SGT1_SOLTU
ID SGT1_SOLTU Reviewed; 488 AA.
AC P93789;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Solanidine UDP-glucose glucosyltransferase 1 {ECO:0000303|PubMed:9076990};
DE EC=2.4.1.- {ECO:0000269|PubMed:9076990};
GN Name=SGT1 {ECO:0000303|PubMed:9076990};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=9076990; DOI=10.1046/j.1365-313x.1997.11020227.x;
RA Moehs C.P., Allen P.V., Friedman M., Belknap W.R.;
RT "Cloning and expression of solanidine UDP-glucose glucosyltransferase from
RT potato.";
RL Plant J. 11:227-236(1997).
RN [2]
RP FUNCTION.
RX AGRICOLA=IND43662550; DOI=10.1016/j.plantsci.2004.08.006;
RA McCue K.F., Shepherd L.V.T., Allen P.V., Maccree M.M., Rockhold D.R.,
RA Corsini D.L., Davies H.V., Belknap W.R.;
RT "Metabolic compensation of steroidal glycoalkaloid biosynthesis in
RT transgenic potato tubers: using reverse genetics to confirm the in vivo
RT enzyme function of a steroidal alkaloid galactosyltransferase.";
RL Plant Sci. 168:267-273(2005).
CC -!- FUNCTION: Glucosyltransferase involved in the glucosylation of the
CC steroidal alkaloid aglycons solanidine, solasodine and tomatidine to
CC produce their corresponding glycoalkaloids.
CC {ECO:0000269|PubMed:9076990, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=solasodine + UDP-alpha-D-glucose = H(+) + solasodine 3-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:145042,
CC ChEBI:CHEBI:145043; Evidence={ECO:0000269|PubMed:9076990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61845;
CC Evidence={ECO:0000269|PubMed:9076990};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=solanidine + UDP-alpha-D-glucose = H(+) + solanidine 3-O-beta-
CC D-glucopyranoside + UDP; Xref=Rhea:RHEA:66280, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:166996,
CC ChEBI:CHEBI:166997; Evidence={ECO:0000269|PubMed:9076990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66281;
CC Evidence={ECO:0000269|PubMed:9076990};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tomatidine + UDP-alpha-D-glucose = H(+) + tomatidine 3-O-beta-
CC D-glucopyranoside + UDP; Xref=Rhea:RHEA:66284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:166998,
CC ChEBI:CHEBI:166999; Evidence={ECO:0000269|PubMed:9076990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66285;
CC Evidence={ECO:0000269|PubMed:9076990};
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem (SAM) and
CC tuber. {ECO:0000269|PubMed:9076990}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:9076990}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U82367; AAB48444.2; -; mRNA.
DR PIR; T07786; T07786.
DR AlphaFoldDB; P93789; -.
DR SMR; P93789; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR BioCyc; MetaCyc:MON-13434; -.
DR Proteomes; UP000011115; Unplaced.
DR ExpressionAtlas; P93789; baseline and differential.
DR GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..488
FT /note="Solanidine UDP-glucose glucosyltransferase 1"
FT /id="PRO_0000452278"
SQ SEQUENCE 488 AA; 55323 MW; E4CFE39C6CA5F00E CRC64;
MVATCNNGEI LHVLFLPFLS AGHFIPLVNA ARLFASRGVK ATILTTPHNA LLFRSTIDDD
VRISGFPISI VTIKFPSAEV GLPEGIESFN SATSPEMPHK IFYALSLLQK PMEDKIRELR
PDCIFSDMYF PWTVDIADEL HIPRILYNLS AYMCYSIMHN LKVYRPHKQP NLDESQSFVV
PGLPDEIKFK LSQLTDDLRK SDDQKTVFDE LLEQVEDSEE RSYGIVHDTF YELEPAYVDY
YQKLKKPKCW HFGPLSHFAS KIRSKELISE HNNNEIVIDW LNAQKPKSVL YVSFGSMARF
PESQLNEIAQ ALDASNVPFI FVLRPNEETA SWLPVGNLED KTKKGLYIKG WVPQLTIMEH
SATGGFMTHC GTNSVLEAIT FGVPMITWPL YADQFYNEKV VEVRGLGIKI GIDVWNEGIE
ITGPVIESAK IREAIERLMI SNGSEEIINI RDRVMAMSKM AQNATNEGGS SWNNLTALIQ
HIKNYNLN