Reviewed, UniProtKB/Swiss-Prot P00950 (PMG1_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphoglycerate mutase 1
      Short name=PGAM 1
    EC=5.4.2.1
Alternative name(s):
    Phosphoglyceromutase 1
    MPGM 1
    BPG-dependent PGAM 1

Gene names

Name:	GPM1
Synonyms:	GPM
Ordered Locus Names:	YKL152C
ORF Names:	YKL607

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subunit structure	Homotetramer.
Miscellaneous	Present with 172000 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from mutant phenotype. Source: SGD glycolysis Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	phosphoglycerate mutase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VID30	P53076	1	EBI-13517,EBI-24173

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.7

Chain

2 – 247

246

Phosphoglycerate mutase 1

PRO_0000179839

Regions

Compositional bias

233 – 242

10

Ala-rich

Sites

Active site

9

1

Tele-phosphohistidine intermediate Ref.15

Active site

182

1

Site

60

1

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.11

Modified residue

116

1

Phosphoserine Ref.11 Ref.10 Ref.12 Ref.13

Modified residue

127

1

Phosphoserine Ref.12 Ref.13

Modified residue

128

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

131

1

Phosphoserine Ref.13

Modified residue

185

1

Phosphoserine Ref.11

Modified residue

197

1

Phosphoserine Ref.12 Ref.13

Secondary structure

1

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247

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

13 – 16

4

Helix

30 – 45

16

Beta strand

51 – 55

5

Helix

59 – 71

13

Beta strand

79 – 81

3

Helix

83 – 85

3

Helix

91 – 93

3

Helix

98 – 115

18

Helix

136 – 138

3

Helix

143 – 145

3

Helix

152 – 165

14

Helix

167 – 172

6

Beta strand

177 – 181

5

Helix

183 – 194

12

Turn

198 – 200

3

Helix

201 – 203

3

Beta strand

212 – 216

5

Beta strand

222 – 224

3

Beta strand

227 – 230

4

Turn

231 – 233

3

Sequences

	Sequence		Length	Mass (Da)
	P00950-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 45E1A9CCDBDC104D	FASTA	247	27,609
	10 20 30 40 50 60 MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA KGQQEAARAG ELLKEKKVYP DVLYTSKLSR 70 80 90 100 110 120 AIQTANIALE KADRLWIPVN RSWRLNERHY GDLQGKDKAE TLKKFGEEKF NTYRRSFDVP 130 140 150 160 170 180 PPPIDASSPF SQKGDERYKY VDPNVLPETE SLALVIDRLL PYWQDVIAKD LLSGKTVMIA 190 200 210 220 230 240 AHGNSLRGLV KHLEGISDAD IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA VANQGKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The amino acid sequence of yeast phosphoglycerate mutase." Fothergill L.A., Harkins R.N. Proc. R. Soc. Lond., B, Biol. Sci. 215:19-44(1982) [PubMed: 6127696] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-247.
[2]	"Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae." White M.F., Fothergill-Gilmore L.A. FEBS Lett. 229:383-387(1988) [PubMed: 2831102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and localization of the gene encoding yeast phosphoglycerate mutase." Heinisch J.J., von Borstel R.C., Rodicio R.M. Curr. Genet. 20:167-171(1991) [PubMed: 1834353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae." Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F. Yeast 10:S35-S40(1994) [PubMed: 8091859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Transcriptional control of yeast phosphoglycerate mutase-encoding gene." Rodicio R., Heinisch J.J., Hollenberg C.P. Gene 125:125-133(1993) [PubMed: 8462867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[7]	Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PARTIAL PROTEIN SEQUENCE OF 2-11. Strain: ATCC 26786 / X2180-1A.
[8]	"Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins." Norbeck J., Blomberg A. Yeast 13:1519-1534(1997) [PubMed: 9509572] [Abstract] Cited for: PROTEIN SEQUENCE OF 110-114 AND 204-217. Strain: ATCC 44827 / SKQ2N.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, MASS SPECTROMETRY.
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-116; SER-128 AND SER-185, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127; SER-128 AND SER-197, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127; SER-128; SER-131 AND SER-197, MASS SPECTROMETRY.
[14]	"Structure and activity of phosphoglycerate mutase." Winn S.I., Watson H.C., Harkins R.N., Fothergill L.A. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:121-130(1981) [PubMed: 6115412] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[15]	"The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase." Rigden D.J., Alexeev D., Phillips S.E.V.P., Fothergill-Gilmore L.A. J. Mol. Biol. 276:449-459(1998) [PubMed: 9512715] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X06408 Genomic DNA. Translation: CAA29698.1.
X58789 Genomic DNA. Translation: CAA41595.1.
Z26877 Genomic DNA. Translation: CAA81501.1.
Z28152 Genomic DNA. Translation: CAA81994.1.
S57976 Genomic DNA. Translation: AAB26026.1. Different termination.

PIR

PMBYY. S00358.

RefSeq

NP_012770.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BQ3	X-ray	2.70	A/B/C/D	2-247	[»]
1BQ4	X-ray	2.50	A/B/C/D	2-247	[»]
1QHF	X-ray	1.70	A/B	2-240	[»]
3PGM	X-ray	2.80	A/B	2-247	[»]
4PGM	X-ray	2.30	A/B/C/D	2-247	[»]
5PGM	X-ray	2.12	A/B/C/D/E/F/G/H	2-246	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6260N.

IntAct

P00950. 23 interactions.

2-D gel databases

SWISS-2DPAGE

P00950.

COMPLUYEAST-2DPAGE

P00950.

Proteomic databases

PeptideAtlas

P00950.

PRIDE

P00950.

Genome annotation databases

Ensembl

YKL152C. Saccharomyces cerevisiae. [Contig view]

GeneID

853705.

GenomeReviews

Gene locus YKL152C in contig Y13137_GR.

KEGG

sce:YKL152C.

NMPDR

fig|4932.3.peg.3749.

Organism-specific databases

CYGD

YKL152c.

SGD

S000001635. GPM1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00950.

OMA

P00950. PMRFLGD.

Enzyme and pathway databases

BRENDA

5.4.2.1. 250.

Gene expression databases

GermOnline

YKL152C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001345. PG/BPGM_mutase.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. Phosphogly_mut1. 1 hit.

Pfam

PF00300. PGAM. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01258. pgm_1. 1 hit.

PROSITE

PS00175. PG_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

974701.

Entry information

Entry name

PMG1_YEAST

Accession

Primary (citable) accession number: P00950
Secondary accession number(s): Q02117

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)