MGDG3_ARATH
ID MGDG3_ARATH Reviewed; 465 AA.
AC Q9SI93; B3H4P3; Q9FZL5; W8PV29;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Monogalactosyldiacylglycerol synthase 3, chloroplastic {ECO:0000305};
DE Short=AtMGD3 {ECO:0000303|PubMed:11553816};
DE EC=2.4.1.46 {ECO:0000269|PubMed:11553816};
DE AltName: Full=MGDG synthase type C {ECO:0000305};
DE Flags: Precursor;
GN Name=MGD3 {ECO:0000303|PubMed:11553816}; Synonyms=MGDC {ECO:0000305};
GN OrderedLocusNames=At2g11810 {ECO:0000312|Araport:AT2G11810};
GN ORFNames=F7E22.4 {ECO:0000312|EMBL:AAD28678.2};
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, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 [7]
RP INDUCTION.
RX PubMed=16762032; DOI=10.1111/j.1365-313x.2006.02778.x;
RA Kobayashi K., Masuda T., Takamiya K., Ohta H.;
RT "Membrane lipid alteration during phosphate starvation is regulated by
RT phosphate signaling and auxin/cytokinin cross-talk.";
RL Plant J. 47:238-248(2006).
RN [8]
RP FUNCTION.
RX PubMed=18808455; DOI=10.1111/j.1365-313x.2008.03692.x;
RA Kobayashi K., Awai K., Nakamura M., Nagatani A., Masuda T., Ohta H.;
RT "Type-B monogalactosyldiacylglycerol synthases are involved in phosphate
RT starvation-induced lipid remodeling, and are crucial for low-phosphate
RT adaptation.";
RL Plant J. 57:322-331(2009).
RN [9]
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 [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=31201686; DOI=10.1007/s11103-019-00891-1;
RA Murakawa M., Ohta H., Shimojima M.;
RT "Lipid remodeling under acidic conditions and its interplay with low Pi
RT stress in Arabidopsis.";
RL Plant Mol. Biol. 101:81-93(2019).
CC -!- FUNCTION: Involved in the synthesis of monogalactosyldiacylglycerol,
CC the major structural component of photosynthetic membranes and in the
CC chloroplast envelope biogenesis. Can use both prokaryotic (18:1/16:0)
CC or eukaryotic (18:2/18:2) 1,2-diacylglycerol species, but operates with
CC some preference for the eukaryotic one. Plays a minor role in
CC galactolipid synthesis in chloroplasts (PubMed:11553816). Is essential
CC for membrane lipid remodeling in phosphate-starved roots
CC (PubMed:18808455, PubMed:31201686). Acts as the major factor involved
CC in digalactosyldiacylglycerol (DGDG) biosynthesis in phosphate-starved
CC roots (PubMed:18808455). Does not seem to be required for plant growth
CC under nutrient-sufficient conditions (PubMed:18808455). Required for
CC membrane lipid remodeling in plants grown in acidic conditions
CC (PubMed:31201686). {ECO:0000269|PubMed:11553816,
CC ECO:0000269|PubMed:18808455, ECO:0000269|PubMed:31201686}.
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:11553816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14946;
CC Evidence={ECO:0000269|PubMed:11553816};
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:11553816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48481;
CC Evidence={ECO:0000269|PubMed:11553816};
CC -!- ACTIVITY REGULATION: Inhibited by galvestine-1.
CC {ECO:0000269|PubMed:21946275}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000305|PubMed:11553816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SI93-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SI93-2; Sequence=VSP_035389, VSP_035390;
CC -!- TISSUE SPECIFICITY: Expressed mainly in roots. Detected in flowers,
CC leaves, stems, siliques and pollen tubes. {ECO:0000269|PubMed:11553816,
CC ECO:0000269|PubMed:14730084}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in early stages of development.
CC {ECO:0000269|PubMed:11553816}.
CC -!- INDUCTION: Induced by phosphate deprivation (PubMed:11553816,
CC PubMed:14730084, PubMed:16762032). Induced in rosette leaves when grown
CC in acidic soil (PubMed:31201686). {ECO:0000269|PubMed:11553816,
CC ECO:0000269|PubMed:14730084, ECO:0000269|PubMed:16762032,
CC ECO:0000269|PubMed:31201686}.
CC -!- MISCELLANEOUS: Auxin activates expression during Pi starvation, whereas
CC cytokinin represses it.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; AB047398; BAB12041.1; -; mRNA.
DR EMBL; KJ138917; AHL38857.1; -; mRNA.
DR EMBL; AC007187; AAD28678.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06183.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06184.1; -; Genomic_DNA.
DR EMBL; BT026357; ABH04464.1; -; mRNA.
DR PIR; C84499; C84499.
DR RefSeq; NP_001118301.1; NM_001124829.2. [Q9SI93-2]
DR RefSeq; NP_565352.1; NM_126865.5. [Q9SI93-1]
DR AlphaFoldDB; Q9SI93; -.
DR SMR; Q9SI93; -.
DR BioGRID; 1028; 8.
DR IntAct; Q9SI93; 2.
DR STRING; 3702.AT2G11810.1; -.
DR SwissLipids; SLP:000001446; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR PaxDb; Q9SI93; -.
DR PRIDE; Q9SI93; -.
DR EnsemblPlants; AT2G11810.1; AT2G11810.1; AT2G11810. [Q9SI93-1]
DR EnsemblPlants; AT2G11810.2; AT2G11810.2; AT2G11810. [Q9SI93-2]
DR GeneID; 815657; -.
DR Gramene; AT2G11810.1; AT2G11810.1; AT2G11810. [Q9SI93-1]
DR Gramene; AT2G11810.2; AT2G11810.2; AT2G11810. [Q9SI93-2]
DR KEGG; ath:AT2G11810; -.
DR Araport; AT2G11810; -.
DR TAIR; locus:2052662; AT2G11810.
DR eggNOG; ENOG502QPXV; Eukaryota.
DR HOGENOM; CLU_028367_3_1_1; -.
DR InParanoid; Q9SI93; -.
DR OMA; WVHANAD; -.
DR OrthoDB; 628561at2759; -.
DR PhylomeDB; Q9SI93; -.
DR BioCyc; MetaCyc:AT2G11810-MON; -.
DR BRENDA; 2.4.1.46; 399.
DR PRO; PR:Q9SI93; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI93; baseline and differential.
DR Genevisible; Q9SI93; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046509; F:1,2-diacylglycerol 3-beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IGI:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
DR GO; GO:0019374; P:galactolipid metabolic process; IMP:TAIR.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro.
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 Alternative splicing; Chloroplast; Glycosyltransferase; Membrane; Plastid;
KW Plastid outer membrane; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..465
FT /note="Monogalactosyldiacylglycerol synthase 3,
FT chloroplastic"
FT /id="PRO_0000349423"
FT BINDING 86
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O81770"
FT BINDING 255
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O81770"
FT BINDING 365..369
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O81770"
FT BINDING 387
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O81770"
FT VAR_SEQ 362
FT /note="A -> H (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035389"
FT VAR_SEQ 363..465
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035390"
SQ SEQUENCE 465 AA; 52990 MW; 05E0157012E50A14 CRC64;
MMKVVSPRTR SDSITEKVFR RVYSNFNIST VEDEYIHRQR SSDYEKESRL RKRGLEDKEE
VMEMEQMGAE RIKTVLILMS DTGGGHRASA EAIRDAFKIE FGDDYRIIIK DVWKEYTGWP
LNDMERQYKF MVKHVGLWSV AFHGTSPKWI HKSYLSALAA YYAKEIEAGL MEYKPDIIIS
VHPLMQHIPL WVMKWQGLHK KVIFVTVITD LNTCHRTWFH HGVSRCYCPS KEVAKRALVD
GLDDSQIRVF GLPVRPSFPR TILNKNELRK ELEIDLNLPA VLLMGGGEGM GPVQKTALAL
GDSLYNSKES NPIGQLIVIC GRNKVLASTL ASHEWKIPVK VRGFETQMEK WMGACDCIIT
KAGPGTIAEA LICGLPIILN DYIPGQEKGN VPYVVDNGAG VFTRSPKETA KIVADWFSNN
KEELKKMSEN ALKLSQPEAV FDIVKDIHHL SQQQQRIPLF NEFSY
