U91D2_STERE
ID U91D2_STERE Reviewed; 473 AA.
AC B3VI56;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=UDP-glycosyltransferase 91D2 {ECO:0000303|PubMed:26358188, ECO:0000303|PubMed:27923373};
DE EC=2.4.1.- {ECO:0000269|PubMed:26358188, ECO:0000269|PubMed:27923373};
GN Name=UGT91D2 {ECO:0000303|PubMed:26358188, ECO:0000303|PubMed:27923373};
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].
RC TISSUE=Leaf;
RA Joseph A.Y., Babu V.S., Dev S.S., Harish M., Rajesh M.D., Anisha S.,
RA Mohankumar C.;
RT "Isolation and cloning of Stevia rebaudiana UDP-glucosyltransferase.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26358188; DOI=10.1038/cr.2015.111;
RA Wang J., Li S., Xiong Z., Wang Y.;
RT "Pathway mining-based integration of critical enzyme parts for de novo
RT biosynthesis of steviolglycosides sweetener in Escherichia coli.";
RL Cell Res. 26:258-261(2016).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27923373; DOI=10.1186/s12934-016-0609-1;
RA Olsson K., Carlsen S., Semmler A., Simon E., Mikkelsen M.D., Moeller B.L.;
RT "Microbial production of next-generation stevia sweeteners.";
RL Microb. Cell Fact. 15:207-207(2016).
CC -!- FUNCTION: Involved in the biosynthesis of steviol glycosides in leaves
CC (PubMed:26358188, PubMed:27923373). Converts the mono-glycoside
CC steviolmonoside to the bi-glycoside steviolbioside (PubMed:26358188,
CC PubMed:27923373). Converts the bi-glycoside rubusoside to the tri-
CC glycoside stevioside (PubMed:27923373). Converts the tri-glycoside
CC stevioside to the tetra-glycoside rebaudioside E (PubMed:27923373).
CC Converts the tetra-glycoside rebaudioside A to the penta-glycoside
CC rebaudioside E (PubMed:27923373). {ECO:0000269|PubMed:26358188,
CC ECO:0000269|PubMed:27923373}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviolmonoside + UDP-alpha-D-glucose = H(+) + steviolbioside
CC + UDP; Xref=Rhea:RHEA:61740, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145009, ChEBI:CHEBI:145010;
CC Evidence={ECO:0000269|PubMed:26358188, ECO:0000269|PubMed:27923373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61741;
CC Evidence={ECO:0000269|PubMed:26358188, ECO:0000269|PubMed:27923373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rubusoside + UDP-alpha-D-glucose = H(+) + stevioside + UDP;
CC Xref=Rhea:RHEA:61748, ChEBI:CHEBI:9271, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:145021;
CC Evidence={ECO:0000269|PubMed:27923373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61749;
CC Evidence={ECO:0000269|PubMed:27923373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=stevioside + UDP-alpha-D-glucose = H(+) + rebaudioside E +
CC UDP; Xref=Rhea:RHEA:61764, ChEBI:CHEBI:9271, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:145018;
CC Evidence={ECO:0000269|PubMed:27923373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61765;
CC Evidence={ECO:0000269|PubMed:27923373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rebaudioside A + UDP-alpha-D-glucose = H(+) + rebaudioside D +
CC UDP; Xref=Rhea:RHEA:61768, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145012, ChEBI:CHEBI:145022;
CC Evidence={ECO:0000269|PubMed:27923373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61769;
CC Evidence={ECO:0000269|PubMed:27923373};
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}.
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DR EMBL; EU751291; ACE87855.1; -; mRNA.
DR AlphaFoldDB; B3VI56; -.
DR SMR; B3VI56; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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; Transferase.
FT CHAIN 1..473
FT /note="UDP-glycosyltransferase 91D2"
FT /id="PRO_0000449300"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT ACT_SITE 121
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 284
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 343..344
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 361..369
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 383..386
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 385..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
SQ SEQUENCE 473 AA; 52946 MW; 6CAEA1CAE0B75541 CRC64;
MATSDSIVDD RKQLHVATFP WLAFGHILPY LQLSKLIAEK GHKVSFLSTT RNIQRLSSHI
SPLINVVQLT LPRVQELPED AEATTDVHPE DIPYLKKASD GLQPEVTRFL EQHSPDWIIY
DYTHYWLPSI AASLGISRAH FSVTTPWAIA YMGPSADAMI NGSDGRTTVE DLTTPPKWFP
FPTKVCWRKH DLARLVPYKA PGISDGYRMG LVLKGSDCLL SKCYHEFGTQ WLPLLETLHQ
VPVVPVGLLP PEVPGDEKDE TWVSIKKWLD GKQKGSVVYV ALGSEVLVSQ TEVVELALGL
ELSGLPFVWA YRKPKGPAKS DSVELPDGFV ERTRDRGLVW TSWAPQLRIL SHESVCGFLT
HCGSGSIVEG LMFGHPLIML PIFGDQPLNA RLLEDKQVGI EIPRNEEDGC LTKESVARSL
RSVVVEKEGE IYKANARELS KIYNDTKVEK EYVSQFVDYL EKNTRAVAID HES
