DGDG2_ARATH
ID DGDG2_ARATH Reviewed; 473 AA.
AC Q8W1S1; O65264; Q56ZV5; Q8W1S0; W8PV82;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Digalactosyldiacylglycerol synthase 2, chloroplastic;
DE EC=2.4.1.241 {ECO:0000269|PubMed:21156807};
GN Name=DGD2; OrderedLocusNames=At4g00550; ORFNames=F6N23.24;
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] (ISOFORMS 1 AND 2), FUNCTION, AND INDUCTION.
RX PubMed=11696551; DOI=10.1074/jbc.m110066200;
RA Kelly A.A., Doermann P.;
RT "DGD2, an arabidopsis gene encoding a UDP-galactose-dependent
RT digalactosyldiacylglycerol synthase is expressed during growth under
RT phosphate-limiting conditions.";
RL J. Biol. Chem. 277:1166-1173(2002).
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=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 [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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14600212; DOI=10.1105/tpc016675;
RA Kelly A.A., Froehlich J.E., Doermann P.;
RT "Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and
RT DGD2 in Arabidopsis reveals the existence of an additional enzyme of
RT galactolipid synthesis.";
RL Plant Cell 15:2694-2706(2003).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF TRP-19; VAL-25;
RP TRP-48; TRP-139; TRP-177; TRP-241; LYS-243; LEU-299; ASP-313 AND CYS-316.
RX PubMed=21156807; DOI=10.1074/jbc.m110.138495;
RA Ge C., Georgiev A., Oehman A., Wieslander A., Kelly A.A.;
RT "Tryptophan residues promote membrane association for a plant lipid
RT glycosyltransferase involved in phosphate stress.";
RL J. Biol. Chem. 286:6669-6684(2011).
RN [9]
RP STRUCTURE BY NMR OF 227-245, FUNCTION, AND INTERACTION WITH LIPIDS.
RX PubMed=21506606; DOI=10.1021/bi200162f;
RA Szpryngiel S., Ge C., Iakovleva I., Georgiev A., Lind J., Wieslander A.,
RA Maler L.;
RT "Lipid interacting regions in phosphate stress glycosyltransferase atDGD2
RT from Arabidopsis thaliana.";
RL Biochemistry 50:4451-4466(2011).
CC -!- FUNCTION: Involved in the synthesis of diacylglycerol galactolipids
CC that are specifically found in thylakoid membranes. Specific for alpha-
CC glycosidic linkages (PubMed:11696551, PubMed:14600212). During
CC phosphate shortage, involved in the biosynthesis of
CC digalactosyldiacylglycerol (DGDG) which rescues the limitation of
CC phospholipids (Probable). {ECO:0000269|PubMed:11696551,
CC ECO:0000269|PubMed:14600212, ECO:0000305|PubMed:21506606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-
CC D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:10520,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:28396,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.241;
CC Evidence={ECO:0000269|PubMed:21156807};
CC -!- ACTIVITY REGULATION: Stimulated by anionic phospholipids.
CC {ECO:0000269|PubMed:21156807}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:14600212}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W1S1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W1S1-2; Sequence=VSP_020911;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and roots, but not in
CC stems and siliques. {ECO:0000269|PubMed:14600212}.
CC -!- INDUCTION: 30-fold up-regulation by phosphate deficiency.
CC {ECO:0000269|PubMed:11696551, ECO:0000269|PubMed:14600212}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:14600212}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94208.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB80864.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF421193; AAL60504.1; -; mRNA.
DR EMBL; AF421194; AAL60505.1; -; mRNA.
DR EMBL; KJ138776; AHL38716.1; -; mRNA.
DR EMBL; AF058919; AAC13625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80864.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81898.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67739.1; -; Genomic_DNA.
DR EMBL; AK228220; BAF00170.1; -; mRNA.
DR EMBL; AK220856; BAD94208.1; ALT_INIT; mRNA.
DR EMBL; BT010144; AAQ22613.1; -; mRNA.
DR PIR; T01219; T01219.
DR RefSeq; NP_001329549.1; NM_001340258.1. [Q8W1S1-1]
DR RefSeq; NP_191964.2; NM_116279.5. [Q8W1S1-1]
DR PDB; 2L7C; NMR; -; A=227-245.
DR PDBsum; 2L7C; -.
DR AlphaFoldDB; Q8W1S1; -.
DR SMR; Q8W1S1; -.
DR BioGRID; 13251; 2.
DR IntAct; Q8W1S1; 2.
DR STRING; 3702.AT4G00550.1; -.
DR SwissLipids; SLP:000001449; -. [Q8W1S1-1]
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q8W1S1; -.
DR PaxDb; Q8W1S1; -.
DR PRIDE; Q8W1S1; -.
DR ProteomicsDB; 224055; -. [Q8W1S1-1]
DR EnsemblPlants; AT4G00550.1; AT4G00550.1; AT4G00550. [Q8W1S1-1]
DR EnsemblPlants; AT4G00550.2; AT4G00550.2; AT4G00550. [Q8W1S1-1]
DR GeneID; 827960; -.
DR Gramene; AT4G00550.1; AT4G00550.1; AT4G00550. [Q8W1S1-1]
DR Gramene; AT4G00550.2; AT4G00550.2; AT4G00550. [Q8W1S1-1]
DR KEGG; ath:AT4G00550; -.
DR Araport; AT4G00550; -.
DR TAIR; locus:2126998; AT4G00550.
DR eggNOG; ENOG502QQ73; Eukaryota.
DR HOGENOM; CLU_011647_1_0_1; -.
DR InParanoid; Q8W1S1; -.
DR OMA; APLTDMQ; -.
DR PhylomeDB; Q8W1S1; -.
DR BioCyc; MetaCyc:AT4G00550-MON; -.
DR BRENDA; 2.4.1.241; 399.
DR PRO; PR:Q8W1S1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W1S1; baseline and differential.
DR Genevisible; Q8W1S1; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0046481; F:digalactosyldiacylglycerol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:TAIR.
DR InterPro; IPR044525; DGDG1/2.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR46132; PTHR46132; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Glycosyltransferase;
KW Membrane; Plastid; Plastid outer membrane; Reference proteome; Transferase.
FT CHAIN 1..473
FT /note="Digalactosyldiacylglycerol synthase 2,
FT chloroplastic"
FT /id="PRO_0000252340"
FT REGION 130..148
FT /note="Interaction with the membrane lipid bilayer"
FT /evidence="ECO:0000269|PubMed:21506606"
FT REGION 227..245
FT /note="Interaction with the membrane lipid bilayer"
FT /evidence="ECO:0000269|PubMed:21506606"
FT VAR_SEQ 1..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11696551"
FT /id="VSP_020911"
FT MUTAGEN 19
FT /note="W->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 19
FT /note="W->F: Reduces catalytic activity 100-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 25
FT /note="V->A: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 48
FT /note="W->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 48
FT /note="W->F: Reduces catalytic activity 100-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 139
FT /note="W->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 139
FT /note="W->F: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 177
FT /note="W->A: Reduces catalytic activity 50-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 177
FT /note="W->F: Reduces catalytic activity 5-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 241
FT /note="W->A: Reduces catalytic activity 100-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 241
FT /note="W->F: Reduces catalytic activity 50-fold."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 243
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 299
FT /note="L->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 313
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT MUTAGEN 316
FT /note="C->A: Slight decrease of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21156807"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:2L7C"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2L7C"
SQ SEQUENCE 473 AA; 53907 MW; 1B04CA5C01F525B1 CRC64;
MTNQQEQHIA IFTTASIPWL TGTAVNPLFR AAYLANDGER RVTLVIPWLT LKHQKLVYPN
SITFSSPSEQ EAYVRQWLEE RVSFRLAFEI RFYPGKFAID KRSILPVGDI SDAIPDEEAD
IAVLEEPEHL TWFHHGQKWK TKFNYVIGIV HTNYLEYVKR EKQGRVKAFF LKYLNSWVVG
IYCHKVIRLS AATQEYPKSI VCNVHGVNPK FLEIGLRKLE QQKLQEQPFT KGAYYIGKMV
WSKGYKELLK LLEKHQKELA ELEVDLYGDG EDSEEIKEAA RKLDLTVNVY PGRDHADSLF
HNYKVFLNPS TTDVVCTTTA EALAMGKIVV CANHISNKFF KQFPNCRTYD DGQGFVRATL
KALGEQPSQL TEQQRHELSW EAATQRFIKV SDLNRLSRAD SNLSKRSVFA SSSISVGKNL
EDMSAYIHFL ASGFEASRTA FGAIPGSLQP DEELCRDLGL SLNTPSPNTR KQD
