PMG2_YEAST
ID PMG2_YEAST Reviewed; 311 AA.
AC Q12008; D6VRW9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Phosphoglycerate mutase 2;
DE Short=PGAM 2;
DE EC=5.4.2.11;
DE AltName: Full=BPG-dependent PGAM 2;
DE AltName: Full=MPGM 2;
DE AltName: Full=Phosphoglyceromutase 2;
GN Name=GPM2; OrderedLocusNames=YDL021W; ORFNames=D2835;
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=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 [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 CHARACTERIZATION.
RX PubMed=9544241;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<203::aid-yea205>3.0.co;2-8;
RA Heinisch J.J., Mueller S., Schlueter E., Jacoby J., Rodicio R.;
RT "Investigation of two yeast genes encoding putative isoenzymes of
RT phosphoglycerate mutase.";
RL Yeast 14:203-213(1998).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
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: Could be non-functional.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; Z48432; CAA88338.1; -; Genomic_DNA.
DR EMBL; Z74069; CAA98580.1; -; Genomic_DNA.
DR EMBL; AY692876; AAT92895.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11829.1; -; Genomic_DNA.
DR PIR; S52498; S52498.
DR RefSeq; NP_010263.1; NM_001180080.1.
DR AlphaFoldDB; Q12008; -.
DR SMR; Q12008; -.
DR BioGRID; 32034; 43.
DR IntAct; Q12008; 2.
DR MINT; Q12008; -.
DR STRING; 4932.YDL021W; -.
DR iPTMnet; Q12008; -.
DR MaxQB; Q12008; -.
DR PaxDb; Q12008; -.
DR PRIDE; Q12008; -.
DR TopDownProteomics; Q12008; -.
DR EnsemblFungi; YDL021W_mRNA; YDL021W; YDL021W.
DR GeneID; 851541; -.
DR KEGG; sce:YDL021W; -.
DR SGD; S000002179; GPM2.
DR VEuPathDB; FungiDB:YDL021W; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_6_1; -.
DR InParanoid; Q12008; -.
DR OMA; EYMYIRR; -.
DR BioCyc; YEAST:G3O-29450-MON; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:Q12008; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12008; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..311
FT /note="Phosphoglycerate mutase 2"
FT /id="PRO_0000179840"
FT ACT_SITE 17
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 16..23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 29..30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 242
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
SQ SEQUENCE 311 AA; 36073 MW; 1E53ECAAF06C932C CRC64;
MTASTPSNVM TLFLLRHGQS ELNHENIFCG WIDAKLTEKG KEQARHSAEL IEQYCKANNL
RLPQIGYTSR LIRTQQTIET MCEEFKLKPQ LQVVYDFNKI KLGDEFGSDD KDNMKIPILQ
TWRLNERHYG SWQGQRKPNV LKEYGKDKYM FIRRDYEGKP PPVDLDREMI QQENEKGSST
GYEFKEPNRQ IKYELECSNH DIVLPDSESL REVVYRLNPF LQNVILKLAN QYDESSCLIV
GHGSSVRSLL KILEGISDDD IKNVDIPNGI PLVVELDKNN GLKFIRKFYL DPESAKINAE
KVRNEGFIKN P
