708G1_CITJP
ID 708G1_CITJP Reviewed; 472 AA.
AC A0A224AM54;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=UDP-glycosyltransferase 708G1 {ECO:0000303|PubMed:28370711};
DE EC=2.4.1.360 {ECO:0000269|PubMed:28370711};
DE AltName: Full=2-hydroxyflavanone C-glucosyltransferase {ECO:0000305};
DE AltName: Full=FcCGT {ECO:0000303|PubMed:28370711};
GN Name=UGT708G1 {ECO:0000303|PubMed:28370711};
OS Citrus japonica (Kumquat) (Fortunella crassifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=76966;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=28370711; DOI=10.1111/tpj.13555;
RA Ito T., Fujimoto S., Suito F., Shimosaka M., Taguchi G.;
RT "C-Glycosyltransferases catalyzing the formation of di-C-glucosyl
RT flavonoids in citrus plants.";
RL Plant J. 91:187-198(2017).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-
CC glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin and 2-
CC hydroxypinocembrin) and phloretin (PubMed:28370711). No activity with
CC flavanones, flavones or flavonols (PubMed:28370711). Exhibits C-
CC glucosylation activity toward 2-phenyl-2',4',6'-trihydroxyacetophenone
CC (PubMed:28370711). Can use UDP-xylose as sugar donor, but catalytic
CC efficiency is much lower toward UDP-xylose than toward UDP-glucose
CC (PubMed:28370711). {ECO:0000269|PubMed:28370711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-
CC glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-
CC oxodihydrochalcone + H(+) + UDP; Xref=Rhea:RHEA:51504,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:142482, ChEBI:CHEBI:142483; EC=2.4.1.360;
CC Evidence={ECO:0000269|PubMed:28370711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000269|PubMed:28370711};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for phloretin {ECO:0000269|PubMed:28370711};
CC KM=0.85 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:28370711};
CC KM=14.4 uM for 3'-C-glucosylphloretin {ECO:0000269|PubMed:28370711};
CC KM=112.5 uM for 6-C-glucosyl-2-hydroxynaringenin
CC {ECO:0000269|PubMed:28370711};
CC KM=71.5 uM for UDP-glucose with 3'-C-glucosylphloretin as acceptor
CC {ECO:0000269|PubMed:28370711};
CC pH dependence:
CC Optimum pH is 8.0-11.0. {ECO:0000269|PubMed:28370711};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:28370711};
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers, and at lower
CC levels in immature fruits. {ECO:0000269|PubMed:28370711}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC131333; BBA18062.1; -; mRNA.
DR AlphaFoldDB; A0A224AM54; -.
DR SMR; A0A224AM54; -.
DR GO; GO:0035251; F:UDP-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; Transferase.
FT CHAIN 1..472
FT /note="UDP-glycosyltransferase 708G1"
FT /id="PRO_0000452139"
FT REGION 283..284
FT /note="UDP"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 117
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 22..25
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 140
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 345..348
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 363..371
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 387..388
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
SQ SEQUENCE 472 AA; 51611 MW; 902AC5A0D56C7C9B CRC64;
MSDSGGFDSH PHVALIPSAG MGHLTPFLRL AASLVQHHCR VTLITTYPTV SLAETQHVSH
FLSAYPQVTE KRFHLLPFDP NSANATDPFF LRWEAIRRSA HLLAPLLSPP LSALITDVTL
ISAVLPVTIN LHLPNYVLFT ASARMFSLTA SFPAIVASKS TSSGSVEFDD DFIEIPGLPP
IPLSSVPPAV MDSKSLFATS FLENGNSFVK SNGVLINSFD ALEADTLVAL NGRRVVAGLP
PVYAVGPLLP CEFEKRDDPS TSLILKWLDD QPEGSVVYVS FGSRLALSME QTKELGNGLL
SSGCRFLWVV KGKTVDKEDE ESLKNVLGHE LMEKIKDQGL VVKNWVDQDK VLSHRAVGGF
VSHGGWNSLV EAARHGVPVL VWPQFGDQKI NAEAVESAGL GMWVRSWGWG TELRAKGDEI
GLKIKDLMAN DFLREQAKRI EEEARKAIGV GGSSERTFKE LIDKWKCNNN TH
