UGPA_MUSAC
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 03-AUG-2022, entry version 72.
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 PRIDE; 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; 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..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