PMG3_YEAST
ID PMG3_YEAST Reviewed; 303 AA.
AC Q12326; D6W211;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phosphoglycerate mutase 3;
DE Short=PGAM 3;
DE EC=5.4.2.11;
DE AltName: Full=BPG-dependent PGAM 3;
DE AltName: Full=MPGM 3;
DE AltName: Full=Phosphoglyceromutase 3;
GN Name=GPM3; OrderedLocusNames=YOL056W; ORFNames=O1236;
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 90843 / S288c / FY73;
RX PubMed=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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 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 -!- MISCELLANEOUS: Present with 3730 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; X91067; CAA62530.1; -; Genomic_DNA.
DR EMBL; Z74798; CAA99064.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10727.1; -; Genomic_DNA.
DR PIR; S61723; S61723.
DR RefSeq; NP_014585.1; NM_001183311.1.
DR AlphaFoldDB; Q12326; -.
DR SMR; Q12326; -.
DR BioGRID; 34345; 95.
DR DIP; DIP-4234N; -.
DR IntAct; Q12326; 5.
DR STRING; 4932.YOL056W; -.
DR MaxQB; Q12326; -.
DR PaxDb; Q12326; -.
DR PRIDE; Q12326; -.
DR EnsemblFungi; YOL056W_mRNA; YOL056W; YOL056W.
DR GeneID; 854098; -.
DR KEGG; sce:YOL056W; -.
DR SGD; S000005417; GPM3.
DR VEuPathDB; FungiDB:YOL056W; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_6_1; -.
DR InParanoid; Q12326; -.
DR OMA; IRTQQTM; -.
DR BioCyc; YEAST:G3O-33467-MON; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:Q12326; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12326; protein.
DR GO; GO:0005737; C:cytoplasm; HDA: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 Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..303
FT /note="Phosphoglycerate mutase 3"
FT /id="PRO_0000179841"
FT REGION 168..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 14
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT ACT_SITE 120
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 13..20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 26..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 120..123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 147..148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 235
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
SQ SEQUENCE 303 AA; 34863 MW; 29C3FF3D28560914 CRC64;
MTVTDTFKLF ILRHGQSELN SENIFCGWID AQLTEKGKSQ ARHSAKLIKQ FCDSNNISLP
QIGYTSRLIR TQQTMDVILE ELGLKHTNYV ITTNTNIKEE LQDTRFEGSM PVLQTWRLNE
RHYGAWQGQR KPDILKEYGK EKYMYIRRDY NGKPPKVNLN LEMVQEENDQ GSSTGYDFKE
PNRHLKYGPE EKANERLPES ESLCEVVVRL KPFLNNVVLS TANKISQESC VIVGHGSSVR
SLLKVLEGIS DEDIKDVDIP NGIPLVIELD RDNYSFVRKF YLDPESAKVN AQMVRDEGFE
KNP
