| General Information |
| MoonProt ID | 99 |
| First appeared in release | 1.0 |
| Name(s) | Fructose 1,6-bisphosphate Aldolase
Fructose-bisphosphate aldolase
FBP aldolase
FBPA
Gene Name:FBA1 |
| UniProt ID | P14540 (ALF_YEAST), Reviewed |
| GO terms | GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0003824 catalytic activity
GO:0004332 fructose-bisphosphate aldolase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
GO:0005739 mitochondrion
GO:0005829 cytosol |
| Organisms for which functions have been demonstrated | Saccharomyces cerevisiae (yeast, fungi) |
| Sequence length | 359 |
| FASTA sequence | >sp|P14540|ALF_YEAST Fructose-bisphosphate aldolase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=FBA1 PE=1 SV=3
MGVEQILKRKTGVIVGEDVHNLFTYAKEHKFAIPAINVTSSSTAVAALEAARDSKSPIILQTSNGGAAYFAGKGISNEGQNASIKGAIAAAHYIRSIAPAYGIPVVLHSDHCAKKLLPWFDGMLEADEAYFKEHGEPLFSSHMLDLSEETDEENISTCVKYFKRMAAMDQWLEMEIGITGGEEDGVNNENADKEDLYTKPEQVYNVYKALHPISPNFSIAAAFGNCHGLYAGDIALRPEILAEHQKYTREQVGCKEEKPLFLVFHGGSGSTVQEFHTGIDNGVVKVNLDTDCQYAYLTGIRDYVLNKKDYIMSPVGNPEGPEKPNKKFFDPRVWVREGEKTMGAKITKSLETFRTTNTL
|
| Structure Information |
| PDB ID | |
| Quaternary structure | |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-7, 356-359 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Aldolase, enzyme
D-fructose 1,6-bisphosphate <=> dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
Glycolysis, Gluconeogenesis |
| References for function | |
| E.C. number | 4.1.2.13 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | binds to vacuolar H+-ATPase and is needed for its assembly
enzymatic catalytic activity not needed for this function |
| References for function | Lu M, Holliday LS, Zhang L, Dunn WA, Gluck SL. Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J Biol Chem. 2001 Aug 10. PMID: 11399750.
Lu M, Sautin YY, Holliday LS, Gluck SL. The glycolytic enzyme aldolase mediates assembly, expression, and activity of vacuolar H+-ATPase. J Biol Chem. 2004 Mar 5. PMID: 14672945.
Lu M, Ammar D, Ives H, Albrecht F, Gluck SL. Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump. J Biol Chem. 2007 Aug 24. PMID: 17576770. |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | mitochondrion |
| Comments | |