UFOG_VITVI
ID UFOG_VITVI Reviewed; 456 AA.
AC P51094; A5BVQ6; A7PBD4; O22303; O22304; Q1G141; Q9AQV0; Q9AR43; Q9AR45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Anthocyanidin 3-O-glucosyltransferase UFGT {ECO:0000305};
DE EC=2.4.1.115 {ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
DE AltName: Full=Flavonol 3-O-glucosyltransferase {ECO:0000305};
DE EC=2.4.1.91 {ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
DE AltName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase {ECO:0000303|PubMed:9535914};
GN Name=UFGT {ECO:0000303|PubMed:9535914};
GN Synonyms=AlUFGT1, AlUFGT2, FlUFGT1, FlUFGT2, ITUFGT1, ITUFGT2, RUUFGT1,
GN RUUFGT2, VVGT1; ORFNames=GSVIVT00014047001, LOC100233099, VITISV_008354;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT VAL-134.
RC STRAIN=cv. Shiraz; TISSUE=Fruit;
RX PubMed=9535914; DOI=10.1074/jbc.273.15.9224;
RA Ford C.M., Boss P.K., Hoj P.B.;
RT "Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-
RT glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-
RT 1 locus that may primarily serve to glucosylate anthocyanidins in vivo.";
RL J. Biol. Chem. 273:9224-9233(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, and
RC cv. Ruby Okuyama;
RX PubMed=11166442; DOI=10.1016/s0168-9452(00)00425-8;
RA Kobayashi S., Ishimaru M., Ding C.K., Yakushiji H., Goto N.;
RT "Comparison of UDP-glucose:flavonoid 3-O-glucosyltransferase (UFGT) gene
RT sequences between white grapes (Vitis vinifera) and their sports with red
RT skin.";
RL Plant Sci. 160:543-550(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Red Globe;
RA Cheng J.H., Wu J., Yang F.C.;
RT "Molecular cloning of UDP-glucose:flavonoid 3-O-glucosyltransferase (UFGT)
RT gene from Vitis vinifera Red Globe.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir;
RX PubMed=18094749; DOI=10.1371/journal.pone.0001326;
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "A high quality draft consensus sequence of the genome of a heterozygous
RT grapevine variety.";
RL PLoS ONE 2:E1326-E1326(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 303-456, AND INDUCTION.
RC STRAIN=cv. Lambrusco Foglia Frastagliata;
RX PubMed=8193299; DOI=10.1007/bf00029856;
RA Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT "Cloning and molecular analysis of structural genes involved in flavonoid
RT and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL Plant Mol. Biol. 24:743-755(1994).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=8980508; DOI=10.1007/bf00019111;
RA Boss P.K., Davies C., Robinson S.P.;
RT "Expression of anthocyanin biosynthesis pathway genes in red and white
RT grapes.";
RL Plant Mol. Biol. 32:565-569(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE-DERIVED
RP DONOR AND KAEMPFEROL OR IN COMPLEX WITH UDP AND QUERCETIN, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-20;
RP THR-141; ASP-374 AND GLN-375.
RX PubMed=16482224; DOI=10.1038/sj.emboj.7600970;
RA Offen W., Martinez-Fleites C., Yang M., Kiat-Lim E., Davis B.G.,
RA Tarling C.A., Ford C.M., Bowles D.J., Davies G.J.;
RT "Structure of a flavonoid glucosyltransferase reveals the basis for plant
RT natural product modification.";
RL EMBO J. 25:1396-1405(2006).
CC -!- FUNCTION: In the presence of other necessary color factors, this
CC glycosylation reaction allows the accumulation of anthocyanin pigments
CC (Probable). Involved in the formation of red wine pigments (Probable).
CC UDP-glucose (UDP-Glc) is the physiological sugar donor, and cyanidin is
CC the natural acceptor in vivo (PubMed:9535914). Can glucosylate the
CC anthocyanidins delphinidin, peonidin, pelargonidin and malvidin
CC (PubMed:9535914). The flavonols quercitin and kaempferol can also be
CC glucosylated in vitro, but with glucosylation rates 50-100 times lower
CC than cyanidin (PubMed:9535914). In vitro, can use UDP-Glc, UDP-5SGlc,
CC UDP-Xyl, UDP-Man, UDP-Gal, UDP-GlcNAc, GDP-Glc, dTDP-Glc and dTDP-Xyl
CC as sugar donors, but not UDP-6OMeGal, UDP-Ara, UDP-6FGal, UDP-GlcN,
CC UDP-2FGal, UDP-5SAra, GDP-Man, GDP-Fuc, UDP-Fuc or UDP-Rha
CC (PubMed:16482224). {ECO:0000269|PubMed:16482224,
CC ECO:0000269|PubMed:9535914, ECO:0000305|PubMed:16482224,
CC ECO:0000305|PubMed:9535914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anthocyanidin + H(+) + UDP-alpha-D-glucose = an
CC anthocyanidin 3-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:20093,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16307, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:143576; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20094;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanidin + UDP-alpha-D-glucose = cyanidin 3-O-beta-D-glucoside
CC + H(+) + UDP; Xref=Rhea:RHEA:60100, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71682,
CC ChEBI:CHEBI:77857; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60101;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delphinidin + UDP-alpha-D-glucose = delphinidin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61500, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:144775, ChEBI:CHEBI:144776;
CC EC=2.4.1.115; Evidence={ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61501;
CC Evidence={ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peonidin + UDP-alpha-D-glucose = peonidin 3-O-beta-D-glucoside
CC + UDP; Xref=Rhea:RHEA:61508, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:144779, ChEBI:CHEBI:144780; EC=2.4.1.115;
CC Evidence={ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61509;
CC Evidence={ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pelargonidin + UDP-alpha-D-glucose = pelargonidin 3-O-beta-D-
CC glucoside + UDP; Xref=Rhea:RHEA:61504, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:144777, ChEBI:CHEBI:144778;
CC EC=2.4.1.115; Evidence={ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61505;
CC Evidence={ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malvidin + UDP-alpha-D-glucose = malvidin 3-O-beta-D-glucoside
CC + UDP; Xref=Rhea:RHEA:61512, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:144781, ChEBI:CHEBI:144782;
CC Evidence={ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61513;
CC Evidence={ECO:0000269|PubMed:9535914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:22300, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16816, ChEBI:CHEBI:28802, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.91;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22302;
CC Evidence={ECO:0000269|PubMed:16482224, ECO:0000269|PubMed:9535914};
CC -!- ACTIVITY REGULATION: Inhibited by Mn(2+) and Zn(2+).
CC {ECO:0000269|PubMed:9535914}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for UDP-Glc (in the presence of quercitin)
CC {ECO:0000269|PubMed:9535914};
CC KM=679 uM for UDP-Glc (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=300 uM for dTDP-Glc (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=166 uM for UDP-5SGlc (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=194 uM for UDP-GlcNAc (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=48.2 uM for UDP-Gal (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=50.1 uM for UDP-Man (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=167 uM for GDP-Glc (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=166 uM for dTDP-Xyl (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=219 uM for UDP-Xyl (in the presence of 100 uM quercitin)
CC {ECO:0000269|PubMed:16482224};
CC KM=15 uM for quercitin (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:9535914};
CC KM=30.8 uM for quercitin (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:16482224};
CC KM=42.3 uM for kaempferol (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:16482224};
CC KM=30 uM for cyanidin (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:9535914};
CC KM=16 uM for delphinidin (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:9535914};
CC KM=35.7 uM for malvidin (in the presence of UDP-Glc)
CC {ECO:0000269|PubMed:9535914};
CC Vmax=18.9 nmol/sec/mg enzyme with quercitin as substrate
CC {ECO:0000269|PubMed:9535914};
CC Vmax=905 nmol/sec/mg enzyme with cyanidin as substrate
CC {ECO:0000269|PubMed:9535914};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16482224,
CC ECO:0000269|PubMed:9535914};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC -!- TISSUE SPECIFICITY: Detected only in berry skin.
CC {ECO:0000269|PubMed:8980508}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:8193299}.
CC -!- MISCELLANEOUS: The expression of UFGT is not detected in white grapes.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53582.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF000371; AAB81682.1; -; mRNA.
DR EMBL; AF000372; AAB81683.1; -; mRNA.
DR EMBL; AB047092; BAB41019.1; -; Genomic_DNA.
DR EMBL; AB047093; BAB41020.1; -; Genomic_DNA.
DR EMBL; AB047094; BAB41021.1; -; Genomic_DNA.
DR EMBL; AB047095; BAB41022.1; -; Genomic_DNA.
DR EMBL; AB047096; BAB41023.1; -; Genomic_DNA.
DR EMBL; AB047097; BAB41024.1; -; Genomic_DNA.
DR EMBL; AB047098; BAB41025.1; -; Genomic_DNA.
DR EMBL; AB047099; BAB41026.1; -; Genomic_DNA.
DR EMBL; DQ513314; ABF59818.1; -; Genomic_DNA.
DR EMBL; AM472935; CAN61846.1; -; Genomic_DNA.
DR EMBL; X75968; CAA53582.1; ALT_FRAME; mRNA.
DR PDB; 2C1X; X-ray; 1.90 A; A=1-456.
DR PDB; 2C1Z; X-ray; 1.90 A; A=1-456.
DR PDB; 2C9Z; X-ray; 2.10 A; A=1-456.
DR PDBsum; 2C1X; -.
DR PDBsum; 2C1Z; -.
DR PDBsum; 2C9Z; -.
DR AlphaFoldDB; P51094; -.
DR SMR; P51094; -.
DR STRING; 29760.VIT_16s0039g02230.t01; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; P51094; -.
DR eggNOG; KOG1192; Eukaryota.
DR BRENDA; 2.4.1.115; 6671.
DR UniPathway; UPA00009; -.
DR EvolutionaryTrace; P51094; -.
DR ExpressionAtlas; P51094; baseline and differential.
DR GO; GO:0047213; F:anthocyanidin 3-O-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102360; F:daphnetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047893; F:flavonol 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102425; F:myricetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033485; P:cyanidin 3-O-glucoside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033330; P:kaempferol O-glucoside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033303; P:quercetin O-glucoside biosynthetic 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 3D-structure; Glycosyltransferase; Transferase.
FT CHAIN 1..456
FT /note="Anthocyanidin 3-O-glucosyltransferase UFGT"
FT /id="PRO_0000074151"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 19
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 141
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 280
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 306
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 333
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 350..358
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT BINDING 374..375
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:16482224,
FT ECO:0007744|PDB:2C1Z"
FT VARIANT 47
FT /note="Q -> Z (in strain: cv. Pinot noir)"
FT VARIANT 69
FT /note="I -> V (in strain: cv. Italia, cv. Pinot noir and
FT cv. Ruby Okuyama)"
FT VARIANT 74
FT /note="P -> A (in strain: cv. Pinot noir / PN40024)"
FT VARIANT 91
FT /note="T -> M (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024, cv. Red Globe and cv. Ruby Okuyama)"
FT VARIANT 134
FT /note="L -> V (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024, cv. Red Globe and cv. Ruby Okuyama)"
FT /evidence="ECO:0000269|PubMed:9535914"
FT VARIANT 153
FT /note="I -> T (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir / PN40024, cv. Red
FT Globe and cv. Ruby Okuyama)"
FT VARIANT 161
FT /note="G -> A (in cv. Red Globe)"
FT VARIANT 163
FT /note="S -> SG (in strain: cv. Pinot noir / PN40024)"
FT VARIANT 255
FT /note="V -> I (in strain: cv. Italia, cv. Pinot noir /
FT PN40024 and cv. Ruby Okuyama)"
FT VARIANT 289
FT /note="V -> L (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024, cv. Red Globe and cv. Ruby Okuyama)"
FT VARIANT 293
FT /note="S -> A (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024, cv. Red Globe and cv. Ruby Okuyama)"
FT VARIANT 312
FT /note="R -> S (in strain: cv. Flame Muscat, cv. Lambrusco
FT Foglia Frastagliata and cv. Muscat of Alexandria)"
FT VARIANT 326
FT /note="Y -> H (in cv. Red Globe)"
FT VARIANT 372
FT /note="F -> Y (in strain: cv. Pinot noir / PN40024)"
FT VARIANT 385
FT /note="V -> A (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024, cv. Red Globe and cv. Ruby Okuyama)"
FT VARIANT 399..400
FT /note="KS -> EN (in strain: cv. Flame Muscat and cv. Muscat
FT of Alexandria)"
FT VARIANT 399
FT /note="K -> E (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /
FT PN40024 and cv. Ruby Okuyama)"
FT VARIANT 423
FT /note="R -> G (in strain: cv. Pinot noir / PN40024)"
FT VARIANT 444
FT /note="I -> K (in strain: cv. Flame Muscat, cv. Italia, cv.
FT Lambrusco Foglia Frastagliata, cv. Muscat of Alexandria,
FT cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and
FT cv. Ruby Okuyama)"
FT MUTAGEN 20
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16482224"
FT MUTAGEN 141
FT /note="T->A: 6-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16482224"
FT MUTAGEN 374
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16482224"
FT MUTAGEN 375
FT /note="Q->H: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16482224"
FT MUTAGEN 375
FT /note="Q->N: Impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:16482224"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:2C1X"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:2C1X"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:2C1X"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:2C1X"
SQ SEQUENCE 456 AA; 50150 MW; 60BF6A70A3D17ABC CRC64;
MSQTTTNPHV AVLAFPFSTH AAPLLAVVRR LAAAAPHAVF SFFSTSQSNA SIFHDSMHTM
QCNIKSYDIS DGVPEGYVFA GRPQEDIELF TRAAPESFRQ GMVMAVAETG RPVSCLVADA
FIWFAADMAA EMGLAWLPFW TAGPNSLSTH VYIDEIREKI GVSGIQGRED ELLNFIPGMS
KVRFRDLQEG IVFGNLNSLF SRMLHRMGQV LPKATAVFIN SFEELDDSLT NDLKSKLKTY
LNIGPFNLIT PPPVVPNTTG CLQWLKERKP TSVVYISFGT VTTPPPAEVV ALSEALEASR
VPFIWSLRDK ARVHLPEGFL EKTRGYGMVV PWAPQAEVLA HEAVGAFVTH CGWNSLWESV
AGGVPLICRP FFGDQRLNGR MVEDVLEIGV RIEGGVFTKS GLMSCFDQIL SQEKGKKLRE
NLRALRETAD RAVGPKGSST ENFITLVDLV SKPKDV
