74AC1_SIRGR
ID 74AC1_SIRGR Reviewed; 454 AA.
AC K7NBW3;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Mogroside IE synthase {ECO:0000305};
DE EC=2.4.1.350 {ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3};
DE AltName: Full=UDP-glycosyltransferase 74AC1 {ECO:0000303|PubMed:25759326};
GN Name=UGT74AC1 {ECO:0000303|PubMed:25759326};
GN Synonyms=UDPG1 {ECO:0000312|EMBL:AEM42999.1};
OS Siraitia grosvenorii (Monk's fruit) (Luo han guo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Siraitieae; Siraitia.
OX NCBI_TaxID=190515;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tang B., Ding L., Zhang Q., Tang W., Pan H.;
RT "Two B-glucosidase genes were isolated from the library of rhizopus
RT stolonifer var. reflexus and expressed in Pichia pastoris.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25759326; DOI=10.1093/pcp/pcv043;
RA Dai L., Liu C., Zhu Y., Zhang J., Men Y., Zeng Y., Sun Y.;
RT "Functional characterization of cucurbitadienol synthase and triterpene
RT glycosyltransferase involved in biosynthesis of mogrosides from Siraitia
RT grosvenorii.";
RL Plant Cell Physiol. 56:1172-1182(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UDP-D-GLUCOSE,
RP DISULFIDE BONDS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF SER-15; HIS-18; ARG-28; HIS-47; LEU-48;
RP MET-76; THR-79; LEU-109 AND ASP-111.
RX DOI=10.1021/acscatal.9b05232;
RA Li J., Yang J.G., Mu S., Shang N., Liu C., Zhu Y., Cai Y., Liu P., Lin J.,
RA Liu W.D., Sun Y.X., Ma Y.;
RT "Efficient O-glycosylation of triterpenes enabled by protein engineering of
RT plant glycosyltransferase UGT74AC1.";
RL ACS Catal. 0:0-0(2020).
CC -!- FUNCTION: Catalyzes the transfer of a glucose moiety to the C-3
CC hydroxyl of mogrol to form mogroside IE (PubMed:25759326, Ref.3).
CC Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin
CC and naringenin as substrate (PubMed:25759326).
CC {ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP;
CC Xref=Rhea:RHEA:52044, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:138974, ChEBI:CHEBI:138975;
CC EC=2.4.1.350; Evidence={ECO:0000269|PubMed:25759326,
CC ECO:0000269|Ref.3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52045;
CC Evidence={ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.4 uM for mogrol {ECO:0000269|PubMed:25759326};
CC KM=49.4 uM for mogrol {ECO:0000269|Ref.3};
CC KM=890.2 uM for UDP-alpha-D-glucose {ECO:0000269|Ref.3};
CC KM=58.2 uM for quercetin {ECO:0000269|PubMed:25759326};
CC KM=54.7 uM for naringenin {ECO:0000269|PubMed:25759326};
CC -!- MISCELLANEOUS: Mogrosides, the major active constituents of
CC S.grosvenorii fruits, are a mixture of cucurbitane-type triterpenoid
CC glycosides that have been proven to be powerful and zero-caloric
CC sweeteners and can hence be used as a sucrose substitute for diabetic
CC and obese patients. {ECO:0000305|PubMed:25759326}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HQ259620; AEM42999.1; -; mRNA.
DR PDB; 6L8W; X-ray; 2.05 A; A=1-454.
DR PDB; 6L8X; X-ray; 1.55 A; A=1-454.
DR PDB; 6L8Z; X-ray; 2.10 A; A=1-454.
DR PDB; 6L90; X-ray; 2.02 A; A=1-454.
DR PDBsum; 6L8W; -.
DR PDBsum; 6L8X; -.
DR PDBsum; 6L8Z; -.
DR PDBsum; 6L90; -.
DR AlphaFoldDB; K7NBW3; -.
DR SMR; K7NBW3; -.
DR KEGG; ag:AEM42999; -.
DR BioCyc; MetaCyc:MON-21296; -.
DR BRENDA; 2.4.1.350; 3400.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; 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 3D-structure; Disulfide bond; Glycosyltransferase; Transferase.
FT CHAIN 1..454
FT /note="Mogroside IE synthase"
FT /id="PRO_0000451485"
FT BINDING 278
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 331..333
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 351..356
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 372..373
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|Ref.3"
FT DISULFID 259..331
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:6L8W,
FT ECO:0007744|PDB:6L8X, ECO:0007744|PDB:6L8Z"
FT MUTAGEN 15
FT /note="S->A: Increases catalytic efficiency more than
FT 10000-fold; when associated with H-28, R-47, M-48, L-76, Y-
FT 79 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 18
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 28
FT /note="R->H: Increases catalytic efficiency more than
FT 10000-fold; when associated with A-15, R-47, M-48, L-76, Y-
FT 79 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 47
FT /note="H->R: Increases catalytic efficiency more than
FT 10000-fold; when associated with A-15, H-28, M-48, L-76, Y-
FT 79 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 48
FT /note="L->M: Increases catalytic efficiency more than
FT 10000-fold; when associated with A-15, H-28, R-47, L-76, Y-
FT 79 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 76
FT /note="M->L: Increases catalytic efficiency more than
FT 10000-fold; when associated with A-15, H-28, R-47, M-48, Y-
FT 79 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 79
FT /note="T->Y: Increases catalytic efficiency more than
FT 10000-fold; when associated with A-15, H-28, R-47, M-48, L-
FT 76 and I-109."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 109
FT /note="L->I: Increases catalytic efficiency more than
FT 10000-fold when associated with A-15, H-28, R-47, M-48, L-
FT 76 and Y-79."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 111
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:6L8X"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 76..98
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6L8W"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6L8X"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6L8Z"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6L8W"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:6L8X"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6L8W"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:6L8X"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:6L8X"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 416..434
FT /evidence="ECO:0007829|PDB:6L8X"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:6L8X"
SQ SEQUENCE 454 AA; 51275 MW; 384BC582A3FB7E3A CRC64;
MEKGDTHILV FPFPSQGHIN PLLQLSKRLI AKGIKVSLVT TLHVSNHLQL QGAYSNSVKI
EVISDGSEDR LETDTMRQTL DRFRQKMTKN LEDFLQKAMV SSNPPKFILY DSTMPWVLEV
AKEFGLDRAP FYTQSCALNS INYHVLHGQL KLPPETPTIS LPSMPLLRPS DLPAYDFDPA
STDTIIDLLT SQYSNIQDAN LLFCNTFDKL EGEIIQWMET LGRPVKTVGP TVPSAYLDKR
VENDKHYGLS LFKPNEDVCL KWLDSKPSGS VLYVSYGSLV EMGEEQLKEL ALGIKETGKF
FLWVVRDTEA EKLPPNFVES VAEKGLVVSW CSQLEVLAHP SVGCFFTHCG WNSTLEALCL
GVPVVAFPQW ADQVTNAKFL EDVWKVGKRV KRNEQRLASK EEVRSCIWEV MEGERASEFK
SNSMEWKKWA KEAVDEGGSS DKNIEEFVAM LKQT
