CGT_ORYSI
ID CGT_ORYSI Reviewed; 471 AA.
AC C3W7B0; A1XFD9;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=UDP-glycosyltransferase CGT {ECO:0000305};
DE EC=2.4.1.360 {ECO:0000269|PubMed:19411659};
DE AltName: Full=UDP-glucose:2-hydroxyflavanone C-glucosyltransferase {ECO:0000303|PubMed:19411659};
DE Short=OsCGT {ECO:0000303|PubMed:19411659};
GN Name=CGT {ECO:0000303|PubMed:19411659};
GN ORFNames=Pi2_C101A51.16 {ECO:0000312|EMBL:ABC94602.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17073304; DOI=10.1094/mpmi-19-1216;
RA Zhou B., Qu S., Liu G., Dolan M., Sakai H., Lu G., Bellizzi M., Wang G.L.;
RT "The eight amino-acid differences within three leucine-rich repeats between
RT Pi2 and Piz-t resistance proteins determine the resistance specificity to
RT Magnaporthe grisea.";
RL Mol. Plant Microbe Interact. 19:1216-1228(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19411659; DOI=10.1074/jbc.m109.009258;
RA Brazier-Hicks M., Evans K.M., Gershater M.C., Puschmann H., Steel P.G.,
RA Edwards R.;
RT "The C-glycosylation of flavonoids in cereals.";
RL J. Biol. Chem. 284:17926-17934(2009).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the c-
CC glucosylation of 2-hydroxyflavanones. Acts preferentially on the
CC dibenzoylmethane tautomers formed in equilibrium with 2-
CC hydroxyflavanones. No activity with naringenin or naringenin chalcone.
CC {ECO:0000269|PubMed:19411659}.
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:19411659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000269|PubMed:19411659};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.5 uM for 2,5,7-trihydroxyflavanone
CC {ECO:0000269|PubMed:19411659};
CC KM=8.3 uM for 2',4',6'-trihydroxydihydrochalcone
CC {ECO:0000269|PubMed:19411659};
CC KM=2.5 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:19411659};
CC KM=4.78 uM for phoretin {ECO:0000269|PubMed:19411659};
CC KM=8.0 uM for 2,4,6-trihydroxybenzophenone
CC {ECO:0000269|PubMed:19411659};
CC Note=kcat is 0.76 sec(-1) with 2,5,7-trihydroxyflavanone as
CC substrate. kcat is 3.13 sec(-1) with 2-hydroxynaringenin as
CC substrate. kcat is 0.75 sec(-1) with 2',4',6'-
CC trihydroxydihydrochalcone as substrate. kcat is 10.84 sec(-1) with
CC phoretin as substrate. kcat is 0.11 sec(-1) with 2,4,6-
CC trihydroxybenzophenone as substrate. {ECO:0000269|PubMed:19411659};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ352453; ABC94602.1; -; Genomic_DNA.
DR EMBL; FM179712; CAQ77160.1; -; Genomic_DNA.
DR AlphaFoldDB; C3W7B0; -.
DR SMR; C3W7B0; -.
DR BioCyc; MetaCyc:MON-15871; -.
DR BRENDA; 2.4.1.360; 11590.
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..471
FT /note="UDP-glycosyltransferase CGT"
FT /id="PRO_0000436256"
FT REGION 280..281
FT /note="UDP"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 120
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 23..26
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 143
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 342..345
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 360..368
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 384..385
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT CONFLICT 325
FT /note="D -> G (in Ref. 1; ABC94602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 49431 MW; 69C515C04135E24E CRC64;
MPSSGDAAGR RPHVVLIPSA GMGHLVPFGR LAVALSSGHG CDVSLVTVLP TVSTAESKHL
DALFDAFPAV RRLDFELAPF DASEFPGADP FFLRFEAMRR SAPLLGPLLT GAGASALATD
IALTSVVIPV AKEQGLPCHI LFTASAAMLS LCAYFPTYLD ANAGGGGGVG DVDIPGVYRI
PKASIPQALH DPNHLFTRQF VANGRSLTSA AGILVNTFDA LEPEAVAALQ QGKVASGFPP
VFAVGPLLPA SNQAKDPQAN YMEWLDAQPA RSVVYVSFGS RKAISREQLR ELAAGLEGSG
HRFLWVVKST VVDRDDAAEL GELLDEGFLE RVEKRGLVTK AWVDQEEVLK HESVALFVSH
CGWNSVTEAA ASGVPVLALP RFGDQRVNSG VVARAGLGVW ADTWSWEGEA GVIGAEEISE
KVKAAMADEA LRMKAASLAE AAAKAVAGGG SSHRCLAEFA RLCQGGTCRT N
