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Database: UniProt
Entry: UFOG7_MANES
LinkDB: UFOG7_MANES
Original site: UFOG7_MANES 
ID   UFOG7_MANES             Reviewed;         287 AA.
AC   Q40289;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Anthocyanidin 3-O-glucosyltransferase 7;
DE            EC=2.4.1.115;
DE   AltName: Full=Flavonol 3-O-glucosyltransferase 7;
DE   AltName: Full=UDP-glucose flavonoid 3-O-glucosyltransferase 7;
DE   Flags: Fragment;
GN   Name=GT7; Synonyms=UGT73A7;
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=7894058; DOI=10.3109/10425179409039703;
RA   Hughes J., Hughes M.A.;
RT   "Multiple secondary plant product UDP-glucose glucosyltransferase genes
RT   expressed in cassava (Manihot esculenta Crantz) cotyledons.";
RL   DNA Seq. 5:41-49(1994).
CC   -!- FUNCTION: In the presence of other necessary color factors, this
CC       glycosylation reaction allows the accumulation of anthocyanin pigments.
CC       {ECO:0000250}.
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   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, roots and
CC       leaves.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all tissues (cotyledon, hypocotyls
CC       and roots) at uniform levels at all stages of development.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X77464; CAA54614.1; -; mRNA.
DR   PIR; S41953; S41953.
DR   AlphaFoldDB; Q40289; -.
DR   SMR; Q40289; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EnsemblPlants; OAY44585; OAY44585; MANES_08G163200.
DR   Gramene; OAY44585; OAY44585; MANES_08G163200.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0047213; F:anthocyanidin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48049:SF29; FLAVONOL 3-O-GLUCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR48049; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           <1..287
FT                   /note="Anthocyanidin 3-O-glucosyltransferase 7"
FT                   /id="PRO_0000074148"
FT   BINDING         162
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         164
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         179
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         182
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         183
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         184
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         187
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         202
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         203
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         204
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   NON_TER         1
SQ   SEQUENCE   287 AA;  31397 MW;  0A0D9C153C193571 CRC64;
     TLNLIPGMSK IQIRDLPEGV LFGNLESLFS QMLHNMGRML PRAAAVLMNS FEELDPTIVS
     DLNSKFNNIL CIGPFNLVSP PPPVPDTYGC MAWLDKQKPA SVAYISFGSV ATPPPHELVA
     LAEALEASKV PFLWSLKDHS KVHLPNGFLD RTKSHGIVLS WAPQVEILEH AALGVFVTHC
     GWNSILESIV GGVPMICRPF FGDQRLNGRM VEDVWEIGLL MDGGVLTKNG AIDGLNQILL
     QGKGKKMREN IKRLKELAKG ATEPKGSSSK SFTELANLVR SRGSYEN
//
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