ID   GOLS1_AJURE             Reviewed;         333 AA.
AC   Q9XGN4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Galactinol synthase 1;
DE            Short=ArGolS1;
DE            Short=GolS-1;
DE            EC=2.4.1.123;
GN   Name=GOLS1;
OS   Ajuga reptans (Bugle).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Ajugoideae; Ajugeae; Ajuga.
OX   NCBI_TaxID=38596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY
RP   COLD, AND CATALYTIC ACTIVITY.
RX   PubMed=10758476; DOI=10.1046/j.1365-313x.2000.00671.x;
RA   Sprenger N., Keller F.;
RT   "Allocation of raffinose family oligosaccharides to transport and storage
RT   pools in Ajuga reptans: the roles of two distinct galactinol synthases.";
RL   Plant J. 21:249-258(2000).
CC   -!- FUNCTION: Major galactinol synthase mainly involved in the biosynthesis
CC       of storage raffinose family oligosaccharides (RFOs) that function as
CC       osmoprotectants. May promote plant stress tolerance.
CC       {ECO:0000269|PubMed:10758476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-
CC         (1->3)-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:12464,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.123;
CC         Evidence={ECO:0000269|PubMed:10758476};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in source leaves, specifically in the
CC       mesophyll. {ECO:0000269|PubMed:10758476}.
CC   -!- INDUCTION: By cold. Follows a circadian rhythm; accumulates mostly at
CC       midday during the light phase. {ECO:0000269|PubMed:10758476}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       Galactosyltransferase subfamily. {ECO:0000305}.
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DR   EMBL; AJ237693; CAB51533.1; -; mRNA.
DR   AlphaFoldDB; Q9XGN4; -.
DR   SMR; Q9XGN4; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   BRENDA; 2.4.1.123; 222.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047216; F:inositol 3-alpha-galactosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052576; P:carbohydrate storage; IDA:UniProtKB.
DR   GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010325; P:raffinose family oligosaccharide biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR030515; GOLS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11183:SF106; PTHR11183:SF106; 1.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Glycosyltransferase; Manganese; Metal-binding; Transferase.
FT   CHAIN           1..333
FT                   /note="Galactinol synthase 1"
FT                   /id="PRO_0000418655"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  37882 MW;  B3D575F9084DFF6B CRC64;
     MGPVVPVEAF RSAGKISALG AKKGYVTFLA GNGDYVKGVV GLAKGLRKVK SAYPLVVAIL
     PDVPEEHREL LRSQGCIVKE IEPIYPPANQ IQFAMAYYVI NYSKLRIWNF EEYSKMVYLD
     ADIQVYENID HLLDTPDGYF YAVMDCFCEK TWSHSRQFSI GYCQQCPNKV TWPAQMGSPP
     PLYFNAGMFV FEPSKTTYQT LLHTLRITPP TPFAEQDFLN MFFEPIYKPI PLVYNLVLAM
     LWRHPENVEL EKVQVVHYCA AGSKPWRYTG QEANMDREDI KMLVKKWWDV YNDESLDFKA
     EDSIAGEETF SMPSFIASLP EPAVSYIPAP SAA