ID   FLRT_CITMA              Reviewed;         452 AA.
AC   Q8GVE3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase;
DE            EC=2.4.1.236 {ECO:0000269|PubMed:1939145};
DE   AltName: Full=1,2 rhamnosyltransferase;
GN   Name=C12RT1; Synonyms=CM12RHAT;
OS   Citrus maxima (Pomelo) (Citrus grandis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=37334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 136-141; 178-186; 221-228;
RP   301-308 AND 379-392, AND TISSUE SPECIFICITY.
RX   PubMed=15361143; DOI=10.1111/j.1365-313x.2004.02193.x;
RA   Frydman A., Weisshaus O., Bar-Peled M., Huhman D.V., Sumner L.W.,
RA   Marin F.R., Lewinsohn E., Fluhr R., Gressel J., Eyal Y.;
RT   "Citrus fruit bitter flavors: isolation and functional characterization of
RT   the gene Cm1,2RhaT encoding a 1,2 rhamnosyltransferase, a key enzyme in the
RT   biosynthesis of the bitter flavonoids of citrus.";
RL   Plant J. 40:88-100(2004).
RN   [2]
RP   SEQUENCE REVISION.
RA   Frydman A., Weisshaus O., Bar-Peled M., Lewinsohn E., Neuman H., Fluhr R.,
RA   Gressel J., Eyal Y.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=1939145; DOI=10.1016/s0021-9258(18)54803-1;
RA   Bar-Peled M., Lewinsohn E., Fluhr R., Gressel J.;
RT   "UDP-rhamnose:flavanone-7-O-glucoside-2''-O-rhamnosyltransferase.
RT   Purification and characterization of an enzyme catalyzing the production of
RT   bitter compounds in citrus.";
RL   J. Biol. Chem. 266:20953-20959(1991).
CC   -!- FUNCTION: Involved in the production of the bitter neohesperidosides in
CC       citrus. Shows a strict specificity for UDP-rhamnose as donor.
CC       {ECO:0000269|PubMed:1939145}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=flavanone 7-O-beta-D-glucoside + UDP-beta-L-rhamnose =
CC         flavanone 7-O-[alpha-L-rhamnosyl-(1->2)-beta-D-glucoside] + H(+) +
CC         UDP; Xref=Rhea:RHEA:15473, ChEBI:CHEBI:15378, ChEBI:CHEBI:27590,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:79985, ChEBI:CHEBI:83836;
CC         EC=2.4.1.236; Evidence={ECO:0000269|PubMed:1939145};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.4 uM for prunin {ECO:0000269|PubMed:1939145};
CC         KM=41.5 uM for hesperetin-7-O-glucoside {ECO:0000269|PubMed:1939145};
CC         KM=1.3 uM for UDP-rhamnose with prunin as substrate
CC         {ECO:0000269|PubMed:1939145};
CC         KM=1.1 uM for UDP-rhamnose with hesperetin-7-O-glucoside as substrate
CC         {ECO:0000269|PubMed:1939145};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1939145}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in young fruits and leaves.
CC       {ECO:0000269|PubMed:15361143}.
CC   -!- INDUCTION: Inhibited by 10 uM UDP. {ECO:0000269|PubMed:1939145}.
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; AY048882; AAL06646.2; -; mRNA.
DR   AlphaFoldDB; Q8GVE3; -.
DR   SMR; Q8GVE3; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAL06646; -.
DR   BRENDA; 2.4.1.236; 1410.
DR   SABIO-RK; Q8GVE3; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033835; F:flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; PTHR48044; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48044:SF9; UDP-GLYCOSYLTRANSFERASES DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Glycosyltransferase; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..452
FT                   /note="Flavanone 7-O-glucoside 2""-O-beta-L-
FT                   rhamnosyltransferase"
FT                   /id="PRO_0000310730"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          407..436
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        121
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         21
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         268
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         330
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         347
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         351
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         352
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
FT   BINDING         355
FT                   /ligand="UDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:83836"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNE6"
SQ   SEQUENCE   452 AA;  51236 MW;  C648E2E5EBBCD8CB CRC64;
     MDTKHQDKPS ILMLPWLAHG HIAPHLELAK KLSQKNFHIY FCSTPNNLQS FGRNVEKNFS
     SSIQLIELQL PNTFPELPSQ NQTTKNLPPH LIYTLVGAFE DAKPAFCNIL ETLKPTLVMY
     DLFQPWAAEA AYQYDIAAIL FLPLSAVACS FLLHNIVNPS LKYPFFESDY QDRESKNINY
     FLHLTANGTL NKDRFLKAFE LSCKFVFIKT SREIESKYLD YFPSLMGNEI IPVGPLIQEP
     TFKEDDTKIM DWLSQKEPRS VVYASFGSEY FPSKDEIHEI ASGLLLSEVN FIWAFRLHPD
     EKMTIEEALP QGFAEEIERN NKGMIVQGWV PQAKILRHGS IGGFLSHCGW GSVVEGMVFG
     VPIIGVPMAY EQPSNAKVVV DNGMGMVVPR DKINQRLGGE EVARVIKHVV LQEEAKQIRR
     KANEISESMK KIGDAEMSVV VEKLLQLVKK SE
//