Hmdb loader
Identification
HMDB Protein ID HMDBP13137
Secondary Accession Numbers None
Name Fructose-bisphosphate aldolase A
Synonyms
  1. 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
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
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. 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 ]
  10. 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 ]
  11. 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 ]
  12. 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 ]
  13. 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 ]
  14. 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 ]
  15. 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 ]