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Identification
HMDB Protein ID HMDBP00979
Secondary Accession Numbers
  • 6267
Name Fructose-bisphosphate aldolase C
Synonyms
  1. Brain-type aldolase
Gene Name ALDOC
Protein Type Enzyme
Biological Properties
General Function Involved in fructose-bisphosphate aldolase activity
Specific Function Not Available
Pathways
  • Fructose and mannose metabolism
  • glycolysis
  • Glycolysis / Gluconeogenesis
  • Pentose phosphate pathway
Reactions
Fructose 1,6-bisphosphate → Dihydroxyacetone phosphate + D-Glyceraldehyde 3-phosphate details
beta-D-Fructose 1,6-bisphosphate → Dihydroxyacetone phosphate + D-Glyceraldehyde 3-phosphate details
Sedoheptulose 1,7-bisphosphate → Dihydroxyacetone phosphate + D-Erythrose 4-phosphate details
Fructose 1-phosphate → Dihydroxyacetone phosphate + Glyceraldehyde details
GO Classification
Biological Process
small molecule metabolic process
fructose 1,6-bisphosphate metabolic process
fructose metabolic process
apoptotic process
organ regeneration
protein heterotetramerization
response to organic nitrogen
glycolysis
gluconeogenesis
aging
protein homotetramerization
response to organic cyclic compound
response to hypoxia
Cellular Component
cytosol
cytoskeleton
mitochondrion
axon
Function
catalytic activity
lyase activity
carbon-carbon lyase activity
aldehyde-lyase activity
fructose-bisphosphate aldolase activity
Molecular Function
fructose-bisphosphate aldolase activity
cytoskeletal protein binding
Process
metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
glucose catabolic process
glycolysis
Cellular Location Not Available
Gene Properties
Chromosome Location 17
Locus 17cen-q12
SNPs ALDOC
Gene Sequence
>1095 bp
ATGCCTCACTCGTACCCAGCCCTTTCTGCTGAGCAGAAGAAGGAGTTGTCTGACATTGCC
CTGCGGATTGTAGCCCCGGGCAAAGGCATTCTGGCTGCGGATGAGTCTGTAGGCAGCATG
GCCAAGCGGCTGAGCCAAATTGGGGTGGAAAACACAGAGGAGAACCGCCGGCTGTACCGC
CAGGTCCTGTTCAGTGCTGATGACCGTGTGAAAAAGTGCATTGGAGGCGTCATTTTCTTC
CATGAGACCCTCTACCAGAAAGATGATAATGGTGTTCCCTTCGTCCGAACCATCCAGGAT
AAGGGCATCGTCGTGGGCATCAAGGTTGACAAGGGTGTGGTGCCTCTAGCTGGGACTGAT
GGAGAAACCACCACTCAAGGGCTGGATGGGCTCTCAGAACGCTGTGCCCAATACAAGAAG
GATGGTGCTGACTTTGCCAAGTGGCGCTGTGTGCTGAAAATCAGTGAGCGTACACCCTCT
GCACTTGCCATTCTGGAGAACGCCAACGTGCTGGCCCGTTATGCCAGTATCTGCCAGCAG
AATGGCATTGTGCCTATTGTGGAACCTGAAATATTGCCTGATGGAGACCACGACCTCAAA
CGTTGTCAGTATGTTACAGAGAAGGTCTTGGCTGCTGTGTACAAGGCCCTGAGTGACCAT
CATGTATACCTGGAGGGGACCCTGCTCAAGCCCAACATGGTGACCCCGGGCCATGCCTGT
CCCATCAAGTATACCCCAGAGGAGATTGCCATGGCAACTGTCACTGCCCTGCGTCGCACT
GTGCCCCCAGCTGTCCCAGGAGTGACCTTCCTGTCTGGGGGTCAGAGCGAAGAAGAGGCA
TCATTCAACCTCAATGCCATCAACCGCTGCCCCCTTCCCCGACCCTGGGCGCTTACCTTC
TCCTATGGGCGTGCCCTGCAAGCCTCTGCACTCAATGCCTGGCGAGGGCAACGGGACAAT
GCTGGGGCTGCCACTGAGGAGTTCATCAAGCGGGCTGAGGTGAATGGGCTTGCAGCCCAG
GGCAAGTATGAAGGCAGTGGAGAAGATGGTGGAGCAGCAGCACAGTCACTCTACATTGCC
AACCATGCCTACTGA
Protein Properties
Number of Residues 364
Molecular Weight 39455.505
Theoretical pI 6.866
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Fructose-bisphosphate aldolase C
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYR
QVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTD
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHAC
PIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTF
SYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIA
NHAY
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P09972
UniProtKB/Swiss-Prot Entry Name ALDOC_HUMAN
PDB IDs
GenBank Gene ID AF054987
GeneCard ID ALDOC
GenAtlas ID ALDOC
HGNC ID HGNC:418
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed:16916647 ]
  5. Rottmann WH, Deselms KR, Niclas J, Camerato T, Holman PS, Green CJ, Tolan DR: The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones. Biochimie. 1987 Feb;69(2):137-45. [PubMed:3105602 ]
  6. Buono P, Paolella G, Mancini FP, Izzo P, Salvatore F: The complete nucleotide sequence of the gene coding for the human aldolase C. Nucleic Acids Res. 1988 May 25;16(10):4733. [PubMed:3267224 ]
  7. Buono P, Mancini FP, Izzo P, Salvatore F: Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene. Eur J Biochem. 1990 Sep 24;192(3):805-11. [PubMed:2209624 ]
  8. Lu M, Holliday LS, Zhang L, Dunn WA Jr, 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;276(32):30407-13. Epub 2001 Jun 8. [PubMed:11399750 ]
  9. Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH: Phospholipase D2 directly interacts with aldolase via Its PH domain. Biochemistry. 2002 Mar 12;41(10):3414-21. [PubMed:11876650 ]
  10. Arakaki TL, Pezza JA, Cronin MA, Hopkins CE, Zimmer DB, Tolan DR, Allen KN: Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function. Protein Sci. 2004 Dec;13(12):3077-84. Epub 2004 Nov 10. [PubMed:15537755 ]