U75C1_ARATH
ID U75C1_ARATH Reviewed; 456 AA.
AC Q0WW21; O23270; Q8RY86;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=UDP-glycosyltransferase 75C1;
DE EC=2.4.1.-;
DE AltName: Full=Anthocyanin 5-O-glucosyltransferase;
DE AltName: Full=UDP glucose:anthocyanin 5-O-glucosyltransferase;
GN Name=UGT75C1; OrderedLocusNames=At4g14090; ORFNames=dl3090c, Z97335.19;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, AND INDUCTION BY PAP1.
RX PubMed=15807784; DOI=10.1111/j.1365-313x.2005.02371.x;
RA Tohge T., Nishiyama Y., Hirai M.Y., Yano M., Nakajima J., Awazuhara M.,
RA Inoue E., Takahashi H., Goodenowe D.B., Kitayama M., Noji M., Yamazaki M.,
RA Saito K.;
RT "Functional genomics by integrated analysis of metabolome and transcriptome
RT of Arabidopsis plants over-expressing an MYB transcription factor.";
RL Plant J. 42:218-235(2005).
RN [8]
RP FUNCTION.
RX PubMed=20085894; DOI=10.1093/mp/ssp071;
RA Pourcel L., Irani N.G., Lu Y., Riedl K., Schwartz S., Grotewold E.;
RT "The formation of anthocyanic vacuolar inclusions in Arabidopsis thaliana
RT and implications for the sequestration of anthocyanin pigments.";
RL Mol. Plant 3:78-90(2010).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Catalyzes the glycosylation of anthocyanins from UDP-glucose.
CC {ECO:0000269|PubMed:15807784, ECO:0000269|PubMed:20085894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5-hydroxy anthocyanidin + UDP-alpha-D-glucose = an
CC anthocyanin 5-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56320,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140277, ChEBI:CHEBI:140278;
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC -!- INDUCTION: By PAP1. {ECO:0000269|PubMed:15807784}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL69494.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z97335; CAB10189.1; -; Genomic_DNA.
DR EMBL; AL161538; CAB78452.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83370.1; -; Genomic_DNA.
DR EMBL; AY062589; AAL32667.1; -; mRNA.
DR EMBL; AY074526; AAL69494.1; ALT_INIT; mRNA.
DR EMBL; AY114654; AAM47973.1; -; mRNA.
DR EMBL; AY133752; AAM91686.1; -; mRNA.
DR EMBL; AK226538; BAE98677.1; -; mRNA.
DR PIR; C71402; C71402.
DR RefSeq; NP_193146.1; NM_117485.3.
DR AlphaFoldDB; Q0WW21; -.
DR SMR; Q0WW21; -.
DR STRING; 3702.AT4G14090.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q0WW21; -.
DR PRIDE; Q0WW21; -.
DR ProteomicsDB; 242613; -.
DR EnsemblPlants; AT4G14090.1; AT4G14090.1; AT4G14090.
DR GeneID; 827046; -.
DR Gramene; AT4G14090.1; AT4G14090.1; AT4G14090.
DR KEGG; ath:AT4G14090; -.
DR Araport; AT4G14090; -.
DR TAIR; locus:2129381; AT4G14090.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q0WW21; -.
DR OMA; HTRYMAQ; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q0WW21; -.
DR BioCyc; ARA:AT4G14090-MON; -.
DR BioCyc; MetaCyc:MON-18511; -.
DR UniPathway; UPA00009; -.
DR PRO; PR:Q0WW21; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WW21; baseline and differential.
DR Genevisible; Q0WW21; AT.
DR GO; GO:0080018; F:anthocyanin 5-O-glucosyltransferase activity; IMP:TAIR.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Glycosyltransferase; Phenylpropanoid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..456
FT /note="UDP-glycosyltransferase 75C1"
FT /id="PRO_0000285274"
FT BINDING 277
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 334..336
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 351..359
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT CONFLICT 279
FT /note="A -> D (in Ref. 5; BAE98677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50703 MW; 0754AB0D3A037E5C CRC64;
MATSVNGSHR RPHYLLVTFP AQGHINPALQ LANRLIHHGA TVTYSTAVSA HRRMGEPPST
KGLSFAWFTD GFDDGLKSFE DQKIYMSELK RCGSNALRDI IKANLDATTE TEPITGVIYS
VLVPWVSTVA REFHLPTTLL WIEPATVLDI YYYYFNTSYK HLFDVEPIKL PKLPLITTGD
LPSFLQPSKA LPSALVTLRE HIEALETESN PKILVNTFSA LEHDALTSVE KLKMIPIGPL
VSSSEGKTDL FKSSDEDYTK WLDSKLERSV IYISLGTHAD DLPEKHMEAL THGVLATNRP
FLWIVREKNP EEKKKNRFLE LIRGSDRGLV VGWCSQTAVL AHCAVGCFVT HCGWNSTLES
LESGVPVVAF PQFADQCTTA KLVEDTWRIG VKVKVGEEGD VDGEEIRRCL EKVMSGGEEA
EEMRENAEKW KAMAVDAAAE GGPSDLNLKG FVDEDE
