MGDG1_ARATH
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 03-AUG-2022, entry version 138.
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.AT4G31780.2; -.
DR SwissLipids; SLP:000001440; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR iPTMnet; O81770; -.
DR PaxDb; O81770; -.
DR PRIDE; O81770; -.
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; locus:2124844; AT4G31780.
DR eggNOG; ENOG502QPXV; Eukaryota.
DR HOGENOM; CLU_028367_3_1_1; -.
DR InParanoid; O81770; -.
DR PhylomeDB; O81770; -.
DR BioCyc; MetaCyc:AT4G31780-MON; -.
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 Genevisible; O81770; AT.
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 InterPro; IPR009695; Diacylglyc_glucosyltr_N.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF06925; MGDG_synth; 1.
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
