ID   GLT2_CROSA              Reviewed;         460 AA.
AC   Q6X1C0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Crocetin glucosyltransferase 2;
DE            EC=2.4.1.271;
GN   Name=GLT2;
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], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP   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|PubMed:15605174, 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|PubMed:15605174,
CC         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;
CC         Evidence={ECO:0000269|PubMed:15605174, 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 fully developed stigmas.
CC       {ECO:0000269|PubMed:15605174}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY262037; AAP94878.1; -; mRNA.
DR   AlphaFoldDB; Q6X1C0; -.
DR   SMR; Q6X1C0; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6X1C0; -.
DR   KEGG; ag:AAP94878; -.
DR   BioCyc; MetaCyc:MON-12719; -.
DR   BRENDA; 2.4.1.271; 7275.
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   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..460
FT                   /note="Crocetin glucosyltransferase 2"
FT                   /id="PRO_0000418815"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         331..333
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         348..356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         370..373
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  50722 MW;  F5DAC83E59D0CA92 CRC64;
     MLNGNKCHIL LLPCPAQGHI NPILQFGKRL ASHNLLTTLV NTRFLSNSTK SEPGPVNIQC
     ISDGFDPGGM NAAPSRRAYF DRPQSRSGQK HVGLIESLRS RGRPGACFGL RPVPLWAMNV
     AERSGLRSVA FFTQPCAVDT IYRHVWEGRI KVPVAEPVRL PGLPPLEPSD LPCVRNGFGR
     VVNPDLLPLR VNQHKNLDKA DMMGRNSIYE LEADLLDGSR LPLPVKSIGP TVPSTYLDNR
     IPSDSHYGFN LYTPDTTPYL DWLDSKAPNS VIYVSFGSLS SLSPDQTNEI ASGLIATNKS
     FIWVVRTSEL AKLPANFTQE NASRGLVVTW CDQLDLLAHV ATGCFVTHCG WNSTMEGVAL
     GVPMVGVPQW SDQPMNAKYV EDVWKVGVRA KTYGKDFVRG EEFKRCVEEV MDGERSGKIR
     ENAARWCKLA KDSVSEGGSS DKCIKEFIHQ CCNDSKISLV