708C1_FAGES
ID 708C1_FAGES Reviewed; 457 AA.
AC A0A0A1HA03;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=UDP-glycosyltransferase 708C1 {ECO:0000303|PubMed:25142187};
DE EC=2.4.1.360 {ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169};
DE AltName: Full=C-glucosyltransferase a {ECO:0000303|PubMed:25142187};
DE Short=FeCGTa {ECO:0000303|PubMed:25142187};
DE AltName: Full=UDP-glucose:2-hydroxyflavanone C-glucosyltransferase {ECO:0000305};
GN Name=UGT708C1 {ECO:0000303|PubMed:25142187};
GN Synonyms=CGTa {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:BAP90360.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-103; 197-213; 257-270;
RP 322-330; 393-413 AND 416-425, 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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP AND MUTAGENESIS OF TYR-102; PHE-130; THR-150; THR-151; PHE-198; ASP-382 AND
RP GLN-383.
RX PubMed=32699169; DOI=10.1105/tpc.20.00002;
RA Liu M., Wang D., Li Y., Li X., Zong G., Fei S., Yang X., Lin J., Wang X.,
RA Shen Y.;
RT "Crystal structures of the c-glycosyltransferase UGT708C1 from buckwheat
RT provide insights into the mechanism of C-glycosylation.";
RL Plant Cell 32:2917-2931(2020).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 17-457.
RA Koyanagi Y., Arai R., Taguchi G.;
RT "Crystal structure of a flavonoid C-glucosyltrasferase from Fagopyrum
RT esculentum.";
RL Submitted (SEP-2020) to the PDB data bank.
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-
CC glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-
CC hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin
CC (PubMed:25142187). No activity with flavanones, flavones or flavonols
CC (PubMed:25142187). Exhibits C-glycosylation activity toward 2',4',6'-
CC trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor
CC (PubMed:32699169). Can use UDP-galactose as sugar donor, but catalytic
CC efficiency is 14-fold lower toward UDP-galactose than toward UDP-
CC glucose (PubMed:32699169). {ECO:0000269|PubMed:25142187,
CC ECO:0000269|PubMed:32699169}.
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, ECO:0000269|PubMed:32699169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:25142187};
CC KM=40 uM for 2-hydroxypinocembrin {ECO:0000269|PubMed:25142187};
CC KM=36.5 uM for 2-phenyl-2',4',6'-trihydroxyactophenone
CC {ECO:0000269|PubMed:25142187};
CC KM=3.73 uM for phloretin {ECO:0000269|PubMed:32699169};
CC KM=14.66 uM for 2',4',6'-trihydroxyacetophenone
CC {ECO:0000269|PubMed:32699169};
CC KM=58.1 uM for UDP-glucose with 2-hydroxypinocembrin as acceptor
CC {ECO:0000269|PubMed:25142187};
CC KM=56.95 uM for UDP-glucose with phloretin as acceptor
CC {ECO:0000269|PubMed:32699169};
CC KM=42.55 uM for UDP-glucose with 2',4',6'-trihydroxyacetophenone as
CC acceptor {ECO:0000269|PubMed:32699169};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25142187};
CC Temperature dependence:
CC Optimum temperature is 45-50 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; AB909375; BAP90360.1; -; mRNA.
DR PDB; 6LLG; X-ray; 2.10 A; A/B=1-457.
DR PDB; 6LLW; X-ray; 2.26 A; A/B=1-457.
DR PDB; 6LLZ; X-ray; 2.01 A; A/B=1-457.
DR PDB; 7CYW; X-ray; 1.80 A; A=17-457.
DR PDBsum; 6LLG; -.
DR PDBsum; 6LLW; -.
DR PDBsum; 6LLZ; -.
DR PDBsum; 7CYW; -.
DR AlphaFoldDB; A0A0A1HA03; -.
DR SMR; A0A0A1HA03; -.
DR KEGG; ag:BAP90360; -.
DR BioCyc; MetaCyc:MON-17888; -.
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 3D-structure; Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..457
FT /note="UDP-glycosyltransferase 708C1"
FT /id="PRO_0000436254"
FT REGION 279..280
FT /note="UDP"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLW"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:32699169"
FT ACT_SITE 129
FT /note="Charge relay"
FT /evidence="ECO:0000305|PubMed:32699169"
FT BINDING 31..34
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLZ"
FT BINDING 150
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLZ"
FT BINDING 340..343
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLZ"
FT BINDING 358..366
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLZ"
FT BINDING 382..383
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:32699169,
FT ECO:0007744|PDB:6LLZ"
FT MUTAGEN 102
FT /note="Y->F: Decreases affinity for phloretin 2.9-fold and
FT increases affinity for UDP-glucose 2-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 130
FT /note="F->A: Decreases affinity for phloretin 2.1-fold and
FT affinity for UDP-glucose 1.5-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 150
FT /note="T->A: Decreases affinity for phloretin 2.7-fold and
FT increases affinity for UDP-glucose 1.2-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 151
FT /note="T->A: Decreases affinity for phloretin 2-fold and
FT affinity for UDP-glucose 4.9-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 198
FT /note="F->A: Decreases affinity for phloretin 6.4-fold and
FT increases affinity for UDP-glucose 1.4-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 382
FT /note="D->E: Decreases affinity for phloretin 2.8-fold and
FT affinity for UDP-glucose 1.2-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 383
FT /note="Q->A: Decreases affinity for phloretin 3.5-fold and
FT affinity for UDP-glucose 3.6-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT MUTAGEN 383
FT /note="Q->H: Decreases affinity for phloretin 3.7-fold and
FT affinity for UDP-glucose 2.1-fold."
FT /evidence="ECO:0000269|PubMed:32699169"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:7CYW"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6LLG"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:7CYW"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:7CYW"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:7CYW"
FT HELIX 443..454
FT /evidence="ECO:0007829|PDB:7CYW"
SQ SEQUENCE 457 AA; 50375 MW; E2AB805302B0F9CD CRC64;
MMGDLTTSFP ATTLTTNDQP HVVVCSGAGM GHLTPFLNLA SALSSAPYNC KVTLLIVIPL
ITDAESHHIS SFFSSHPTIH RLDFHVNLPA PKPNVDPFFL RYKSISDSAH RLPVHLSALS
PPISAVFSDF LFTQGLNTTL PHLPNYTFTT TSARFFTLMS YVPHLAKSSS SSPVEIPGLE
PFPTDNIPPP FFNPEHIFTS FTISNAKYFS LSKGILVNTF DSFEPETLSA LNSGDTLSDL
PPVIPIGPLN ELEHNKQEEL LPWLDQQPEK SVLYVSFGNR TAMSSDQILE LGMGLERSDC
RFIWVVKTSK IDKDDKSELR KLFGEELYLK LSEKGKLVKW VNQTEILGHT AVGGFLSHCG
WNSVMEAARR GVPILAWPQH GDQRENAWVV EKAGLGVWER EWASGIQAAI VEKVKMIMGN
NDLRKSAMKV GEEAKRACDV GGSSATALMN IIGSLKR
