FBP1/YLR377C Summary Help

Standard Name FBP1
Systematic Name YLR377C
Alias ACN8
Feature Type ORF, Verified
Description Fructose-1,6-bisphosphatase; key regulatory enzyme in the gluconeogenesis pathway, required for glucose metabolism; undergoes either proteasome-mediated or autophagy-mediated degradation depending on growth conditions; glucose starvation results in redistribution to the periplasm; interacts with Vid30p (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description Fructose-1,6-BisPhosphatase
Chromosomal Location
ChrXII:874792 to 873746 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All FBP1 GO evidence and references
  View Computational GO annotations for FBP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 8 genes
Classical genetics
Large-scale survey
80 total interaction(s) for 65 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-Western: 19
  • Co-fractionation: 3
  • Reconstituted Complex: 1
  • Two-hybrid: 8

Genetic Interactions
  • Negative Genetic: 17
  • Positive Genetic: 11
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 348
Molecular Weight (Da) 38,262
Isoelectric Point (pI) 5.89
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXII:874792 to 873746 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1047 874792..873746 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004369

Gluconeogenesis is the process whereby glucose is synthesized from non-carbohydrate precursors, which enables yeast cells to grow on non-sugar carbon sources like ethanol, glycerol, or peptone. The reactions of gluconeogenesis, shown here, mediate conversion of pyruvate to glucose, which is the opposite of glycolysis, the formation of pyruvate from glucose. While these two pathways have several reactions in common, they are not the exact reverse of each other. As the glycolytic enzymes phosphofructokinase (Pfk1p, Pfk2p) and pyruvate kinase (Cdc19p) only function in the forward direction, the gluconeogenesis pathway replaces those steps with the enzymes pyruvate carboxylase (Pyc1p, Pyc2p) and phosphoenolpyruvate carboxykinase (Pck1p)-generating oxaloacetate as an intermediate from pyruvate to phosphoenolpyruvate-and also the enzyme fructose-1,6-bisphosphatase (Fbp1p) (reviewed in 6). Overall, the gluconeogenic reactions convert two molecules of pyruvate to a molecule of glucose, with the expenditure of six high-energy phosphate bonds, four from ATP and two from GTP. Expression of genes encoding several of the gluconeogenic enzymes is subject to glucose repression (7).

In addition to regulation of transcription (through catabolite repression), the amount of Fbp1p in the cell is regulated by mRNA and protein degradation when glucose-starved cells are replenished with glucose (8, 9). There appear to be two pathways for degradation of Fbp1p: a proteasomal pathway that acts following short-term glucose starvation and a vacuolar pathway that functions following long-term glucose starvation (3). Transcriptional regulation is effected through consensus sequences in the FBP1 promoter region for the repressor Mig1p, the activating HAP complex, and the derepressing zinc finger protein Cat8p (10, reviewed in 6).

Last updated: 2005-06-21 Contact SGD

References cited on this page View Complete Literature Guide for FBP1
1) Entian KD, et al.  (1988) Isolation and primary structure of the gene encoding fructose-1,6-bisphosphatase from Saccharomyces cerevisiae. FEBS Lett 236(1):195-200
2) Hoffman M and Chiang HL  (1996) Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 143(4):1555-66
3) Hung GC, et al.  (2004) Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J Biol Chem 279(47):49138-50
4) Santt O, et al.  (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
5) Alibhoy AA, et al.  (2012) Vps34p is required for the decline of extracellular fructose-1,6-bisphosphatase in the vacuole import and degradation pathway. J Biol Chem 287(39):33080-93
6) Klein CJ, et al.  (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1)():13-24
7) Haarasilta S and Oura E  (1975) On the activity and regulation of anaplerotic and gluconeogenetic enzymes during the growth process of baker's yeast. The biphasic growth. Eur J Biochem 52(1):1-7
8) Mercado JJ, et al.  (1994) The levels of yeast gluconeogenic mRNAs respond to environmental factors. Eur J Biochem 224(2):473-81
9) Holzer H and Purwin C  (1986) How does glucose initiate proteolysis of yeast fructose-1,6-bisphosphatase? Biomed Biochim Acta 45(11-12):1657-63
10) Mercado JJ and Gancedo JM  (1992) Regulatory regions in the yeast FBP1 and PCK1 genes. FEBS Lett 311(2):110-4