P12709 (G6PI_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 117.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glucose-6-phosphate isomerase Short name=GPI EC=5.3.1.9 Alternative name(s): Phosphoglucose isomerase Short name=PGI Phosphohexose isomerase Short name=PHI | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 554 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 | D-glucose 6-phosphate = D-fructose 6-phosphate. |
| Pathway | |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Miscellaneous | Present with 91600 molecules/cell in log phase SD medium. Ref.8 |
| Sequence similarities | Belongs to the GPI family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis Glycolysis |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from mutant phenotype. Source: SGD glycolysisInferred from mutant phenotype. Source: SGD pentose-phosphate shuntInferred from mutant phenotype. Source: SGD |
| Cellular component | mitochondrion Inferred from direct assay. Source: SGD plasma membrane enriched fractionInferred from direct assay. Source: SGD |
| Molecular function | glucose-6-phosphate isomerase activity Inferred from mutant phenotype. 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 | ||||||
| Chain | 2 – 554 | 553 | Glucose-6-phosphate isomerase | PRO_0000180578 | |||||
Sites | |||||||||
| Active site | 367 | 1 | Proton donor By similarity | ||||||
| Active site | 398 | 1 | By similarity | ||||||
| Active site | 520 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.7 | ||||||
| Modified residue | 33 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 51 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 53 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 102 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 193 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 198 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 223 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 470 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 534 | 1 | Phosphoserine Ref.11 Ref.12 | ||||||
| Modified residue | 537 | 1 | Phosphoserine Ref.11 Ref.12 | ||||||
| Modified residue | 538 | 1 | Phosphothreonine Ref.12 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The isolation, characterization and nucleotide sequence of the phosphoglucoisomerase gene of Saccharomyces cerevisiae." Tekamp-Olson P., Najarian R., Burke R.L. Gene 73:153-161(1988) [PubMed: 3072254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The structure and regulation of phosphoglucose isomerase in Saccharomyces cerevisiae." Green J.B.A., Wright A.P.H., Cheung W.Y., Lancashire W.E., Hartley B.S. Mol. Gen. Genet. 215:100-106(1988) [PubMed: 3071735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204510 / AB320. |
| [3] | "RIM2, MSI1 and PGI1 are located within an 8 kb segment of Saccharomyces cerevisiae chromosome II, which also contains the putative ribosomal gene L21 and a new putative essential gene with a leucine zipper motif." Demolis N., Mallet L., Bussereau F., Jacquet M. Yeast 9:645-659(1993) [PubMed: 8346681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | "Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K.EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [5] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [6] | "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family." Mallet L., Bussereau F., Jacquet M. Yeast 10:819-831(1994) [PubMed: 7975899] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-554. Strain: ATCC 204508 / S288c. |
| [7] | "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2. |
| [8] | "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]. |
| [9] | "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, MASS SPECTROMETRY. Strain: YAL6B. |
| [10] | "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-193 AND THR-198, MASS SPECTROMETRY. |
| [11] | "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-534 AND SER-537, MASS SPECTROMETRY. |
| [12] | "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 THR-51; THR-53; THR-102; THR-223; SER-470; SER-534; SER-537 AND THR-538, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M37267 Genomic DNA. Translation: AAA34862.1. M21696 Genomic DNA. Translation: AAA34894.1. X13977 Genomic DNA. Translation: CAA32158.1. Z21487 Genomic DNA. Translation: CAA79683.1. Z36065 Genomic DNA. Translation: CAA85158.1. BK006936 Genomic DNA. Translation: DAA07310.1. |
| PIR | NUBY. JT0484. |
| RefSeq | NP_009755.1. NM_001178544.1. |
3D structure databases | |
| ProteinModelPortal | P12709. |
| SMR | P12709. Positions 6-553. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-1605N. |
| IntAct | P12709. 15 interactions. |
| MINT | MINT-386473. |
| STRING | P12709. |
Proteomic databases | |
| PeptideAtlas | P12709. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YBR196C; YBR196C; YBR196C. |
| GeneID | 852495. |
| KEGG | sce:YBR196C. |
| NMPDR | fig|4932.3.peg.463. |
Organism-specific databases | |
| SGD | S000000400. PGI1. |
Phylogenomic databases | |
| eggNOG | fuNOG04321. |
| GeneTree | EFGT00050000004334. |
| HOGENOM | HBG352954. |
| OMA | GPKIVSQ. |
| OrthoDB | EOG43NBN0. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-6121. |
Gene expression databases | |
| ArrayExpress | P12709. |
| Genevestigator | P12709. |
| GermOnline | YBR196C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001672. G6P_Isomerase. IPR023096. G6P_Isomerase_C. IPR018189. Phosphoglucose_isomerase_CS. [Graphical view] |
| Gene3D | G3DSA:1.10.1390.10. G6P_Isomerase_C. 1 hit. |
| KO | K01810. |
| PANTHER | PTHR11469. G6P_Isomerase. 1 hit. |
| Pfam | PF00342. PGI. 1 hit. [Graphical view] |
| PRINTS | PR00662. G6PISOMERASE. |
| PROSITE | PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit. PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit. PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 971489. |
Entry information
| Entry name | G6PI_YEAST | ||||||||
| Accession | Primary (citable) accession number: P12709 Secondary accession number(s): D6VQJ0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome II Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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