PMU1_YEAST
ID PMU1_YEAST Reviewed; 295 AA.
AC P36069; D6VX67; E9P8Y9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable phosphoglycerate mutase PMU1;
DE EC=5.4.-.-;
DE AltName: Full=Phosphomutase homolog 1 {ECO:0000303|PubMed:8913738};
GN Name=PMU1 {ECO:0000303|PubMed:8913738}; OrderedLocusNames=YKL128C;
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=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 [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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=8913738; DOI=10.1093/genetics/144.3.923;
RA Elliott B., Haltiwanger R.S., Futcher B.;
RT "Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces
RT cerevisiae.";
RL Genetics 144:923-933(1996).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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).
CC -!- FUNCTION: Probable phosphomutase that may have a function related to
CC the manipulation of phosphate groups on carbohydrates. Reduces
CC trehalose-6-phosphate levels when overexpressed in TPS2-deleted cells.
CC Reduces 5'-Phosphoribosyl-4-carboxamide-5-aminoimidazole (AICAR)
CC levels, a metabolic intermediate at the crossroads between AMP and
CC histidine biosynthesis pathways, when overexpressed in a ADE3-ADE16-
CC ADE17 triple deletant. {ECO:0000269|PubMed:8913738}.
CC -!- INTERACTION:
CC P36069; P39940: RSP5; NbExp=2; IntAct=EBI-26862, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
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DR EMBL; Z28128; CAA81969.1; -; Genomic_DNA.
DR EMBL; AY692900; AAT92919.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09033.1; -; Genomic_DNA.
DR PIR; S37957; S37957.
DR RefSeq; NP_012794.1; NM_001179694.1.
DR AlphaFoldDB; P36069; -.
DR SMR; P36069; -.
DR BioGRID; 34007; 39.
DR IntAct; P36069; 1.
DR MINT; P36069; -.
DR STRING; 4932.YKL128C; -.
DR iPTMnet; P36069; -.
DR MaxQB; P36069; -.
DR PaxDb; P36069; -.
DR PRIDE; P36069; -.
DR EnsemblFungi; YKL128C_mRNA; YKL128C; YKL128C.
DR GeneID; 853730; -.
DR KEGG; sce:YKL128C; -.
DR SGD; S000001611; PMU1.
DR VEuPathDB; FungiDB:YKL128C; -.
DR eggNOG; KOG4754; Eukaryota.
DR HOGENOM; CLU_039184_0_0_1; -.
DR InParanoid; P36069; -.
DR OMA; GRHGQGF; -.
DR BioCyc; YEAST:G3O-31909-MON; -.
DR PRO; PR:P36069; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36069; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Nucleus; Reference proteome.
FT CHAIN 1..295
FT /note="Probable phosphoglycerate mutase PMU1"
FT /id="PRO_0000203152"
FT ACT_SITE 61
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT SITE 254
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT CONFLICT 44
FT /note="I -> V (in Ref. 3; AAT92919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33776 MW; B30CDCC0906922F5 CRC64;
MSLRAVPGYF AAYPSEGFQG LDSTKYDHLE LINHKNWKEL YHAIPRNTKN RHYKLLILAR
HGQGYHNAAI LRYGMEKWDA YWSLLSGDEH GEWLDSKLTP LGKDQVRRTG SNVLLPMAKQ
LGMLPHVFFS SPMRRCLETF IESWTPVLAE TQELPAGTKI STRIIEGLRE TLGSHTCDKR
VAHSMAVDEY QDFSTESGHT VHWQYVPDYP EDDELWLPDH RETCAEMDKR TLNGLFELFN
QLSSEEKFIS LTCHSGVIQS VLRNLQHPPI YNLDTGKVVA VVVEVPVNTA DRGRL
