Fructose-bisphosphate aldolase class 2
Details
- Name
- Fructose-bisphosphate aldolase class 2
- Kind
- protein
- Synonyms
- 4.1.2.13
- fba
- FBP aldolase
- fda
- Fructose-1,6-bisphosphate aldolase
- Fructose-bisphosphate aldolase class II
- Gene Name
- fbaA
- UniProtKB Entry
- P0AB71Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016648|Fructose-bisphosphate aldolase class 2 MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQ FSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWI DGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTG GEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPT ILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGV LNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
- Number of residues
- 359
- Molecular Weight
- 39147.03
- Theoretical pI
- 5.72
- GO Classification
- Functionsfructose-bisphosphate aldolase activity / zinc ion bindingProcessesglycolytic processComponentscytosol
- General Function
- Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (PubMed:10712619). In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphosphate bypass pathway (PubMed:19756045). Catalyzes the cleavage of D-sedoheptulose 1,7-bisphosphate to glyceraldehyde 3-phosphate and erythrose 4-phosphate (PubMed:19756045).
- Specific Function
- fructose-bisphosphate aldolase activity
- Pfam Domain Function
- F_bP_aldolase (PF01116)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016649|Fructose-bisphosphate aldolase class 2 (fbaA) ATGTCTAAGATTTTTGATTTCGTAAAACCTGGCGTAATCACTGGTGATGACGTACAGAAA GTTTTCCAGGTAGCAAAAGAAAACAACTTCGCACTGCCAGCAGTAAACTGCGTCGGTACT GACTCCATCAACGCCGTACTGGAAACCGCTGCTAAAGTTAAAGCGCCGGTTATCGTTCAG TTCTCCAACGGTGGTGCTTCCTTTATCGCTGGTAAAGGCGTGAAATCTGACGTTCCGCAG GGTGCTGCTATCCTGGGCGCGATCTCTGGTGCGCATCACGTTCACCAGATGGCTGAACAT TATGGTGTTCCGGTTATCCTGCACACTGACCACTGCGCGAAGAAACTGCTGCCGTGGATC GACGGTCTGTTGGACGCGGGTGAAAAACACTTCGCAGCTACCGGTAAGCCGCTGTTCTCT TCTCACATGATCGACCTGTCTGAAGAATCTCTGCAAGAGAACATCGAAATCTGCTCTAAA TACCTGGAGCGCATGTCCAAAATCGGCATGACTCTGGAAATCGAACTGGGTTGCACCGGT GGTGAAGAAGACGGCGTGGACAACAGCCACATGGACGCTTCTGCACTGTACACCCAGCCG GAAGACGTTGATTACGCATACACCGAACTGAGCAAAATCAGCCCGCGTTTCACCATCGCA GCGTCCTTCGGTAACGTACACGGTGTTTACAAGCCGGGTAACGTGGTTCTGACTCCGACC ATCCTGCGTGATTCTCAGGAATATGTTTCCAAGAAACACAACCTGCCGCACAACAGCCTG AACTTCGTATTCCACGGTGGTTCCGGTTCTACTGCTCAGGAAATCAAAGACTCCGTAAGC TACGGCGTAGTAAAAATGAACATCGATACCGATACCCAATGGGCAACCTGGGAAGGCGTT CTGAACTACTACAAAGCGAACGAAGCTTATCTGCAGGGTCAGCTGGGTAACCCGAAAGGC GAAGATCAGCCGAACAAGAAATACTACGATCCGCGCGTATGGCTGCGTGCCGGTCAGACT TCGATGATCGCTCGTCTGGAGAAAGCATTCCAGGAACTGAACGCGATCGACGTTCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AB71 UniProtKB Entry Name ALF_ECOLI GenBank Gene ID X14436 PDB ID(s) 1B57, 1DOS, 1GYN, 1ZEN KEGG ID ecj:JW2892 NCBI Gene ID 947415 - General References
- Alefounder PR, Perham RN: Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli. Mol Microbiol. 1989 Jun;3(6):723-32. [Article]
- Alefounder PR, Baldwin SA, Perham RN, Short NJ: Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Biochem J. 1989 Jan 15;257(2):529-34. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
- Berry A, Marshall KE: Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 1993 Feb 22;318(1):11-6. [Article]
- Zgiby SM, Thomson GJ, Qamar S, Berry A: Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases. Eur J Biochem. 2000 Mar;267(6):1858-68. [Article]
- Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
- Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. doi: 10.1074/mcp.M111.012658. Epub 2011 Sep 9. [Article]
- Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y: Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol. 2011 Jan;7(1):58-63. doi: 10.1038/nchembio.495. Epub 2010 Dec 12. [Article]
- Blom NS, Tetreault S, Coulombe R, Sygusch J: Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat Struct Biol. 1996 Oct;3(10):856-62. [Article]
- Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN: The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Structure. 1996 Nov 15;4(11):1303-15. [Article]
- Hall DR, Leonard GA, Reed CD, Watt CI, Berry A, Hunter WN: The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity. J Mol Biol. 1999 Mar 26;287(2):383-94. [Article]
- Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN: The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase. Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):611-4. Epub 2003 Feb 21. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Phosphoglycolohydroxamic Acid experimental unknown target Details