MPG1_YEAST
ID MPG1_YEAST Reviewed; 361 AA.
AC P41940; D6VRU1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000303|Ref.2};
DE EC=2.7.7.13 {ECO:0000269|PubMed:9195935};
DE AltName: Full=ATP-mannose-1-phosphate guanylyltransferase {ECO:0000305};
DE AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000305};
DE AltName: Full=NDP-hexose pyrophosphorylase {ECO:0000305};
GN Name=PSA1; Synonyms=MPG1, SRB1, VIG9 {ECO:0000303|PubMed:9195935};
GN OrderedLocusNames=YDL055C;
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].
RX PubMed=8821656; DOI=10.1007/bf02221573;
RA Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.;
RT "Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1
RT N-glycosylation mutants.";
RL Curr. Genet. 29:106-113(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schultz J., Sprague G.F. Jr.;
RT "Isolation of the gene encoding mannose-1-phosphate guanyltransferase from
RT yeast.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=9195935; DOI=10.1074/jbc.272.26.16308;
RA Hashimoto H., Sakakibara A., Yamasaki M., Yoda K.;
RT "Saccharomyces cerevisiae VIG9 encodes GDP-mannose pyrophosphorylase, which
RT is essential for protein glycosylation.";
RL J. Biol. Chem. 272:16308-16314(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=11055399; DOI=10.1271/bbb.64.1937;
RA Yoda K., Kawada T., Kaibara C., Fujie A., Abe M., Hashimoto H., Shimizu J.,
RA Tomishige N., Noda Y., Yamasaki M.;
RT "Defect in cell wall integrity of the yeast Saccharomyces cerevisiae caused
RT by a mutation of the GDP-mannose pyrophosphorylase gene VIG9.";
RL Biosci. Biotechnol. Biochem. 64:1937-1941(2000).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, 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 IDENTIFICATION BY MASS SPECTROMETRY [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000269|PubMed:11055399, ECO:0000269|PubMed:9195935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000269|PubMed:9195935};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000269|PubMed:9195935}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9195935}.
CC -!- MISCELLANEOUS: Present with 97100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; U19608; AAC49289.1; -; Genomic_DNA.
DR EMBL; U24437; AAA69677.1; -; Genomic_DNA.
DR EMBL; Z74103; CAA98617.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11801.1; -; Genomic_DNA.
DR PIR; S67590; S67590.
DR RefSeq; NP_010228.1; NM_001180114.1.
DR AlphaFoldDB; P41940; -.
DR SMR; P41940; -.
DR BioGRID; 32003; 186.
DR DIP; DIP-4322N; -.
DR IntAct; P41940; 488.
DR MINT; P41940; -.
DR STRING; 4932.YDL055C; -.
DR iPTMnet; P41940; -.
DR MaxQB; P41940; -.
DR PaxDb; P41940; -.
DR PRIDE; P41940; -.
DR TopDownProteomics; P41940; -.
DR EnsemblFungi; YDL055C_mRNA; YDL055C; YDL055C.
DR GeneID; 851504; -.
DR KEGG; sce:YDL055C; -.
DR SGD; S000002213; PSA1.
DR VEuPathDB; FungiDB:YDL055C; -.
DR eggNOG; KOG1322; Eukaryota.
DR GeneTree; ENSGT00940000158909; -.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; P41940; -.
DR OMA; PFLTHQL; -.
DR BioCyc; YEAST:YDL055C-MON; -.
DR BRENDA; 2.7.7.13; 984.
DR UniPathway; UPA00126; UER00930.
DR PRO; PR:P41940; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41940; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IDA:SGD.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045233; GMPPB_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; GTP-binding; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..361
FT /note="Mannose-1-phosphate guanyltransferase"
FT /id="PRO_0000068741"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 50
FT /note="V -> A (in Ref. 2; AAA69677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39566 MW; DBF1C39BEAE0B776 CRC64;
MKGLILVGGY GTRLRPLTLT VPKPLVEFGN RPMILHQIEA LANAGVTDIV LAVNYRPEVM
VETLKKYEKE YGVNITFSVE TEPLGTAGPL KLAEDVLKKD NSPFFVLNSD VICEYPFKEL
ADFHKAHGGK GTIVATKVDE PSKYGVIVHD IATPNLIDRF VEKPKEFVGN RINAGLYILN
PEVIDLIEMK PTSIEKETFP ILVEEKQLYS FDLEGFWMDV GQPKDFLSGT VLYLNSLAKR
QPKKLATGAN IVGNALIDPT AKISSTAKIG PDVVIGPNVT IGDGVRITRS VVLCNSTIKN
HSLVKSTIVG WNSTVGQWCR LEGVTVLGDD VEVKDEIYIN GGKVLPHKSI SDNVPKEAII
M
