ID   PMG3_YEAST              Reviewed;         303 AA.
AC   Q12326;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Phosphoglycerate mutase 3;
DE            Short=PGAM 3;
DE            EC=5.4.2.1;
DE   AltName: Full=Phosphoglyceromutase 3;
DE   AltName: Full=MPGM 3;
DE   AltName: Full=BPG-dependent PGAM 3;
GN   Name=GPM3; OrderedLocusNames=YOL056W; ORFNames=O1236;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90843 / S288c / FY73;
RX   MEDLINE=96381248; 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 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   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.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   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   CHARACTERIZATION.
RX   MEDLINE=98205882; PubMed=9544241;
RX   DOI=10.1002/(SICI)1097-0061(199802)14:3<203::AID-YEA205>3.3.CO;2-#;
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   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., 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: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5.
CC   -!- INTERACTION:
CC       P43582:-; NbExp=1; IntAct=EBI-13526, EBI-22766;
CC       Q08409:AUS1; NbExp=1; IntAct=EBI-13526, EBI-35723;
CC       Q06525:URN1; NbExp=1; IntAct=EBI-13526, EBI-35138;
CC   -!- MISCELLANEOUS: Present with 3730 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; X91067; CAA62530.1; -; Genomic_DNA.
DR   EMBL; Z74798; CAA99064.1; -; Genomic_DNA.
DR   PIR; S61723; S61723.
DR   RefSeq; NP_014585.1; -.
DR   HSSP; P00950; 1QHF.
DR   DIP; DIP:4234N; -.
DR   IntAct; Q12326; 10.
DR   PeptideAtlas; Q12326; -.
DR   Ensembl; YOL056W; Saccharomyces cerevisiae.
DR   GeneID; 854098; -.
DR   GenomeReviews; Y13140_GR; YOL056W.
DR   KEGG; sce:YOL056W; -.
DR   NMPDR; fig|4932.3.peg.5677; -.
DR   CYGD; YOL056w; -.
DR   SGD; S000005417; GPM3.
DR   HOGENOM; Q12326; -.
DR   OMA; Q12326; NVARERW.
DR   BRENDA; 5.4.2.1; 250.
DR   NextBio; 975767; -.
DR   GermOnline; YOL056W; Saccharomyces cerevisiae.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    303       Phosphoglycerate mutase 3.
FT                                /FTId=PRO_0000179841.
FT   ACT_SITE     14     14       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    235    235       By similarity.
FT   SITE         70     70       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
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
//