ID   SCGT_TOBAC              Reviewed;         476 AA.
AC   Q9AT54;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Scopoletin glucosyltransferase;
DE            EC=2.4.1.128;
DE   AltName: Full=Phenylpropanoid:glucosyltransferase 1;
GN   Name=TOGT1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INDUCTION, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=cv. Samsun NN;
RX   PubMed=9824316; DOI=10.1016/s0014-5793(98)01257-5;
RA   Fraissinet-Tachet L., Baltz R., Chong J., Kauffmann S., Fritig B.,
RA   Saindrenan P.;
RT   "Two tobacco genes induced by infection, elicitor and salicylic acid encode
RT   glucosyltransferases acting on phenylpropanoids and benzoic acid
RT   derivatives, including salicylic acid.";
RL   FEBS Lett. 437:319-323(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=12034899; DOI=10.1105/tpc.010436;
RA   Chong J., Baltz R., Schmitt C., Beffa R., Fritig B., Saindrenan P.;
RT   "Downregulation of a pathogen-responsive tobacco UDP-Glc:phenylpropanoid
RT   glucosyltransferase reduces scopoletin glucoside accumulation, enhances
RT   oxidative stress, and weakens virus resistance.";
RL   Plant Cell 14:1093-1107(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=15159640; DOI=10.1023/b:plan.0000028775.58537.fe;
RA   Gachon C., Baltz R., Saindrenan P.;
RT   "Over-expression of a scopoletin glucosyltransferase in Nicotiana tabacum
RT   leads to precocious lesion formation during the hypersensitive response to
RT   tobacco mosaic virus but does not affect virus resistance.";
RL   Plant Mol. Biol. 54:137-146(2004).
CC   -!- FUNCTION: Glucosyltransferase acting preferentially on aromatic
CC       substrates of the phenylpropanoid types. The best substrates are
CC       scopoletin and esculetin. Required for full resistance to virus.
CC       {ECO:0000269|PubMed:12034899, ECO:0000269|PubMed:15159640}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=scopoletin + UDP-alpha-D-glucose = H(+) + scopolin + UDP;
CC         Xref=Rhea:RHEA:20453, ChEBI:CHEBI:15378, ChEBI:CHEBI:16065,
CC         ChEBI:CHEBI:17488, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.128; Evidence={ECO:0000269|PubMed:9824316};
CC   -!- INDUCTION: Up-regulated by elicitor, salicylic acid and virus
CC       infection. {ECO:0000269|PubMed:9824316}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF346431; AAK28303.1; -; mRNA.
DR   AlphaFoldDB; Q9AT54; -.
DR   SMR; Q9AT54; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BioCyc; MetaCyc:MON-17896; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0050275; F:scopoletin 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   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..476
FT                   /note="Scopoletin glucosyltransferase"
FT                   /id="PRO_0000418418"
SQ   SEQUENCE   476 AA;  53648 MW;  E68CD936C2C0E88B CRC64;
     MGQLHFFFFP VMAHGHMIPT LDMAKLFASR GVKATIITTP LNEFVFSKAI QRNKHLGIEI
     EIRLIKFPAV ENGLPEECER LDQIPSDEKL PNFFKAVAMM QEPLEQLIEE CRPDCLISDM
     FLPWTTDTAA KFNIPRIVFH GTSFFALCVE NSVRLNKPFK NVSSDSETFV VPDLPHEIKL
     TRTQVSPFER SGEETAMTRM IKTVRESDSK SYGVVFNSFY ELETDYVEHY TKVLGRRAWA
     IGPLSMCNRD IEDKAERGKK SSIDKHECLK WLDSKKPSSV VYVCFGSVAN FTASQLHELA
     MGIEASGQEF IWVVRTELDN EDWLPEGFEE RTKEKGLIIR GWAPQVLILD HESVGAFVTH
     CGWNSTLEGV SGGVPMVTWP VFAEQFFNEK LVTEVLKTGA GVGSIQWKRS ASEGVKREAI
     AKAIKRVMVS EEADGFRNRA KAYKEMARKA IEEGGSSYTG LTTLLEDIST YSSTGH