708C2_FAGES
ID 708C2_FAGES Reviewed; 457 AA.
AC A0A0A1H7N4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=UDP-glycosyltransferase 708C2 {ECO:0000303|PubMed:25142187};
DE EC=2.4.1.360 {ECO:0000269|PubMed:25142187};
DE AltName: Full=C-glucosyltransferase b {ECO:0000303|PubMed:25142187};
DE Short=FeCGTb {ECO:0000303|PubMed:25142187};
DE AltName: Full=UDP-glucose:2-hydroxyflavanone C-glucosyltransferase {ECO:0000305};
GN Name=UGT708C2 {ECO:0000303|PubMed:25142187};
GN Synonyms=CGTb {ECO:0000303|PubMed:25142187};
OS Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX NCBI_TaxID=3617 {ECO:0000312|EMBL:BAP90361.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-103; 197-213; 257-270;
RP 322-330; 393-413; 416-424 AND 440-456, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25142187; DOI=10.1111/tpj.12645;
RA Nagatomo Y., Usui S., Ito T., Kato A., Shimosaka M., Taguchi G.;
RT "Purification, molecular cloning and functional characterization of
RT flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat)
RT cotyledon.";
RL Plant J. 80:437-448(2014).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the c-
CC glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-
CC hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin. No activity
CC with flavanones, flavones or flavonols. {ECO:0000269|PubMed:25142187}.
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:25142187};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000269|PubMed:25142187};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:25142187};
CC KM=6.5 uM for 2-hydroxypinocembrin {ECO:0000269|PubMed:25142187};
CC KM=38.5 uM for 2-phenyl-2',4',6'-trihydroxyactophenone
CC {ECO:0000269|PubMed:25142187};
CC KM=36 uM for UDP-glucose with 2-hydroxypinocembrin as acceptor
CC {ECO:0000269|PubMed:25142187};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25142187};
CC Temperature dependence:
CC Optimum temperature is 50-55 degrees Celsius.
CC {ECO:0000269|PubMed:25142187};
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons. Not detected in flowers,
CC leaves, roots and hypocotyls. {ECO:0000269|PubMed:25142187}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds and during
CC cotyledon development. {ECO:0000269|PubMed:25142187}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB909376; BAP90361.1; -; mRNA.
DR AlphaFoldDB; A0A0A1H7N4; -.
DR SMR; A0A0A1H7N4; -.
DR KEGG; ag:BAP90361; -.
DR BRENDA; 2.4.1.360; 2227.
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 Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..457
FT /note="UDP-glycosyltransferase 708C2"
FT /id="PRO_0000436255"
FT REGION 279..280
FT /note="UDP"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 129
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 31..34
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 150
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 340..343
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 358..366
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 382..383
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
SQ SEQUENCE 457 AA; 50433 MW; 211CB340244CF2C1 CRC64;
MMGDLTTSFP ATTLTTNEQP HVVVCSGAGM GHLIPFLNLA STLSSAPYRC KVTLLIVIPL
ITDAESHHIS SFFSSHPTIH RLDFHVNLPA PKPNVDPFFL RYKSISDSAH RLPVHLSTLA
PPISAVFSDF LFTQGLNTTL PHLPNYTFTT TSARFFTLMS YVPHLAKSSS SSPVEIPGLE
PFPTDNIPPP FFNPDHIFTS FTISNANYLS LSKGIIVNTF DSFEPETLSA LNSGDSLPDL
PPVIPIGPLN ELEHNKQEEL LPWLDQQPEK SVLYVSFGNR TAMSSDQILE LGMGLERSDC
RFIWVVKTSK IDKDDKSELR KLFGEELYVK LSEKGKLVKW VNQTEILGHT AVGGFLSHCG
WNSVMEAARR GVPILAWPQH GDQRENAWVV EKAGLGVWER EWSSGIQVAI VEKVKMIMGN
NDLRNSAVRV GEEAKRACDV GGSSATALMN IIGSLKR
