U85C2_STERE
ID U85C2_STERE Reviewed; 481 AA.
AC Q6VAB0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=UDP-glycosyltransferase 85C2 {ECO:0000303|PubMed:15610349};
DE EC=2.4.1.- {ECO:0000269|PubMed:15610349};
GN Name=UGT85C2 {ECO:0000303|PubMed:15610349};
OS Stevia rebaudiana (Stevia) (Eupatorium rebaudianum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Eupatorieae; Stevia.
OX NCBI_TaxID=55670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX PubMed=15610349; DOI=10.1111/j.1365-313x.2004.02275.x;
RA Richman A., Swanson A., Humphrey T., Chapman R., McGarvey B., Pocs R.,
RA Brandle J.;
RT "Functional genomics uncovers three glucosyltransferases involved in the
RT synthesis of the major sweet glucosides of Stevia rebaudiana.";
RL Plant J. 41:56-67(2005).
RN [2]
RP INDUCTION.
RX PubMed=28215607; DOI=10.1016/j.phytochem.2017.02.002;
RA Yoneda Y., Nakashima H., Miyasaka J., Ohdoi K., Shimizu H.;
RT "Impact of blue, red, and far-red light treatments on gene expression and
RT steviol glycoside accumulation in Stevia rebaudiana.";
RL Phytochemistry 137:57-65(2017).
CC -!- FUNCTION: Involved in the biosynthesis of steviol glycosides in leaves
CC (PubMed:15610349). Converts steviol to the mono-glycoside
CC steviolmonoside (PubMed:15610349). Converts the mono-glycoside
CC steviolmonoside to the bi-glycoside rubusoside (PubMed:15610349).
CC {ECO:0000269|PubMed:15610349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviol + UDP-alpha-D-glucose = H(+) + steviolmonoside + UDP;
CC Xref=Rhea:RHEA:61732, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145010, ChEBI:CHEBI:145011;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61733;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviolmonoside + UDP-alpha-D-glucose = rubusoside + UDP;
CC Xref=Rhea:RHEA:61736, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:145010, ChEBI:CHEBI:145021;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61737;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.3 uM for steviol {ECO:0000269|PubMed:15610349};
CC -!- INDUCTION: Induced by blue light and red:far-red light in a ratio of
CC 1.22. {ECO:0000269|PubMed:28215607}.
CC -!- MISCELLANEOUS: Leaves of the 'sweet herb' Stevia rebaudiana contain a
CC mix of steviol glycosides, compounds that are unique in the plant world
CC because of their intense sweetness and high concentration in leaf
CC tissue (Probable). Stevia leaves have been used as natural sweeteners
CC in South America for centuries (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY345978; AAR06916.1; -; mRNA.
DR AlphaFoldDB; Q6VAB0; -.
DR SMR; Q6VAB0; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR BioCyc; MetaCyc:MON-17483; -.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..481
FT /note="UDP-glycosyltransferase 85C2"
FT /id="PRO_0000434470"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT ACT_SITE 120
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 303
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 359..360
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 377..385
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 399..402
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 401..402
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
SQ SEQUENCE 481 AA; 54462 MW; 3BFFC8DFD9D90302 CRC64;
MDAMATTEKK PHVIFIPFPA QSHIKAMLKL AQLLHHKGLQ ITFVNTDFIH NQFLESSGPH
CLDGAPGFRF ETIPDGVSHS PEASIPIRES LLRSIETNFL DRFIDLVTKL PDPPTCIISD
GFLSVFTIDA AKKLGIPVMM YWTLAACGFM GFYHIHSLIE KGFAPLKDAS YLTNGYLDTV
IDWVPGMEGI RLKDFPLDWS TDLNDKVLMF TTEAPQRSHK VSHHIFHTFD ELEPSIIKTL
SLRYNHIYTI GPLQLLLDQI PEEKKQTGIT SLHGYSLVKE EPECFQWLQS KEPNSVVYVN
FGSTTVMSLE DMTEFGWGLA NSNHYFLWII RSNLVIGENA VLPPELEEHI KKRGFIASWC
SQEKVLKHPS VGGFLTHCGW GSTIESLSAG VPMICWPYSW DQLTNCRYIC KEWEVGLEMG
TKVKRDEVKR LVQELMGEGG HKMRNKAKDW KEKARIAIAP NGSSSLNIDK MVKEITVLAR
N
