ID   UGPA1_ARATH             Reviewed;         470 AA.
AC   P57751; Q3E9G5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 1.
DT   04-NOV-2026, entry version 159.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 1;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase 1;
DE            Short=AtUGP1 {ECO:0000303|PubMed:20435647};
DE            Short=UDPGP 1;
DE            Short=UGPase 1;
GN   Name=UGP1 {ECO:0000303|PubMed:19366709}; OrderedLocusNames=At5g17310;
GN   ORFNames=MKP11.16;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SUCROSE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19366709; DOI=10.1093/pcp/pcp052;
RA   Meng M., Geisler M., Johansson H., Harholt J., Scheller H.V.,
RA   Mellerowicz E.J., Kleczkowski L.A.;
RT   "UDP-glucose pyrophosphorylase is not rate limiting, but is essential in
RT   Arabidopsis.";
RL   Plant Cell Physiol. 50:998-1011(2009).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20435647; DOI=10.1093/pcp/pcq057;
RA   Park J.I., Ishimizu T., Suwabe K., Sudo K., Masuko H., Hakozaki H.,
RA   Nou I.S., Suzuki G., Watanabe M.;
RT   "UDP-glucose pyrophosphorylase is rate limiting in vegetative and
RT   reproductive phases in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 51:981-996(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=23438466; DOI=10.1021/pr3010887;
RA   Chivasa S., Tome D.F., Slabas A.R.;
RT   "UDP-glucose pyrophosphorylase is a novel plant cell death regulator.";
RL   J. Proteome Res. 12:1743-1753(2013).
CC   -!- FUNCTION: Converts glucose 1-phosphate to UDP-glucose, which is the
CC       major glycosyl donor for polysaccharides. Acts redundantly with UGP2
CC       and is essential for the synthesis of sucrose, starch and cell wall,
CC       and callose deposition (PubMed:19366709, PubMed:20435647). Involved in
CC       the regulation of the programmed cell death (PCD) induced by the fungal
CC       toxin fumonisin B1 (FB1) (PubMed:23438466).
CC       {ECO:0000269|PubMed:19366709, ECO:0000269|PubMed:20435647,
CC       ECO:0000269|PubMed:23438466}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + UTP + H(+) = UDP-alpha-D-glucose
CC         + diphosphate; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:58885; EC=2.7.7.9;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P57751-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC       stems, flowers and siliques. {ECO:0000269|PubMed:19366709}.
CC   -!- INDUCTION: By sucrose. {ECO:0000269|PubMed:19366709}.
CC   -!- DISRUPTION PHENOTYPE: Reduced number of seeds (PubMed:19366709). The
CC       double mutants upg1 and ugp2 display severe growth defects and male
CC       sterility due to the absence of callose deposition around microspores
CC       (PubMed:20435647). {ECO:0000269|PubMed:19366709,
CC       ECO:0000269|PubMed:20435647}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; AB005238; BAB10518.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92412.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7052584.1; -; Genomic_DNA.
DR   EMBL; AF360244; AAK25954.1; -; mRNA.
DR   EMBL; AY040042; AAK64100.1; -; mRNA.
DR   EMBL; AF361816; AAK32829.1; -; mRNA.
DR   AlphaFoldDB; P57751; -.
DR   SMR; P57751; -.
DR   BioGRID; 16872; 16.
DR   FunCoup; P57751; 3003.
DR   IntAct; P57751; 1.
DR   STRING; 3702.P57751; -.
DR   iPTMnet; P57751; -.
DR   PaxDb; 3702-P57751; -.
DR   ProteomicsDB; 245265; -. [P57751-1]
DR   KEGG; ath:AT5G17310; -.
DR   Araport; AT5G17310; -.
DR   TAIR; AT5G17310; UGP2.
DR   eggNOG; KOG2638; Eukaryota.
DR   InParanoid; P57751; -.
DR   OMA; AACNVNI; -.
DR   PhylomeDB; P57751; -.
DR   BioCyc; ARA:AT5G17310-MONOMER; -.
DR   BRENDA; 2.7.7.9; 399.
DR   PRO; PR:P57751; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Proteomes; UP001984100; Chromosome 5.
DR   ExpressionAtlas; P57751; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0052543; P:callose deposition in cell wall; IGI:TAIR.
DR   GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR   GO; GO:0009555; P:pollen development; IGI:TAIR.
DR   GO; GO:0006011; P:UDP-alpha-D-glucose metabolic process; IBA:GO_Central.
DR   CDD; cd00897; UGPase_euk; 1.
DR   FunFam; 2.160.10.10:FF:000001; UTP--glucose-1-phosphate uridylyltransferase; 1.
DR   FunFam; 3.90.550.10:FF:000073; UTP--glucose-1-phosphate uridylyltransferase; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR002618; UDPGP_fam.
DR   InterPro; IPR016267; UDPGP_trans.
DR   PANTHER; PTHR43511; -; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   PIRSF; PIRSF000806; UDPGP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   CHAIN           2..470
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase 1"
FT                   /id="PRO_0000185756"
FT   BINDING         86..89
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         88..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         100
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         163
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         192
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         221..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         223
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         361
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   470 AA;  51920 MW;  488C4A034DC73AE8 CRC64;
     MAATATEKLP QLKSAVDGLT EMSENEKSGF INLVSRYLSG EAQHIEWSKI QTPTDEIVVP
     YDKMANVSED ASETKYLLDK LVVLKLNGGL GTTMGCTGPK SVIEVRDGLT FLDLIVIQIE
     NLNNKYNCKV PLVLMNSFNT HDDTQKIVEK YTKSNVDIHT FNQSKYPRVV ADEFVPWPSK
     GKTDKDGWYP PGHGDVFPSL MNSGKLDAFL SQGKEYVFIA NSDNLGAIVD LKILKHLIQN
     KNEYCMEVTP KTLADVKGGT LISYEGKVQL LEIAQVPDEH VNEFKSIEKF KIFNTNNLWV
     NLKAIKKLVE ADALKMEIIP NPKEVDGVKV LQLETAAGAA IRFFDNAIGV NVPRSRFLPV
     KATSDLLLVQ SDLYTLVDGF VTRNKARTNP TNPAIELGPE FKKVASFLSR FKSIPSIVEL
     DSLKVSGDVW FGSGVVLKGK VTVKANAGTK LEIPDNAVLE NKDINGPEDL
//