GOLS1_ARATH
ID GOLS1_ARATH Reviewed; 344 AA.
AC O22893;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Galactinol synthase 1;
DE Short=AtGolS1;
DE Short=GolS-1;
DE EC=2.4.1.123;
GN Name=GOLS1; OrderedLocusNames=At2g47180; ORFNames=T3D7, T8I13;
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], INDUCTION BY DROUGHT; ABA AND HIGH-SALINITY
RP STRESSES, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=11846875; DOI=10.1046/j.0960-7412.2001.01227.x;
RA Taji T., Ohsumi C., Iuchi S., Seki M., Kasuga M., Kobayashi M.,
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Important roles of drought- and cold-inducible genes for galactinol
RT synthase in stress tolerance in Arabidopsis thaliana.";
RL Plant J. 29:417-426(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY HEAT, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24, cv. Columbia, and cv. Wassilewskija;
RX PubMed=15466240; DOI=10.1104/pp.104.042606;
RA Panikulangara T.J., Eggers-Schumacher G., Wunderlich M., Stransky H.,
RA Schoeffl F.;
RT "Galactinol synthase1. A novel heat shock factor target gene responsible
RT for heat-induced synthesis of raffinose family oligosaccharides in
RT Arabidopsis.";
RL Plant Physiol. 136:3148-3158(2004).
RN [7]
RP FUNCTION, INDUCTION BY METHYLVIOLOGEN, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18502973; DOI=10.1104/pp.108.122465;
RA Nishizawa A., Yabuta Y., Shigeoka S.;
RT "Galactinol and raffinose constitute a novel function to protect plants
RT from oxidative damage.";
RL Plant Physiol. 147:1251-1263(2008).
CC -!- FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose
CC family oligosaccharides (RFOs) that function as osmoprotectants.
CC Promotes plant stress tolerance such as heat, chilling, salinity and
CC methylviologen (MV), a superoxide radical generating drug, by mediating
CC raffinose accumulation, an osmoprotective substance.
CC {ECO:0000269|PubMed:15466240, ECO:0000269|PubMed:18502973}.
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:11846875};
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: Accumulates in mature seeds. Expressed in seedlings
CC (axes and cotyledons), meristems, vascular tissues and emerging lateral
CC roots. Present in abscission zones. {ECO:0000269|PubMed:11846875,
CC ECO:0000269|PubMed:15466240}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), heat, drought and high-
CC salinity stresses. Promoted by methylviologen (MV), a superoxide
CC radical generating drug. {ECO:0000269|PubMed:11846875,
CC ECO:0000269|PubMed:15466240, ECO:0000269|PubMed:18502973}.
CC -!- DISRUPTION PHENOTYPE: Impaired raffinose accumulation in response to
CC heat stress. {ECO:0000269|PubMed:15466240}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC Galactosyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AB062848; BAB78530.1; -; mRNA.
DR EMBL; AC002337; AAB63818.1; -; Genomic_DNA.
DR EMBL; AC007236; AAM15468.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10811.1; -; Genomic_DNA.
DR EMBL; AY056139; AAL07218.1; -; mRNA.
DR EMBL; AY091426; AAM14365.1; -; mRNA.
DR EMBL; AY085006; AAM61564.1; -; mRNA.
DR PIR; A84912; A84912.
DR RefSeq; NP_182240.1; NM_130286.3.
DR AlphaFoldDB; O22893; -.
DR SMR; O22893; -.
DR STRING; 3702.AT2G47180.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; O22893; -.
DR PRIDE; O22893; -.
DR ProteomicsDB; 248441; -.
DR EnsemblPlants; AT2G47180.1; AT2G47180.1; AT2G47180.
DR GeneID; 819331; -.
DR Gramene; AT2G47180.1; AT2G47180.1; AT2G47180.
DR KEGG; ath:AT2G47180; -.
DR Araport; AT2G47180; -.
DR TAIR; locus:2062860; AT2G47180.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_049943_3_0_1; -.
DR InParanoid; O22893; -.
DR OMA; HVCVCNL; -.
DR OrthoDB; 818680at2759; -.
DR PhylomeDB; O22893; -.
DR BRENDA; 2.4.1.123; 399.
DR PRO; PR:O22893; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22893; baseline and differential.
DR Genevisible; O22893; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
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:0006012; P:galactose metabolic process; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP: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:SF148; PTHR11183:SF148; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..344
FT /note="Galactinol synthase 1"
FT /id="PRO_0000418657"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 39596 MW; 46784EA16DBD3A46 CRC64;
MAPGLTQTAD AMSTVTITKP SLPSVQDSDR AYVTFLAGNG DYVKGVVGLA KGLRKVKSAY
PLVVAMLPDV PEEHRRILVD QGCIVREIEP VYPPENQTQF AMAYYVINYS KLRIWKFVEY
SKMIYLDGDI QVYENIDHLF DLPDGYLYAV MDCFCEKTWS HTPQYKIRYC QQCPDKVQWP
KAELGEPPAL YFNAGMFLYE PNLETYEDLL RTLKITPPTP FAEQDFLNMY FKKIYKPIPL
VYNLVLAMLW RHPENVELGK VKVVHYCAAG SKPWRYTGKE ANMEREDIKM LVKKWWDIYD
DESLDYKKPV TVVDTEVDLV NLKPFITALT EAGRLNYVTA PSAA
