708G2_CITUN
ID 708G2_CITUN Reviewed; 472 AA.
AC A0A224AKZ9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=UDP-glycosyltransferase 708G2 {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=CuCGT {ECO:0000303|PubMed:28370711};
GN Name=UGT708G2; ORFNames=CUMW_024380 {ECO:0000312|EMBL:GAY36765.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase;
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-
CC glucosylation of 2-hydroxyflavanones (2-hydroxylnaringenin 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 pH dependence:
CC Optimum pH is 8.0-11.0. {ECO:0000269|PubMed:28370711};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:28370711};
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, flowers and
CC immature leaves. {ECO:0000269|PubMed:28370711}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC131334; BBA18063.1; -; mRNA.
DR EMBL; BDQV01000004; GAY36765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A224AKZ9; -.
DR SMR; A0A224AKZ9; -.
DR STRING; 55188.A0A224AKZ9; -.
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 708G2"
FT /id="PRO_0000452140"
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; 51624 MW; 16E360D86D4E8A8C CRC64;
MSDSGGFDSH PHVALIPSAG MGHLTPFLRL AASLVQHHCR VTLITTYPTV SLAETQHVSH
FLSAYPQVTE KRFHLLPFDP NSANATDPFL LRWEAIRRSA HLLAPLLSPP LSALITDVTL
ISAVLPVTIN LHLPNYVLFT ASAKMFSLTA SFPAIVASKS TSSGSVEFDD DFIEIPGLPP
IPLSSVPPAV MDSKSLFATS FLENGNSFVK SNGVLINSFD ALEADTLVAL NGRRVVAGLP
PVYAVGPLLP CEFEKRDDPS TSLILKWLDD QPEGSVVYVS FGSRLALSME QTKELGDGLL
SSGCRFLWVV KGKIVDKEDE ESLKNVLGHE LTEKIKDQGL VVKNWVDQDK VLSHRAVGGF
VSHGGWNSLV EAARHGVPLL VWPHFGDQKI NAEAVERAGL GMWVRSWGWG TELRAKGDEI
GLKIKDLMAN DFLREQAKRI EEEARKAIGV GGSSERTFKE LIDKWKCNNN TH
