| Identification |
| HMDB Protein ID
| HMDBP13137 |
| Secondary Accession Numbers
| None |
| Name
| Fructose-bisphosphate aldolase A |
| Synonyms
|
- Muscle-type aldolase
|
| Gene Name
| ALDOA |
| Protein Type
| Unknown |
| Biological Properties |
| General Function
| Not Available |
| Specific Function
| Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein. |
| Pathways
|
- Biosynthesis of amino acids
- Carbon metabolism
- Fructose and mannose metabolism
- glycolysis
- Glycolysis / Gluconeogenesis
- HIF-1 signaling pathway
- Pentose phosphate pathway
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| protein homotetramerization |
| glycolysis |
| positive regulation of cell migration |
| negative regulation of Arp2/3 complex-mediated actin nucleation |
| Cellular Component |
| I band |
| M band |
| Molecular Function |
| fructose-bisphosphate aldolase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
| Number of Residues
| 364 |
| Molecular Weight
| 39342.555 |
| Theoretical pI
| 8.095 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P00883 |
| UniProtKB/Swiss-Prot Entry Name
| ALDOA_RABIT |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
| General References
| - Putney SD, Herlihy WC, Schimmel P: A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing. Nature. 1983 Apr 21;302(5910):718-21. doi: 10.1038/302718a0. [PubMed:6687628 ]
- Tolan DR, Amsden AB, Putney SD, Urdea MS, Penhoet EE: The complete nucleotide sequence for rabbit muscle aldolase A messenger RNA. J Biol Chem. 1984 Jan 25;259(2):1127-31. [PubMed:6546378 ]
- Sajgo M, Hajos G: The amino acid sequence of rabbit muscle aldolase. Acta Biochim Biophys Acad Sci Hung. 1974;9(3):239-41. [PubMed:4417717 ]
- Lai CY, Nakai N, Chang D: Amino acid sequence of rabbit muscle aldolase and the structure of the active center. Science. 1974 Mar;183(130):1204-6. doi: 10.1126/science.183.4130.1204. [PubMed:4812352 ]
- Benfield PA, Forcina BG, Gibbons I, Perham RN: Extended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver. Biochem J. 1979 Nov 1;183(2):429-44. doi: 10.1042/bj1830429. [PubMed:534504 ]
- Lai CY: Studies on the structure of rabbit muscle aldolase. Determination of the primary structure of the COOH-terminal BrCN peptide; the complete sequence of the subunit polypeptide chain. Arch Biochem Biophys. 1975 Jan;166(1):358-68. doi: 10.1016/0003-9861(75)90398-7. [PubMed:1122142 ]
- Hartman FC, Welch MH: Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate. Biochem Biophys Res Commun. 1974 Mar 15;57(1):85-92. doi: 10.1016/s0006-291x(74)80360-8. [PubMed:4857186 ]
- Hartman FC, Brown JP: Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase. J Biol Chem. 1976 May 25;251(10):3057-62. [PubMed:5453 ]
- Patthy L, Varadi A, Thesz J, Kovacs K: Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography. Eur J Biochem. 1979 Sep;99(2):309-13. doi: 10.1111/j.1432-1033.1979.tb13258.x. [PubMed:499203 ]
- Gizak A, Maciaszczyk E, Dzugaj A, Eschrich K, Rakus D: Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase. Proteins. 2008 Jul;72(1):209-16. doi: 10.1002/prot.21909. [PubMed:18214967 ]
- Blom N, Sygusch J: Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Nat Struct Biol. 1997 Jan;4(1):36-9. doi: 10.1038/nsb0197-36. [PubMed:8989320 ]
- Choi KH, Mazurkie AS, Morris AJ, Utheza D, Tolan DR, Allen KN: Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,). Biochemistry. 1999 Sep 28;38(39):12655-64. doi: 10.1021/bi9828371. [PubMed:10504235 ]
- Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J: A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases. J Biol Chem. 2002 Mar 15;277(11):9474-83. doi: 10.1074/jbc.M107600200. Epub 2002 Jan 4. [PubMed:11779856 ]
- Sherawat M, Tolan DR, Allen KN: Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant. Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):543-50. doi: 10.1107/S0907444908004976. Epub 2008 Apr 19. [PubMed:18453690 ]
- Rangarajan ES, Park H, Fortin E, Sygusch J, Izard T: Mechanism of aldolase control of sorting nexin 9 function in endocytosis. J Biol Chem. 2010 Apr 16;285(16):11983-90. doi: 10.1074/jbc.M109.092049. Epub 2010 Feb 2. [PubMed:20129922 ]
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