ID   UGPA_ASTPN              Reviewed;         471 AA.
AC   Q9LKG7;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
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;
GN   Name=UGP;
OS   Astragalus penduliflorus (Mountain lentil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Galegeae; Astragalus.
OX   NCBI_TaxID=158323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RA   Wu X.J., Liu D., Hu Z.B.;
RT   "cDNA cloning and expression in E.coli of UDP-glucose pyrophosphorylase of
RT   Astragalus membranaceus.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; AF281081; AAF86501.1; -; mRNA.
DR   AlphaFoldDB; Q9LKG7; -.
DR   SMR; Q9LKG7; -.
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..471
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000185758"
FT   BINDING         87..90
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         101
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         164
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         193
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         222..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         224
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         362
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   471 AA;  51550 MW;  127CD3037FA17B53 CRC64;
     MATATATDRL SNLKSSVAGL NQISENEKSG FINLVARYLS GEAQHVEWSK IQTPTDEVVV
     PYDTLAPTPD GSLEIKNLLD KLVVLKLNGG LGTTMGCTGP KSVIEVRDGL TFLDLIVIQI
     ENLNSKYGSN VPLLLMNSFN THDDTQTIVE KYQNSNIEIH TFNQSQYPRL VVDDFLPLPS
     KGRTDKDGWY PPGHGSMFPS LSNSGKLDAL ISQGKEYVFV ANSDNLGAIV DLKILNHLVA
     HKNEYCMEVT PKTLADVKGG TLISYEGRVQ LLEIAQVPDE HVGEFKSIEK FKIFNTNNLW
     VNLKAIKRLV EADALKMEII PNPKEVDGVK VLQLETAAGA AIRFFDKAIG INVPRSRFLP
     VKATSDLLLV QSDLYTVENG SVIRNKARTN PENPSIELGP EFKKVSNFLG RFKSIPSIVE
     LDSLKVVGDV WFGTGVILKG KVSIVAKSGV KVEIPDGAVI ANKEINGPKD L