CGT_ORYSJ
ID CGT_ORYSJ Reviewed; 471 AA.
AC Q5VMI0; B9FST5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=UDP-glycosyltransferase CGT {ECO:0000305};
DE EC=2.4.1.360 {ECO:0000250|UniProtKB:C3W7B0};
DE AltName: Full=UDP-glucose:2-hydroxyflavanone C-glucosyltransferase {ECO:0000305};
DE Short=OsCGT {ECO:0000305};
GN Name=CGT {ECO:0000305};
GN OrderedLocusNames=Os06g0288300 {ECO:0000312|EMBL:BAS97297.1},
GN LOC_Os06g18010 {ECO:0000305};
GN ORFNames=B1197G05.8 {ECO:0000312|EMBL:BAD69345.1},
GN b29O05.13 {ECO:0000312|EMBL:ABE02743.1},
GN OsJ_21017 {ECO:0000312|EMBL:EEE65546.1},
GN P0649C11.32 {ECO:0000312|EMBL:BAD69117.1};
OS Oryza sativa subsp. japonica (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=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17249423; DOI=10.1094/mpmi-20-0063;
RA Zhou B., Dolan M., Sakai H., Wang G.L.;
RT "The genomic dynamics and evolutionary mechanism of the Pi2/9 locus in
RT rice.";
RL Mol. Plant Microbe Interact. 20:63-71(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the c-
CC glucosylation of 2-hydroxyflavanones. {ECO:0000250|UniProtKB:C3W7B0}.
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:0000250|UniProtKB:C3W7B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000250|UniProtKB:C3W7B0};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE65546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ454158; ABE02743.1; -; Genomic_DNA.
DR EMBL; AP005659; BAD69117.1; -; Genomic_DNA.
DR EMBL; AP006584; BAD69345.1; -; Genomic_DNA.
DR EMBL; AP008212; BAH93454.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97297.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65546.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015641684.1; XM_015786198.1.
DR AlphaFoldDB; Q5VMI0; -.
DR SMR; Q5VMI0; -.
DR STRING; 4530.OS06T0288300-01; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q5VMI0; -.
DR PRIDE; Q5VMI0; -.
DR EnsemblPlants; Os06t0288300-01; Os06t0288300-01; Os06g0288300.
DR GeneID; 9266253; -.
DR Gramene; Os06t0288300-01; Os06t0288300-01; Os06g0288300.
DR KEGG; osa:9266253; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_1_1; -.
DR InParanoid; Q5VMI0; -.
DR OMA; WEGEEGM; -.
DR OrthoDB; 508327at2759; -.
DR BRENDA; 2.4.1.360; 8948.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS: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 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..471
FT /note="UDP-glycosyltransferase CGT"
FT /id="PRO_0000436257"
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"
SQ SEQUENCE 471 AA; 49457 MW; 577358DD10F99A1B CRC64;
MPSSGDAAGR RPHVVLIPSA GMGHLVPFGR LAVALSSGHG CDVSLVTVLP TVSTAESKHL
DALFDAFPAV RRLDFELAPF DASEFPSADP FFLRFEAMRR SAPLLGPLLT GAGASALATD
IALTSVVIPV AKEQGLPCHI LFTASAAMLS LCAYFPTYLD ANAGDGGGVG DVDIPGVYRI
PKASIPQALH DPNHLFTRQF VANGRSLTSA AGILVNTFDA LEPEAVAALQ QGKVASGFPP
VFAVGPLLPA SNQAKDPQAN YMEWLDAQPA RSVVYVSFGS RKAISGEQLR ELAAGLETSG
HRFLWVVKST VVDRDDAAEL GELLGEGFLK RVEKRGLVTK AWVDQEEVLK HESVALFVSH
CGWNSVTEAA ASGVPVLALP RFGDQRVNSG VVARAGLGVW ADTWSWEGEA GVIGAEEISE
KVKAAMADEA LRRKAASLAK AAAKAVAGGG SSHRCLVEFA RLCQGGTCRT N
