ID   DGDG1_SOYBN             Reviewed;         783 AA.
AC   Q6DW76;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Digalactosyldiacylglycerol synthase 1, chloroplastic;
DE            EC=2.4.1.241;
DE   Flags: Precursor;
GN   Name=DGD1;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=cv. Stevens;
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: Expressed in leaves, roots and nodules.
CC       {ECO:0000269|PubMed:15159398}.
CC   -!- DEVELOPMENTAL STAGE: Very low expression in young nodules, increasing
CC       in the later stages of development. {ECO:0000269|PubMed:15159398}.
CC   -!- INDUCTION: Up-regulated in leaves by phosphate deficiency.
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; AY635907; AAT67420.1; -; mRNA.
DR   AlphaFoldDB; Q6DW76; -.
DR   STRING; 3847.GLYMA03G36050.1; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; Q6DW76; -.
DR   eggNOG; ENOG502QQ73; Eukaryota.
DR   InParanoid; Q6DW76; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR   GO; GO:0043661; C:peribacteroid membrane; IEA:UniProtKB-SubCell.
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:0019375; P:galactolipid biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..783
FT                   /note="Digalactosyldiacylglycerol synthase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000252339"
SQ   SEQUENCE   783 AA;  89341 MW;  AB35EF4853CF3D37 CRC64;
     MATHPQTPTS SNAFSFISKG WREVRDSADA DLRLMRDRAN SFKDLATSFD RELENFFNSA
     TPPFSVPAMR SPPPKEIEFV KSLRPKLSEI RRAYSSPDFS KKVLEKWRPR TQIRINLSAI
     KNAIVSAEEE EEGIVDFEKR RRRRLSFWEE WKGEGEGESR DWEPIRVLKT RLKEFEKRGS
     SFDAFKNSEF VEKVKSSLKS MCKEPLESKE VPPLDVPELL AYIVKQSGPF LDHLGVKRDI
     CDKIVESLYS KCKNHQLLHS LSGEESSVLG NGNINDELDL RIASVLQSTG HRYEGGFWTD
     HAKHDPLDNE RHVAIVTTAS LPWMTGTAVN PLFRAAYLSQ SAKQKVTLLV PWLCKSDQEL
     VYPSNLTFTS PEEQEAYIRS WLEERIGFKA DFKISFYPGK FSEARRSIIP AGDTSQFIPS
     RDADIAILEE PEHLNWYHHG KRWTDKFNHV VGIVHTNYLE YIKREKNGAL QAFLVKHINN
     WVTRAYCHKV LRLSAATQDL PKSVICNVHG VNPKFLKIGE KIAAERELGQ KAFTKGAYFL
     GKMVWAKGYK ELIDLLAKHK ADLDGFKLDV FGNGEDANEV QSAARRLDLN LNFQKGRDHA
     DDSLHRYKVF INPSISDVLC TATAEALAMG KFVVCADHPS NEFFRSFPNC LTYRTSEDFV
     TKVKEALENE PYPLTPEQRY QLSWEAATQR FMEYSELDGI LNKENNGEKS RVDKGKLIAK
     SASMPNLTEL VDGGLAFAHY CLTGNEFLRL CTGAIPGTRD YDKQHCKDLH LLPPQVENPI
     YGW