UGPA1_YEAST
ID UGPA1_YEAST Reviewed; 499 AA.
AC P32861; D6VXQ0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000305};
DE EC=2.7.7.9 {ECO:0000269|PubMed:7588797};
DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000303|PubMed:7588797};
DE Short=UDPGP {ECO:0000303|PubMed:7588797};
DE Short=UGPase {ECO:0000303|PubMed:7588797};
GN Name=UGP1 {ECO:0000303|PubMed:7588797}; OrderedLocusNames=YKL035W;
GN ORFNames=YKL248;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1481573; DOI=10.1002/yea.320081108;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT reveals five new open reading frames, including a zinc finger protein and a
RT homolog of the UDP-glucose pyrophosphorylase from potato.";
RL Yeast 8:977-986(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7588797; DOI=10.1111/j.1432-1033.1995.520_2.x;
RA Daran J.M., Dallies N., Thines-Sempoux D., Paquet V., Francois J.;
RT "Genetic and biochemical characterization of the UGP1 gene encoding the
RT UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 233:520-530(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-19 AND SER-21, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP METHYLATION AT ARG-369.
RX PubMed=23865587; DOI=10.1021/pr400556c;
RA Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL J. Proteome Res. 12:3884-3899(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 12-499, SUBUNIT, OLIGOMERIZATION
RP REGION, AND PROBABLE MAGNESIUM-BINDING SITES.
RX PubMed=17010990; DOI=10.1016/j.jmb.2006.08.079;
RA Roeben A., Plitzko J.M., Korner R., Bottcher U.M., Siegers K.,
RA Hayer-Hartl M., Bracher A.;
RT "Structural basis for subunit assembly in UDP-glucose pyrophosphorylase
RT from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 364:551-560(2006).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways. {ECO:0000269|PubMed:7588797}.
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; Evidence={ECO:0000269|PubMed:7588797};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:17010990}.
CC -!- INTERACTION:
CC P32861; P31374: PSK1; NbExp=3; IntAct=EBI-19987, EBI-9442;
CC P32861; Q08217: PSK2; NbExp=3; IntAct=EBI-19987, EBI-9839;
CC -!- MISCELLANEOUS: Present with 17200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; X69584; CAA49303.1; -; Genomic_DNA.
DR EMBL; Z28035; CAA81872.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09120.1; -; Genomic_DNA.
DR PIR; S30007; S30007.
DR RefSeq; NP_012889.3; NM_001179601.3.
DR PDB; 2I5K; X-ray; 3.10 A; A/B=12-499.
DR PDBsum; 2I5K; -.
DR AlphaFoldDB; P32861; -.
DR SMR; P32861; -.
DR BioGRID; 34096; 177.
DR DIP; DIP-4534N; -.
DR IntAct; P32861; 42.
DR MINT; P32861; -.
DR STRING; 4932.YKL035W; -.
DR iPTMnet; P32861; -.
DR MaxQB; P32861; -.
DR PaxDb; P32861; -.
DR PRIDE; P32861; -.
DR EnsemblFungi; YKL035W_mRNA; YKL035W; YKL035W.
DR GeneID; 853830; -.
DR KEGG; sce:YKL035W; -.
DR SGD; S000001518; UGP1.
DR VEuPathDB; FungiDB:YKL035W; -.
DR eggNOG; KOG2638; Eukaryota.
DR GeneTree; ENSGT00940000153464; -.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; P32861; -.
DR OMA; TNNLWAK; -.
DR BioCyc; MetaCyc:YKL035W-MON; -.
DR BioCyc; YEAST:YKL035W-MON; -.
DR BRENDA; 2.7.7.9; 984.
DR Reactome; R-SCE-173599; Formation of the active cofactor, UDP-glucuronate.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR ChiTaRS; UGP1; yeast.
DR EvolutionaryTrace; P32861; -.
DR PRO; PR:P32861; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32861; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070569; F:uridylyltransferase activity; IDA:SGD.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IMP:SGD.
DR GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IMP:SGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IMP:SGD.
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 3D-structure; Acetylation; Magnesium; Metal-binding; Methylation;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..499
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000185765"
FT REGION 448..499
FT /note="Oligomerization"
FT ACT_SITE 388
FT /evidence="ECO:0000305"
FT BINDING 109..112
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 111..112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 123
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 186
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 215
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 244..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 246
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 388
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 369
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:23865587"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2I5K"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2I5K"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:2I5K"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2I5K"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2I5K"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 446..457
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 462..470
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2I5K"
FT STRAND 484..498
FT /evidence="ECO:0007829|PDB:2I5K"
SQ SEQUENCE 499 AA; 55988 MW; 9B9F4BED885E004D CRC64;
MSTKKHTKTH STYAFESNTN SVAASQMRNA LNKLADSSKL DDAARAKFEN ELDSFFTLFR
RYLVEKSSRT TLEWDKIKSP NPDEVVKYEI ISQQPENVSN LSKLAVLKLN GGLGTSMGCV
GPKSVIEVRE GNTFLDLSVR QIEYLNRQYD SDVPLLLMNS FNTDKDTEHL IKKYSANRIR
IRSFNQSRFP RVYKDSLLPV PTEYDSPLDA WYPPGHGDLF ESLHVSGELD ALIAQGREIL
FVSNGDNLGA TVDLKILNHM IETGAEYIME LTDKTRADVK GGTLISYDGQ VRLLEVAQVP
KEHIDEFKNI RKFTNFNTNN LWINLKAVKR LIESSNLEME IIPNQKTITR DGHEINVLQL
ETACGAAIRH FDGAHGVVVP RSRFLPVKTC SDLLLVKSDL FRLEHGSLKL DPSRFGPNPL
IKLGSHFKKV SGFNARIPHI PKIVELDHLT ITGNVFLGKD VTLRGTVIIV CSDGHKIDIP
NGSILENVVV TGNLQILEH
