ID   UGPA_MUSAC              Reviewed;         467 AA.
AC   Q9SDX3;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   22-FEB-2023, entry version 75.
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=UGPA;
OS   Musa acuminata (Banana) (Musa cavendishii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=4641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lim S.S.W., Pua E.C.;
RT   "Molecular cloning and characterization of UDP-glucose pyrophosphorylase in
RT   banana.";
RL   Submitted (NOV-1999) 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; AF203909; AAF19422.1; -; mRNA.
DR   AlphaFoldDB; Q9SDX3; -.
DR   SMR; Q9SDX3; -.
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; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR002618; UDPGP_fam.
DR   InterPro; IPR016267; UDPGP_trans.
DR   PANTHER; PTHR43511; -; 1.
DR   PANTHER; PTHR43511:SF4; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 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   Cytoplasm; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..467
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000185760"
FT   BINDING         83..86
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         85..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         97
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         160
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         189
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         218..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         220
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         358
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   467 AA;  51362 MW;  7EFFF37BD0B1147B CRC64;
     MADAKIAKLQ SAVAELNQIS ENEKSGFISL VSRYLSGEAE QIEWSKIQTP TDEVVVPYDT
     LSPPPEDLEA TKKLLDKLAV LKLNGGLGTT MGCTGPKSVI EVRNGFTFLD LIVIQIESLN
     KKYGCNVPLL LMNSFNTHDD TQKIVEKYAN SNIEIHTFNQ SQYPRLVMED FQPLPSKGHA
     GKDGWYPPGH GDVFPSLMNS GKLDALLSQG KEYVFIANSD NLGAIVDIKI LNHLINNQNE
     YCMEVTPKTL ADVKGGTLIS YEGRVQLLEI AQVPDAHVNE FKSIEKFKIF NTNNLWVNLK
     AIKRLVEADA LKMEIIPNPK EVDGVKVLQL ETAAGAAIRF FDHAIGINVP RSRFLPVKAT
     SDLLLVQSDL YMLVDGFVIR NKARTNPSNP SIELGPEFKK VANFLSRFKS IPSIVELDSL
     KVSGDVWFGE GVVLKGNVSI AAKSGVKLEI SDGAVLENKV INGPEDI
//