DGDG2_SOYBN
ID DGDG2_SOYBN Reviewed; 463 AA.
AC Q6DW75;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Digalactosyldiacylglycerol synthase 2, chloroplastic;
DE EC=2.4.1.241;
GN Name=DGD2;
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; AY635908; AAT67421.1; -; mRNA.
DR RefSeq; NP_001237488.1; NM_001250559.1.
DR RefSeq; XP_006601859.1; XM_006601796.2.
DR RefSeq; XP_014625733.1; XM_014770247.1.
DR AlphaFoldDB; Q6DW75; -.
DR STRING; 3847.GLYMA18G46300.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PRIDE; Q6DW75; -.
DR EnsemblPlants; KRH00685; KRH00685; GLYMA_18G228900.
DR GeneID; 547762; -.
DR Gramene; KRH00685; KRH00685; GLYMA_18G228900.
DR KEGG; gmx:547762; -.
DR eggNOG; ENOG502QQEJ; Eukaryota.
DR HOGENOM; CLU_011647_1_0_1; -.
DR InParanoid; Q6DW75; -.
DR OMA; APLTDMQ; -.
DR OrthoDB; 972633at2759; -.
DR Proteomes; UP000008827; Chromosome 18.
DR Genevisible; Q6DW75; GM.
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.
FT CHAIN 1..463
FT /note="Digalactosyldiacylglycerol synthase 2,
FT chloroplastic"
FT /id="PRO_0000252342"
SQ SEQUENCE 463 AA; 52563 MW; 07BE0B5CF47D2624 CRC64;
MDKKEHIAIF TTASLPWLTG TAVNPLFRAA YLAKSGERDV TLVIPWLSLK DQRLVYPNNI
TFASPSEHEK YICQWLEERV GFTSGFSIQF YPGKFSRDKR SILAVGDISE IIPDKVADIA
VLEEPEHLTW YHHGKRWKTK FRLVIGIIHT NYLEYVKREK NGVMQAFLLK YLNNWVVSIY
CHKVIRLSAA TQDYTGSIIC NVHGVNPKFL EIGKKKREQQ QKGEHAFTKG AYFIGKMIWS
KGYKELLQLL KDHEKELSAL EVDLFGSGED SDEVQKAAEK LELAVRVHPA RDHADALFHD
YKLFLNPSTT DVVCTTTAEA LAMGKIVVCA NHPSNDFFKQ FPNCWTYDDD DGFVKLTLKA
LAEQPAQPTD AQRHDLSWEA ATKRFLKAAD LDKPLERKLS RTTSNFLAAS LNLQEKVDEA
SAYVHHVASG FEVSRRIFGA IPDSLQPDEE LRKELGLTDA STK