P00950 (PMG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate mutase 1
Short name=PGAM 1
EC=5.4.2.1

Alternative name(s):
BPG-dependent PGAM 1
MPGM 1
Phosphoglyceromutase 1

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from mutant phenotype PubMed 3033435. Source: SGD glycolysis Inferred from mutant phenotype PubMed 11015729. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 3332961. Source: SGD mitochondrial intermembrane space Inferred from direct assay PubMed 22984289. Source: SGD
Molecular_function	phosphoglycerate mutase activity Inferred from direct assay PubMed 1386023. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.8

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.16

Active site

182

1

Site

60

1

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.12

Modified residue

116

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

127

1

Phosphoserine Ref.13 Ref.14

Modified residue

128

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

131

1

Phosphoserine Ref.14

Modified residue

185

1

Phosphoserine Ref.12

Modified residue

197

1

Phosphoserine Ref.13 Ref.14

Secondary structure

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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

Beta strand

116 – 118

3

Beta strand

126 – 130

5

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

208 – 210

3

Beta strand

212 – 216

5

Turn

218 – 220

3

Beta strand

222 – 224

3

Beta strand

227 – 230

4

Turn

231 – 233

3

Sequences

	Sequence		Length	Mass (Da)
	P00950 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Transcriptional control of yeast phosphoglycerate mutase-encoding gene." Rodicio R., Heinisch J.J., Hollenberg C.P. Gene 125:125-133(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[8]	Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11. Strain: ATCC 26786 / X2180-1A.
[9]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 110-114 AND 204-217. Strain: ATCC 44827 / SKQ2N.
[10]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, MASS SPECTROMETRY. Strain: ADR376.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-116; SER-128 AND SER-185, MASS SPECTROMETRY.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127; SER-128 AND SER-197, MASS SPECTROMETRY.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-127; SER-128; SER-131 AND SER-197, MASS SPECTROMETRY.
[15]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
BK006944 Genomic DNA. Translation: DAA09011.1.

PIR

PMBYY. S00358.

RefSeq

NP_012770.1. NM_001179718.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00950.

SMR

P00950. Positions 2-236.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6260N.

IntAct

P00950. 18 interactions.

MINT

MINT-603921.

STRING

4932.YKL152C.

2D gel databases

COMPLUYEAST-2DPAGE

P00950.

SWISS-2DPAGE

P00950.

Proteomic databases

PaxDb

P00950.

PeptideAtlas

P00950.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKL152C; YKL152C; YKL152C.

GeneID

853705.

KEGG

sce:YKL152C.

Organism-specific databases

SGD

S000001635. GPM1.

Phylogenomic databases

eggNOG

COG0588.

GeneTree

ENSGT00390000016700.

HOGENOM

HOG000221682.

KO

K01834.

OMA

GRKEACA.

OrthoDB

EOG4X6GJK.

Enzyme and pathway databases

UniPathway

UPA00109; UER00186.

Gene expression databases

Genevestigator

P00950.

GermOnline

YKL152C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. PTHR11931. 1 hit.

Pfam

PF00300. His_Phos_1. 1 hit.
[Graphical view]

SMART

SM00855. PGAM. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01258. pgm_1. 1 hit.

PROSITE

PS00175. PG_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00950.

NextBio

974701.

Entry information

Entry name

PMG1_YEAST

Accession

Primary (citable) accession number: P00950
Secondary accession number(s): D6VX45, Q02117

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program