ID   UGPA_HORVU              Reviewed;         473 AA.
AC   Q43772;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE            Short=UGPase;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bomi; TISSUE=Endosperm, and Leaf;
RX   PubMed=8666250; DOI=10.1016/0378-1119(95)00873-x;
RA   Eimert K., Villand P., Kilian A., Kleczkowski L.A.;
RT   "Cloning and characterization of several cDNAs for UDP-glucose
RT   pyrophosphorylase from barley (Hordeum vulgare) tissues.";
RL   Gene 170:227-232(1996).
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways.
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.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; X91347; CAA62689.1; -; mRNA.
DR   PIR; JC4785; JC4785.
DR   AlphaFoldDB; Q43772; -.
DR   SMR; Q43772; -.
DR   PRIDE; Q43772; -.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0418770.1; HORVU.MOREX.r2.5HG0418770.1; HORVU.MOREX.r2.5HG0418770.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0418770.1.mrna1; HORVU.MOREX.r2.5HG0418770.1.mrna1; HORVU.MOREX.r2.5HG0418770.1.
DR   Gramene; HORVU.MOREX.r2.5HG0418770.1; HORVU.MOREX.r2.5HG0418770.1; HORVU.MOREX.r2.5HG0418770.
DR   Gramene; HORVU.MOREX.r2.5HG0418770.1.mrna1; HORVU.MOREX.r2.5HG0418770.1.mrna1; HORVU.MOREX.r2.5HG0418770.1.
DR   BRENDA; 2.7.7.9; 2687.
DR   SABIO-RK; Q43772; -.
DR   ExpressionAtlas; Q43772; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
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   Cytoplasm; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..473
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000185759"
FT   BINDING         89..92
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         91..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         103
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         166
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         195
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         224..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         226
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         364
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   473 AA;  51644 MW;  1155AA1C90E748FF CRC64;
     MAAAAVAADS KIDGLRDAVA KLGEISENEK AGFISLVSRY LSGEAEQIEW SKIQTPTDEV
     VVPYDTLAPP PEDLDAMKAL LDKLVVLKLN GGLGTTMGCT GPKSVIEVRN GFTFLDLIVI
     QIESLNKKYG CSVPLLLMNS FNTHDDTQKI VEKYSNSNIE IHTFNQSQYP RIVTEDFLPL
     PSKGQTGKDG WYPPGHGDVF PSLNNSGKLD TLLSQGKEYV FVANSDNLGA IVDIKILNHL
     IHNQNEYCME VTPKTLADVK GGTLISYEGR VQLLEIAQVP DEHVDEFKSI EKFKIFNTNN
     LWVNLKAIKR LVDAEALKME IIPNPKEVDG VKVLQLETAA GAAIRFFEKA IGINVPRSRF
     LPVKATSDLL LVQSDLYTLV DGYVIRNPAR VKPSNPSIEL GPEFKKVANF LARFKSIPSI
     VELDSLKVSG DVSFGSGVVL KGNVTIAAKA GVKLEIPDGA VLENKDINGP EDI