UGPA_SOLTU
ID UGPA_SOLTU Reviewed; 477 AA.
AC P19595; Q43192; Q5F1U8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
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 Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT ALA-2.
RC TISSUE=Tuber;
RX PubMed=2229031; DOI=10.1093/oxfordjournals.jbchem.a123200;
RA Katsube T., Kazuta Y., Mori H., Nakano K., Tanizawa K., Fukui T.;
RT "UDP-glucose pyrophosphorylase from potato tuber: cDNA cloning and
RT sequencing.";
RL J. Biochem. 108:321-326(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Lemhi Russet;
RX PubMed=9074509; DOI=10.1016/s0378-1119(96)00724-x;
RA Borovkov A.Y., McClean P.E., Secor G.A.;
RT "Organization and transcription of the gene encoding potato UDP-glucose
RT pyrophosphorylase.";
RL Gene 186:293-297(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RA Spychalla J.P., Bevan M.W.;
RT "UDP-glucose pyrophosphorylase of potato tuber: cDNA sequence, transgenic
RT tuber-specific inhibition and control of post-harvest sugar metabolism.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. ND860-2, and cv. Russet Burbank-1;
RX PubMed=15384406; DOI=10.1016/j.jplph.2004.04.006;
RA Sowokinos J.R., Vigdorovich V., Abrahamsen M.;
RT "Molecular cloning and sequence variation of UDP-glucose pyrophosphorylase
RT cDNAs from potatoes sensitive and resistant to cold sweetening.";
RL J. Plant Physiol. 161:947-955(2004).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Tuber;
RX PubMed=2558111; DOI=10.1093/oxfordjournals.jbchem.a122886;
RA Nakano K., Omura Y., Tagaya M., Fukui T.;
RT "UDP-glucose pyrophosphorylase from potato tuber: purification and
RT characterization.";
RL J. Biochem. 106:528-532(1989).
RN [6]
RP MUTAGENESIS OF LYSINE RESIDUES.
RX PubMed=1909568; DOI=10.1021/bi00099a008;
RA Katsube T., Kazuta Y., Tanizawa K., Fukui T.;
RT "Expression in Escherichia coli of UDP-glucose pyrophosphorylase cDNA from
RT potato tuber and functional assessment of the five lysyl residues located
RT at the substrate-binding site.";
RL Biochemistry 30:8546-8551(1991).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibition by uncomplexed, free UTP.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; D00667; BAA00570.1; -; mRNA.
DR EMBL; U20345; AAB71613.1; -; Genomic_DNA.
DR EMBL; Z18924; CAA79357.1; -; mRNA.
DR EMBL; AY082618; AAL99193.1; -; mRNA.
DR EMBL; AY082619; AAL99194.1; -; mRNA.
DR PIR; JX0128; XNPOU.
DR PIR; S31431; S31431.
DR AlphaFoldDB; P19595; -.
DR SMR; P19595; -.
DR STRING; 4113.PGSC0003DMT400034699; -.
DR iPTMnet; P19595; -.
DR PRIDE; P19595; -.
DR eggNOG; KOG2638; Eukaryota.
DR SABIO-RK; P19595; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P19595; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Magnesium;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2229031"
FT CHAIN 2..477
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000185762"
FT BINDING 92..95
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 106
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 169
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 198
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 227..229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 229
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 367
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:0000269|PubMed:2229031"
FT VARIANT 5
FT /note="T -> A (in strain: cv. Desiree, cv. ND860-2 and cv.
FT Russet Burbank-1)"
FT VARIANT 30
FT /note="E -> D (in strain: cv. Desiree, cv. ND860-2 and cv.
FT Russet Burbank-1)"
FT VARIANT 82
FT /note="K -> N (in strain: cv. Desiree, cv. ND860-2 and cv.
FT Russet Burbank-1)"
FT VARIANT 445
FT /note="K -> E (in strain: cv. Desiree, cv. ND860-2 and cv.
FT Russet Burbank-1)"
FT VARIANT 450
FT /note="V -> I (in strain: cv. Desiree, cv. ND860-2 and cv.
FT Russet Burbank-1)"
FT MUTAGEN 263
FT /note="K->Q: Significant decreased Vmax values."
FT /evidence="ECO:0000269|PubMed:1909568"
FT MUTAGEN 329
FT /note="K->Q: Increased Km, Vmax like wild-type."
FT /evidence="ECO:0000269|PubMed:1909568"
FT MUTAGEN 367
FT /note="K->Q: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:1909568"
FT MUTAGEN 409
FT /note="K->Q: Activity almost like wild-type."
FT /evidence="ECO:0000269|PubMed:1909568"
FT MUTAGEN 410
FT /note="K->Q: Activity almost like wild-type."
FT /evidence="ECO:0000269|PubMed:1909568"
FT CONFLICT 2
FT /note="A -> V (in Ref. 2; AAB71613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 51874 MW; 060E8D08AAE22709 CRC64;
MATATTLSPA DAEKLNNLKS AVAGLNQISE NEKSGFINLV GRYLSGEAQH IDWSKIQTPT
DEVVVPYDKL APLSEDPAET KKLLDKLVVL KLNGGLGTTM GCTGPKSVIE VRNGLTFLDL
IVKQIEALNA KFGCSVPLLL MNSFNTHDDT LKIVEKYANS NIDIHTFNQS QYPRLVTEDF
APLPCKGNSG KDGWYPPGHG DVFPSLMNSG KLDALLAKGK EYVFVANSDN LGAIVDLKIL
NHLILNKNEY CMEVTPKTLA DVKGGTLISY EGKVQLLEIA QVPDEHVNEF KSIEKFKIFN
TNNLWVNLSA IKRLVEADAL KMEIIPNPKE VDGVKVLQLE TAAGAAIKFF DRAIGANVPR
SRFLPVKATS DLLLVQSDLY TLTDEGYVIR NPARSNPSNP SIELGPEFKK VANFLGRFKS
IPSIIDLDSL KVTGDVWFGS GVTLKGKVTV AAKSGVKLEI PDGAVIANKD INGPEDI
