UGPA1_ARATH
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 03-AUG-2022, entry version 139.
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 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 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 [5]
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 [6]
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 + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; 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; AF360244; AAK25954.1; -; mRNA.
DR EMBL; AY040042; AAK64100.1; -; mRNA.
DR EMBL; AF361816; AAK32829.1; -; mRNA.
DR RefSeq; NP_197233.1; NM_121737.4. [P57751-1]
DR AlphaFoldDB; P57751; -.
DR SMR; P57751; -.
DR BioGRID; 16872; 16.
DR STRING; 3702.AT5G17310.2; -.
DR iPTMnet; P57751; -.
DR PaxDb; P57751; -.
DR PRIDE; P57751; -.
DR ProteomicsDB; 245265; -. [P57751-1]
DR EnsemblPlants; AT5G17310.2; AT5G17310.2; AT5G17310. [P57751-1]
DR GeneID; 831596; -.
DR Gramene; AT5G17310.2; AT5G17310.2; AT5G17310. [P57751-1]
DR KEGG; ath:AT5G17310; -.
DR Araport; AT5G17310; -.
DR TAIR; locus:2167220; AT5G17310.
DR eggNOG; KOG2638; Eukaryota.
DR InParanoid; P57751; -.
DR OMA; MHFKSAT; -.
DR PhylomeDB; P57751; -.
DR BioCyc; ARA:AT5G17310-MON; -.
DR BRENDA; 2.7.7.9; 399.
DR PRO; PR:P57751; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P57751; baseline and differential.
DR Genevisible; P57751; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central.
DR CDD; cd00897; UGPase_euk; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR002618; UDPGP_fam.
DR InterPro; IPR016267; UDPGP_trans.
DR PANTHER; PTHR43511; PTHR43511; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 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
