-2; Sequence=VSP_035387, VSP_035388;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC       siliques and seeds. {ECO:0000269|PubMed:11171188,
CC       ECO:0000269|PubMed:11553816, ECO:0000269|PubMed:14730084}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed throughout whole developmental
CC       stages. Transient increase in embryos at the globular stage.
CC       {ECO:0000269|PubMed:11553816, ECO:0000269|PubMed:17940034}.
CC   -!- INDUCTION: Induced by illumination and cytokinin treatment in etiolated
CC       seedlings. Not induced by phosphate deprivation.
CC       {ECO:0000269|PubMed:11553816, ECO:0000269|PubMed:14730084}.
CC   -!- DISRUPTION PHENOTYPE: Plants show defects in chloroplast biogenesis and
CC       a dwarf and albino phenotype. The amount of
CC       monogalactosyldiacylglycerol was reduced by 98% in the mutant leaves,
CC       indicating that MGD2 or MGD3 cannot compensate for loss of MGD1
CC       function. {ECO:0000269|PubMed:10869420}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AF241797; AAF65066.1; -; mRNA.
DR   EMBL; AB047399; BAB12042.1; -; mRNA.
DR   EMBL; KJ138730; AHL38670.1; -; mRNA.
DR   EMBL; AL031004; CAA19745.1; -; Genomic_DNA.
DR   EMBL; AL161579; CAB79896.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85956.1; -; Genomic_DNA.
DR   EMBL; AY092965; AAM12964.1; -; mRNA.
DR   EMBL; BT008890; AAP68329.1; -; mRNA.
DR   PIR; T05092; T05092.
DR   RefSeq; NP_194906.1; NM_119327.3. [O81770-1]
DR   PDB; 4WYI; X-ray; 2.50 A; A=137-533.
DR   PDB; 4X1T; X-ray; 2.25 A; A=137-533.
DR   PDBsum; 4WYI; -.
DR   PDBsum; 4X1T; -.
DR   AlphaFoldDB; O81770; -.
DR   SMR; O81770; -.
DR   STRING; 3702.O81770; -.
DR   SwissLipids; SLP:000001440; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   PaxDb; 3702-AT4G31780-2; -.
DR   ProteomicsDB; 238894; -. [O81770-1]
DR   EnsemblPlants; AT4G31780.2; AT4G31780.2; AT4G31780. [O81770-1]
DR   GeneID; 829306; -.
DR   Gramene; AT4G31780.2; AT4G31780.2; AT4G31780. [O81770-1]
DR   KEGG; ath:AT4G31780; -.
DR   Araport; AT4G31780; -.
DR   TAIR; AT4G31780; MGD1.
DR   eggNOG; ENOG502QPXV; Eukaryota.
DR   HOGENOM; CLU_028367_3_1_1; -.
DR   InParanoid; O81770; -.
DR   PhylomeDB; O81770; -.
DR   BioCyc; MetaCyc:AT4G31780-MONOMER; -.
DR   BRENDA; 2.4.1.336; 399.
DR   BRENDA; 2.4.1.46; 399.
DR   PRO; PR:O81770; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O81770; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0046509; F:1,2-diacylglycerol 3-beta-galactosyltransferase activity; IMP:TAIR.
DR   GO; GO:0035250; F:UDP-galactosyltransferase activity; TAS:TAIR.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IDA:TAIR.
DR   GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
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.
DR   Genevisible; O81770; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chloroplast; Glycosyltransferase;
KW   Membrane; Plastid; Plastid inner membrane; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..533
FT                   /note="Monogalactosyldiacylglycerol synthase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000349421"
FT   REGION          192..215
FT                   /note="Required for binding to diacyl glycerol"
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   BINDING         155
FT                   /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT                   /ligand_id="ChEBI:CHEBI:64716"
FT                   /evidence="ECO:0000269|PubMed:32100029"
FT   BINDING         155
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   BINDING         189
FT                   /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT                   /ligand_id="ChEBI:CHEBI:64716"
FT                   /evidence="ECO:0000269|PubMed:32100029"
FT   BINDING         324
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   BINDING         413
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   BINDING         414
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   BINDING         434..438
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   BINDING         456
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:26935252,
FT                   ECO:0007744|PDB:4X1T"
FT   VAR_SEQ         456..504
FT                   /note="EAGNVPYVVENGCGKFSKSPKEISKIVADWFGPASKELEIMSQNALRLA ->
FT                   VSRECTVRGGKRMWEILKITERDIEDCSGLVWTGIERVGDNVTECIEAG (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035387"
FT   VAR_SEQ         505..533
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035388"
FT   MUTAGEN         150
FT                   /note="D->E: No effect on enzyme activation by
FT                   phosphatidate (PA) and phosphatidylglycerol (PG)."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         150
FT                   /note="D->N: Slight increase of enzyme activation by
FT                   phosphatidylglycerol (PG)."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         155
FT                   /note="H->A,R: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         186
FT                   /note="T->A: Abolishes enzyme activation by
FT                   phosphatidylglycerol (PG), and reduces enzyme activation by
FT                   phosphatidate (PA)1.5-fold."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         189
FT                   /note="P->A: Reduces enzyme activation by
FT                   phosphatidylglycerol (PG) 2-fold."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         192..215
FT                   /note="Missing: Almost abolishes catalytic activity and
FT                   binding to diacyl glycerol."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         251
FT                   /note="H->A: Reduces enzyme activation by phosphatidate
FT                   (PA) and phosphatidylglycerol (PG) 4-fold."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         260
FT                   /note="R->A: Slight increase of enzyme activation by
FT                   phosphatidylglycerol (PG)."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   MUTAGEN         279
FT                   /note="D->E: Reduces catalytic activity 25-fold."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         279
FT                   /note="D->N: Reduces catalytic activity 50-fold."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         287
FT                   /note="W->A: Abolishes enzyme activation by
FT                   phosphatidylglycerol (PG), and reduces enzyme activation by
FT                   phosphatidate (PA)3-fold."
FT   MUTAGEN         430
FT                   /note="K->R: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         433
FT                   /note="P->A: Reduces catalytic activity 20-fold."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         435
FT                   /note="T->A: Reduces catalytic activity 1.5-fold."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         455
FT                   /note="Q->N: Reduces catalytic activity 7-fold."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         456
FT                   /note="E->N: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:26935252"
FT   MUTAGEN         456
FT                   /note="E->N: Reduces enzyme activation by phosphatidate
FT                   (PA) and phosphatidylglycerol (PG) 15-fold."
FT                   /evidence="ECO:0000269|PubMed:20023301"
FT   STRAND          143..147
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            150..153
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           156..170
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           232..242
FT                   /evidence="ECO:0007829|PDB:4WYI"
FT   STRAND          245..249
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            252..255
FT                   /evidence="ECO:0007829|PDB:4WYI"
FT   HELIX           256..263
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:4WYI"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          271..276
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:4WYI"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           300..309
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           313..315
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:4WYI"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           334..341
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            355..358
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           362..372
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            376..379
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          380..382
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          384..388
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           393..401
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          408..412
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           417..422
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          425..429
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           433..441
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          446..448
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            453..458
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           459..464
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            465..467
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   STRAND          468..471
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           475..485
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            486..489
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           490..503
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   HELIX           508..520
FT                   /evidence="ECO:0007829|PDB:4X1T"
FT   TURN            521..523
FT                   /evidence="ECO:0007829|PDB:4X1T"
SQ   SEQUENCE   533 AA;  58538 MW;  E581E67317CB9CC8 CRC64;
     MQNPSTVTQE SAAPVFDFFP RLRGLTSRNR SPCSNSDGYA LSSSNALYFN GFRTLPSRRM
     GKTLASLSFN TKSSAGSSLR RFISDFNSFI RFHCDKVVPE SFASVGGVGL SSDENGIREN
     GTGGVLGEEG LPLNGVEADR PKKVLILMSD TGGGHRASAE AIRAAFNQEF GDEYQVFITD
     LWTDHTPWPF NQLPRSYNFL VKHGTLWKMT YYGTSPRIVH QSNFAATSTF IAREIAQGLM
     KYQPDIIISV HPLMQHVPLR VLRSKGLLKK IVFTTVITDL STCHPTWFHK LVTRCYCPST
     EVAKRAQKAG LETSQIKVYG LPVRPSFVKP VRPKVELRRE LGMDENLPAV LLMGGGEGMG
     PIEATARALA DALYDKNLGE AVGQVLIICG RNKKLQSKLS SLDWKIPVQV KGFITKMEEC
     MGACDCIITK AGPGTIAEAM IRGLPIILNG YIAGQEAGNV PYVVENGCGK FSKSPKEISK
     IVADWFGPAS KELEIMSQNA LRLAKPEAVF KIVHDMHELV RKKNSLPQLS CTA
//