U71C2_ARATH
ID U71C2_ARATH Reviewed; 474 AA.
AC O82382;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UDP-glycosyltransferase 71C2;
DE EC=2.4.1.-;
GN Name=UGT71C2; OrderedLocusNames=At2g29740; ORFNames=T27A16.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:4338-4343(2001).
RN [5]
RP FUNCTION.
RX PubMed=15352060; DOI=10.1002/bit.20154;
RA Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT regioselective synthesis of diverse quercetin glucosides.";
RL Biotechnol. Bioeng. 87:623-631(2004).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19261311; DOI=10.1016/j.phytochem.2009.01.013;
RA Hansen E.H., Osmani S.A., Kristensen C., Moeller B.L., Hansen J.;
RT "Substrate specificities of family 1 UGTs gained by domain swapping.";
RL Phytochemistry 70:473-482(2009).
CC -!- FUNCTION: Possesses low quercetin 3-O-glucosyltransferase, 7-O-
CC glucosyltransferase and 3'-O-glucosyltransferase activities in vitro.
CC Glucosylates other secondary metabolites in vitro like vanillin, trans-
CC resveratrol, curumin and etoposide. {ECO:0000269|PubMed:15352060,
CC ECO:0000269|PubMed:19261311}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for trans-resveratrol {ECO:0000269|PubMed:19261311};
CC KM=0.59 mM for curcumin {ECO:0000269|PubMed:19261311};
CC KM=1.18 mM for vanillin {ECO:0000269|PubMed:19261311};
CC KM=31 mM for etoposide {ECO:0000269|PubMed:19261311};
CC Vmax=0.140 umol/min/mg enzyme towards vanillin
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.074 umol/min/mg enzyme towards curcumin
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.010 umol/min/mg enzyme towards trans-resveratrol
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.002 umol/min/mg enzyme towards etoposide
CC {ECO:0000269|PubMed:19261311};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC005496; AAC35238.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08299.1; -; Genomic_DNA.
DR EMBL; BT004155; AAO42176.1; -; mRNA.
DR EMBL; BT005489; AAO63909.1; -; mRNA.
DR PIR; A84700; A84700.
DR RefSeq; NP_180535.1; NM_128528.4.
DR AlphaFoldDB; O82382; -.
DR SMR; O82382; -.
DR STRING; 3702.AT2G29740.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; O82382; -.
DR PRIDE; O82382; -.
DR ProteomicsDB; 228674; -.
DR EnsemblPlants; AT2G29740.1; AT2G29740.1; AT2G29740.
DR GeneID; 817524; -.
DR Gramene; AT2G29740.1; AT2G29740.1; AT2G29740.
DR KEGG; ath:AT2G29740; -.
DR Araport; AT2G29740; -.
DR TAIR; locus:2060664; AT2G29740.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; O82382; -.
DR OMA; ITILHWS; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; O82382; -.
DR PRO; PR:O82382; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82382; baseline and differential.
DR Genevisible; O82382; AT.
DR GO; GO:0080045; F:quercetin 3'-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
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; Reference proteome; Transferase.
FT CHAIN 1..474
FT /note="UDP-glycosyltransferase 71C2"
FT /id="PRO_0000409054"
FT BINDING 293
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 352..354
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 369..377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 391..394
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 53185 MW; D00FD4C0425C0DDB CRC64;
MAKQQEAELI FIPFPIPGHI LATIELAKRL ISHQPSRIHT ITILHWSLPF LPQSDTIAFL
KSLIETESRI RLITLPDVQN PPPMELFVKA SESYILEYVK KMVPLVRNAL STLLSSRDES
DSVHVAGLVL DFFCVPLIDV GNEFNLPSYI FLTCSASFLG MMKYLLERNR ETKPELNRSS
DEETISVPGF VNSVPVKVLP PGLFTTESYE AWVEMAERFP EAKGILVNSF ESLERNAFDY
FDRRPDNYPP VYPIGPILCS NDRPNLDLSE RDRILKWLDD QPESSVVFLC FGSLKSLAAS
QIKEIAQALE LVGIRFLWSI RTDPKEYASP NEILPDGFMN RVMGLGLVCG WAPQVEILAH
KAIGGFVSHC GWNSILESLR FGVPIATWPM YAEQQLNAFT IVKELGLALE MRLDYVSEYG
EIVKADEIAG AVRSLMDGED VPRRKLKEIA EAGKEAVMDG GSSFVAVKRF IDGL
