3-Phosphoglycerate kinase (EC 2.7.2.3) of Saccharomyces cerevisiae, a highly abundant monomeric two-domain Mg2+-dependent enzyme that catalyses reversible phosphoryl transfer between 1,3-bisphosphoglycerate and ADP, forming 3-phosphoglycerate and ATP. It carries out the first substrate-level phosphorylation of glycolysis and, in the reverse direction, the ATP-consuming step of gluconeogenesis; PGK1 is the only phosphoglycerate kinase gene in yeast and pgk1 mutants cannot use glucose. Pgk1 is predominantly cytosolic, with a minor pool detected in mitochondrial fractions. Its strong constitutive promoter is widely used for heterologous expression.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004618 phosphoglycerate kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA from PTN000150497 (PGK family incl. human PGK1, E. coli Pgk and yeast Pgk1). Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl PMID:6254992 has been shown by both biochemical and genetic methods to contain the structural gene PGK for yeast 3-phosphoglycerate kinase |
| GO:0004618 phosphoglycerate kinase activity | IDA PMID:6254992 Isolation and characterization of the yeast 3-phosphoglycero... | ACCEPT | Summary: Hitzeman et al. cloned PGK by immunological screening and showed the clone directs synthesis of functional 3-phosphoglycerate kinase in yeast. Supporting Evidence: PMID:6254992 has been shown by both biochemical and genetic methods to contain the structural gene PGK for yeast 3-phosphoglycerate kinase PMID:6254992 functional enzyme is synthesized from the cloned gene in yeast, but not in E. coli |
| GO:0004618 phosphoglycerate kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from EC 2.7.2.3 / RHEA:14801 and PGK InterPro signatures; correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0004618 phosphoglycerate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (GLUCFERMEN-PWY); activity correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0004618 phosphoglycerate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (gluconeogenesis I); PGK operates reversibly. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0004618 phosphoglycerate kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (glycolysis); activity correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0005524 ATP binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA ATP binding; ATP/ADP is the phosphoryl-donor/acceptor substrate of PGK. Reason: Substrate binding implied by the kinase activity; non-core. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: Kumar et al. proteome-scale immunolocalization: cytoplasmic. Supporting Evidence: PMID:11914276 By high-throughput immunolocalization of tagged gene products, we have determined the subcellular localization of 2744 yeast proteins. file:yeast/PGK1/PGK1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}. |
| GO:0005737 cytoplasm | IDA PMID:27385335 Detection of protein-protein interactions at the septin coll... | ACCEPT | Summary: Finnigan et al. imaged endogenously GFP-tagged Pgk1 with a prominent cytosolic distribution. Supporting Evidence: PMID:27385335 exhibited a very prominent cytosolic distribution |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (Cytoplasm); correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | KEEP AS NON CORE | Summary: PROMITO mitochondrial proteome detected Pgk1. Reason: Minor mitochondria-associated pool of an abundant cytosolic glycolytic enzyme; not the site of its core function. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified by use of multidimensional LC-MS/MS |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | KEEP AS NON CORE | Summary: Renvoise et al. mitochondrial proteome detected Pgk1. Reason: Minor mitochondria-associated pool of an abundant cytosolic glycolytic enzyme; not the site of its core function. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria |
| GO:0005739 mitochondrion | IDA PMID:16962558 Enolase takes part in a macromolecular complex associated to... | KEEP AS NON CORE | Summary: Brandina et al.: all glycolytic enzymes are associated with yeast mitochondria. Reason: Minor mitochondria-associated pool of an abundant cytosolic glycolytic enzyme; not the site of its core function. Supporting Evidence: PMID:16962558 we show that all glycolytic enzymes are associated with mitochondria in yeast |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular-location mapping (Mitochondrion) derived from the PROMITO data. Reason: Minor mitochondria-associated pool of an abundant cytosolic glycolytic enzyme; not the site of its core function. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Mitochondrion {ECO:0000269|PubMed:16823961}. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: IBA cytosol from human PGK1/E. coli Pgk; consistent with localisation data. Supporting Evidence: PMID:27385335 exhibited a very prominent cytosolic distribution |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA cytosol (GLUCFERMEN-PWY); correct. Supporting Evidence: PMID:27385335 exhibited a very prominent cytosolic distribution |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA cytosol (GLUCONEO-PWY-1); correct. Supporting Evidence: PMID:27385335 exhibited a very prominent cytosolic distribution |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA cytosol (GLYCOLYSIS); correct. Supporting Evidence: PMID:27385335 exhibited a very prominent cytosolic distribution |
| GO:0005886 plasma membrane | HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and... | MARK AS OVER ANNOTATED | Summary: Delom et al. detected Pgk1 in a stripped plasma-membrane proteome fraction. Pgk1 is among the most abundant cytosolic proteins and has no membrane-targeting features; co-purification is the likely explanation. Reason: High-throughput detection of an abundant cytosolic enzyme in a membrane fraction; no supporting functional evidence for plasma-membrane residence. Supporting Evidence: PMID:16622836 Proteins from a stripped plasma membrane fraction were solubilized with the neutral and non-denaturing detergent |
| GO:0006094 gluconeogenesis | IBA GO_REF:0000033 | ACCEPT | Summary: IBA gluconeogenesis; PGK is the only enzyme for the 3PG -> 1,3BPG step needed for gluconeogenesis. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0006094 gluconeogenesis | IMP PMID:400791 Isolation and characterization of Saccharomyces cerevisiae g... | ACCEPT | Summary: Lam & Marmur isolated pgk mutants; the curator annotated gluconeogenesis from the full text. As the sole PGK, Pgk1 is required in both directions. Reason: Defer to curator; consistent with the reversible reaction. Supporting Evidence: PMID:400791 cause defects in pyruvate kinase, pyruvate decarboxylase, 3-phosphoglycerate kinase, and 3-phosphoglycerate mutase |
| GO:0006094 gluconeogenesis | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (gluconeogenesis I); correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0006096 glycolysis | IBA GO_REF:0000033 | ACCEPT | Summary: IBA glycolysis from the PGK family; correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:0006096 glycolysis | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from UniPathway UPA00109; correct. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:0006096 glycolysis | IMP PMID:400791 Isolation and characterization of Saccharomyces cerevisiae g... | ACCEPT | Summary: pgk mutants are unable to use glucose as a carbon source. Supporting Evidence: PMID:400791 cause defects in pyruvate kinase, pyruvate decarboxylase, 3-phosphoglycerate kinase, and 3-phosphoglycerate mutase PMID:400791 Cells carrying these mutations were unable to use glucose as a carbon source |
| GO:0019658 bifid shunt | RCA GO_REF:0000123 | REMOVE | Summary: GLUCFERMEN-PWY (superpathway of glucose fermentation) mis-mapped to 'bifid shunt', a Bifidobacterium phosphoketolase pathway producing lactate and acetate; not present in S. cerevisiae. Reason: Erroneous pathway-to-GO mapping. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0043531 ADP binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA ADP binding; ADP is a substrate of the forward glycolytic reaction. Reason: Substrate binding implied by catalytic activity; non-core. Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
| GO:0047134 protein-disulfide reductase [NAD(P)H] activity | IDA NOT PMID:11130727 Phosphoglycerate kinase acts in tumour angiogenesis as a dis... | ACCEPT | Summary: NOT annotation from Lay et al. (mammalian PGK acts as a secreted plasmin disulfide reductase). The NOT qualifier, presumably from a yeast PGK control reported in the full text, records that yeast Pgk1 lacks this activity; there is no evidence of such a role in yeast. Reason: Accept the negative annotation; defer to curator. Supporting Evidence: PMID:11130727 Here we show that the plasmin reductase isolated from conditioned medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate kinase. |
| GO:0061620 obsolete glycolytic process through glucose-6-phosphate | RCA GO_REF:0000123 | MODIFY | Summary: RCA to obsolete 'glycolytic process through glucose-6-phosphate'; biology correct, term retired. Reason: Update to current glycolysis term. Proposed replacements: glycolysis Supporting Evidence: file:yeast/PGK1/PGK1-uniprot.txt Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl |
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