Reviewed, UniProtKB/Swiss-Prot P00560 (PGK_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphoglycerate kinase
    EC=2.7.2.3

Gene names

Name:	PGK1
Ordered Locus Names:	YCR012W
ORF Names:	YCR12W

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	416 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)

Catalytic activity	ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 314000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation 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 electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglycerate kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 416

415

Phosphoglycerate kinase

PRO_0000145893

Regions

Nucleotide binding

371 – 374

4

ATP

Region

24 – 26

3

Substrate binding

Region

63 – 66

4

Substrate binding

Sites

Binding site

39

1

Substrate

Binding site

122

1

Substrate

Binding site

169

1

Substrate

Binding site

218

1

ATP

Binding site

311

1

ATP; via carbonyl oxygen

Binding site

335

1

ATP

Binding site

342

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

4

1

Phosphoserine

Modified residue

5

1

Phosphoserine

Modified residue

8

1

Phosphoserine

Modified residue

36

1

Phosphoserine

Modified residue

76

1

Phosphoserine

Modified residue

93

1

Phosphothreonine

Modified residue

110

1

Phosphoserine

Modified residue

114

1

Phosphoserine

Modified residue

130

1

Phosphoserine

Modified residue

154

1

Phosphoserine

Modified residue

203

1

Phosphothreonine

Modified residue

241

1

Phosphothreonine

Modified residue

331

1

Phosphothreonine

Modified residue

376

1

Phosphothreonine

Modified residue

391

1

Phosphoserine

Modified residue

392

1

Phosphothreonine

Modified residue

397

1

Phosphoserine

Modified residue

413

1

Phosphoserine

Experimental info

Mutagenesis

22

1

R → K: 2-fold reduction of Vmax

Mutagenesis

22

1

R → M: 7-fold reduction of Vmax

Sequence conflict

185

1

G → S AA sequence Ref.4

Sequence conflict

191

1

E → I AA sequence Ref.4

Secondary structure

1

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416

Helix Strand Turn

Details...

Helix

9 – 11

3

Beta strand

18 – 22

5

Beta strand

29 – 35

7

Helix

38 – 51

14

Beta strand

56 – 61

6

Helix

78 – 88

11

Beta strand

92 – 94

3

Beta strand

98 – 100

3

Helix

101 – 108

8

Beta strand

114 – 117

4

Helix

121 – 123

3

Turn

125 – 128

4

Beta strand

129 – 133

5

Beta strand

136 – 139

4

Helix

142 – 153

12

Beta strand

157 – 161

5

Helix

164 – 166

3

Helix

172 – 175

4

Beta strand

182 – 184

3

Helix

186 – 200

15

Beta strand

204 – 211

8

Turn

216 – 218

3

Helix

219 – 226

8

Beta strand

230 – 235

6

Helix

236 – 238

3

Helix

239 – 246

8

Helix

258 – 273

16

Beta strand

277 – 279

3

Beta strand

282 – 291

10

Beta strand

296 – 300

5

Turn

301 – 303

3

Beta strand

310 – 314

5

Helix

316 – 328

13

Beta strand

330 – 336

7

Helix

344 – 346

3

Helix

348 – 362

15

Beta strand

366 – 369

4

Helix

373 – 380

8

Helix

384 – 386

3

Beta strand

387 – 390

4

Helix

395 – 401

7

Helix

407 – 410

4

Sequences

	Sequence		Length	Mass (Da)
	P00560-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 378AB944DB34EFF0	FASTA	416	44,738
	10 20 30 40 50 60 MSLSSKLSVQ DLDLKDKRVF IRVDFNVPLD GKKITSNQRI VAALPTIKYV LEHHPRYVVL 70 80 90 100 110 120 ASHLGRPNGE RNEKYSLAPV AKELQSLLGK DVTFLNDCVG PEVEAAVKAS APGSVILLEN 130 140 150 160 170 180 LRYHIEEEGS RKVDGQKVKA SKEDVQKFRH ELSSLADVYI NDAFGTAHRA HSSMVGFDLP 190 200 210 220 230 240 QRAAGFLLEK ELKYFGKALE NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIIIGGGMAF 250 260 270 280 290 300 TFKKVLENTE IGDSIFDKAG AEIVPKLMEK AKAKGVEVVL PVDFIIADAF SADANTKTVT 310 320 330 340 350 360 DKEGIPAGWQ GLDNGPESRK LFAATVAKAK TIVWNGPPGV FEFEKFAAGT KALLDEVVKS 370 380 390 400 410 SAAGNTVIIG GGDTATVAKK YGVTDKISHV STGGGASLEL LEGKELPGVA FLSEKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the Saccharomyces cerevisiae gene for 3-phosphoglycerate kinase." Hitzeman R.A., Hagie F.E., Hayflick J.S., Chen C.Y., Seeburg P.H., Derynck R. Nucleic Acids Res. 10:7791-7808(1982) [PubMed: 6296791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm of chromosome III from Saccharomyces cerevisiae reveals seven open reading frames including the RVS161, ADP1 and PGK genes." Skala J., Purnelle B., Goffeau A. Yeast 8:409-417(1992) [PubMed: 1626432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pall