ID   DGDG1_LOTJA             Reviewed;         786 AA.
AC   Q6DW74;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Digalactosyldiacylglycerol synthase 1, chloroplastic;
DE            EC=2.4.1.241;
DE   Flags: Precursor;
GN   Name=DGD1;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15159398; DOI=10.1074/jbc.m404098200;
RA   Gaude N., Tippmann H., Flemetakis E., Katinakis P., Udvardi M.,
RA   Doermann P.;
RT   "The galactolipid digalactosyldiacylglycerol accumulates in the
RT   peribacteroid membrane of nitrogen-fixing nodules of Soybean and Lotus.";
RL   J. Biol. Chem. 279:34624-34630(2004).
CC   -!- FUNCTION: Involved in the synthesis of diacylglycerol galactolipids
CC       that are specifically found in thylakoid membranes. Specific for alpha-
CC       glycosidic linkages. {ECO:0000269|PubMed:15159398}.
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   -!- SUBCELLULAR LOCATION: Symbiosome, peribacteroid membrane {ECO:0000305}.
CC       Plastid, chloroplast outer membrane {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: High expression in nodules infected cells, but low
CC       in nodule inner cortex and root central cylinder.
CC       {ECO:0000269|PubMed:15159398}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AY635909; AAT67422.1; -; mRNA.
DR   AlphaFoldDB; Q6DW74; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043661; C:peribacteroid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046481; F:digalactosyldiacylglycerol synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR   InterPro; IPR044525; DGDG1/2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR46132; PTHR46132; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Glycosyltransferase; Membrane; Nodulation; Plastid;
KW   Plastid outer membrane; Transferase; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..786
FT                   /note="Digalactosyldiacylglycerol synthase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000252338"
SQ   SEQUENCE   786 AA;  89191 MW;  56C024A925D1983F CRC64;
     MASQRQPPSS SNAFSFLSKG WREVRDSADA DLQLMKDRAN SFKNLATSFD RELENFFNSA
     APAFSVPAMR SASPPPAEIE FVKKLQPKLS EFRRAYSSPD FSKKVLEKWR PRARIRIDLS
     AIKNAIVSEE IDEGIVDFER GKRERRLSFW EELKGEGEAQ DWEPIRALKT RLKEFEKRSS
     SVEFFDGFKN SEFLEKVKSS LKSMCKEPRD SKEVPPLDVA ELLAYFVKQS GPFLDQLGVR
     RDVCDKIVES LYSKRKNQLL LPSLSGEESS LLGNGNINDE LDLRIASVLQ STGHRNEGGF
     WTDHAKHDLS DNERHVAIVT TASLPWMTGT AVNPLFRAAY LSQSEKQKVT LLVPWLCKSD
     QELVYPSNLT FTSPEEQEGY IRNWLEERIG FKADFKISFY PGKFSQARRS IIPAGDTAQF
     IPSKDADIAI LEEPEHLNWY HHGTRWTDKF NHVVGIVHTN YLEYIKREKN GALQAFLVKH
     INNWVARAYC DKVLRLSAAT QDLPKSVVCN VHGVNPKFLK IGESIAAERE LGQKGFTKGA
     YFLGKMVWAK GYKELIDLLA KHKADLDGVK LDVFGNGEDA NEVQSAARRF DLNLNFQKGR
     DHADDSLHRY KVFINPSISD VLCTATAEAL AMGKFVVCAD HPSNEFFRSF PNCLTYKTPE
     DFAVKVKEAL ANEPYPLTPE QRYQLSWEAA TQRFMEYSEL DKVLNKEKDG AKPSKNNRKI
     MAKSASMPNL TELVDGGLAF AHYCLTGNEF LRLCTGATPG TRDYDKQHCK DLNLLPPQVE
     NPIYGW