ID   UGPA2_YEAST             Reviewed;         493 AA.
AC   P38709; D3DKQ1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE            Short=UGPase;
GN   OrderedLocusNames=YHL012W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
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   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; U11582; AAB65065.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06674.1; -; Genomic_DNA.
DR   PIR; S46826; S46826.
DR   RefSeq; NP_011851.1; NM_001179092.1.
DR   AlphaFoldDB; P38709; -.
DR   SMR; P38709; -.
DR   BioGRID; 36411; 54.
DR   IntAct; P38709; 1.
DR   STRING; 4932.YHL012W; -.
DR   PaxDb; P38709; -.
DR   PRIDE; P38709; -.
DR   TopDownProteomics; P38709; -.
DR   EnsemblFungi; YHL012W_mRNA; YHL012W; YHL012W.
DR   GeneID; 856374; -.
DR   KEGG; sce:YHL012W; -.
DR   SGD; S000001004; YHL012W.
DR   VEuPathDB; FungiDB:YHL012W; -.
DR   eggNOG; KOG2638; Eukaryota.
DR   GeneTree; ENSGT00940000153464; -.
DR   HOGENOM; CLU_023632_0_0_1; -.
DR   InParanoid; P38709; -.
DR   OMA; NESASTC; -.
DR   PRO; PR:P38709; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38709; protein.
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   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   3: Inferred from homology;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..493
FT                   /note="Probable UTP--glucose-1-phosphate
FT                   uridylyltransferase"
FT                   /id="PRO_0000185766"
FT   BINDING         105..108
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         181
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         211
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         240..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         242
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   493 AA;  56000 MW;  EFC7FA4A8F681DE2 CRC64;
     MTVFSGVNKI EFEGTFEGIG KDVVMSQMIR ALQKHFPSIR DKNYEFSLFL HIFQRYVLEN
     TSITHDLVCD KIRLPIIDEV VELDDIKNYG LLEGKLLSKL AILKLTGKAN PIIGKESPLF
     EVKNGMSSLD VIVRQTQNLN VRYNSDVPLI FMTSLETESQ VSNFLEEHYS SSKVRWKTVV
     QSSFPQIDKD RLLPIDLQIN SHENDFWYPC GTGNLTDTLY FSGELDKLIA QGKEILFVSN
     VDNLGATGDL NILNFIINEK IEYLVEVVER TANVSNTGVL ATYKGKLRSV YYNCLSNESA
     STCRIVNTNN IWIDLKKLKV LIESNSLNLP IHSSESKITH KNEEIECLQF KTQLVDCIAF
     FPNSRVLKVS RDRFLPLRTC KDLFLLKSTL YDLDSNGTFN LYPLKFGLLP SIDLGDEFAT
     YETFKIGVPD IPNILELEHL TVMGNVFFGR NITLKGTVII ICDENDVITV PDGSILENVT
     IWHKSQLEDM NGY