ID   GLT3_CROSA              Reviewed;         475 AA.
AC   Q6WFW1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Crocetin glucosyltransferase 3;
DE            EC=2.4.1.271;
GN   Name=GLT3;
OS   Crocus sativus (Saffron).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Croceae; Crocus.
OX   NCBI_TaxID=82528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15605174; DOI=10.1007/s00425-004-1299-1;
RA   Moraga A.R., Nohales P.F., Perez J.A., Gomez-Gomez L.;
RT   "Glucosylation of the saffron apocarotenoid crocetin by a
RT   glucosyltransferase isolated from Crocus sativus stigmas.";
RL   Planta 219:955-966(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1016/S0168-9452(99)00248-4;
RA   Cote F., Cormier F., Dufresne C., Willemot C.;
RT   "Properties of a glucosyltransferase involved in crocin synthesis.";
RL   Plant Sci. 153:55-63(2000).
CC   -!- FUNCTION: Crocetin glucosyltransferase involved in the synthesis of
CC       crocin, one of the apocarotenoids responsible for the color and bitter
CC       taste of saffron. {ECO:0000269|PubMed:15605174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=crocetin + UDP-alpha-D-glucose = beta-D-glucosyl crocetin +
CC         UDP; Xref=Rhea:RHEA:31463, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:62766, ChEBI:CHEBI:62767; EC=2.4.1.271;
CC         Evidence={ECO:0000269|Ref.2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-glucosyl crocetin + UDP-alpha-D-glucose = bis(beta-D-
CC         glucosyl) crocetin + UDP; Xref=Rhea:RHEA:31467, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:62766, ChEBI:CHEBI:62768;
CC         EC=2.4.1.271; Evidence={ECO:0000269|Ref.2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-gentiobiosyl crocetin + UDP-alpha-D-glucose = beta-D-
CC         gentiobiosyl beta-D-glucosyl crocetin + UDP; Xref=Rhea:RHEA:31471,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:62770,
CC         ChEBI:CHEBI:62771; EC=2.4.1.271; Evidence={ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.17 mM for crocetin {ECO:0000269|Ref.2};
CC         KM=0.72 mM for UDP-glucose {ECO:0000269|Ref.2};
CC         Note=These parameters were determined on purified activity containing
CC         a mix of 2 enzymes, probably GLT2 and GLT3.;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in stamens.
CC       {ECO:0000269|PubMed:15605174}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY290820; AAQ56280.1; -; mRNA.
DR   AlphaFoldDB; Q6WFW1; -.
DR   SMR; Q6WFW1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..475
FT                   /note="Crocetin glucosyltransferase 3"
FT                   /id="PRO_0000418816"
FT   BINDING         289
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         371..379
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         393..396
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  52650 MW;  935755D523895FAA CRC64;
     MAKEHIVLFP FMSQGHIIPF LSLAKLISER HPTYTITLLN TPLNILNLQS TLPPNSNIHL
     KSLPYRSSDF GLPPDRENTD SLPFPLVLSF YQSGESLATH FTHFVSDLTR QNHDTPPLLI
     VADVFFGWTA EIAKRLNTHV SFSTCGAYGT AAYFSVWLHL PHAETDLPDF TAPGFPETFK
     LQRNQLSTYL KKADGSDRWS KFFQRQISLS LTSDAMICNT VEEMEAEGLR LLRKNTGLRV
     WSIGPLLPSL PPNSSLGRSG RKSGMEVSYI MKWLDSHPPG SVVYVSFGSI HDTAAQMTSL
     AVGLAVELAT RSCGHSGRRF GGNRNRNSNP NGVPDEFEAR MRGSGRGILI HGWAPQLEIL
     EHESTGAFVS HCGWNSTLES LSRGVCMIGW PLAAEQFYNS KMVEEDWEWG GTCEGSGGGV
     RSEEVERLVR LVTEDEKGSD EENEQYDEMI GGYEEKGGEG SLSGQLIKFI GMESQ