Alpha-amylase

Details

Name
Alpha-amylase
Synonyms
  • 1,4-alpha-D-glucan glucanohydrolase
  • 3.2.1.1
Gene Name
Not Available
Organism
Bacillus amyloliquefaciens
Amino acid sequence
>lcl|BSEQ0016542|Alpha-amylase
MIQKRKRTVSFRLVLMCTLLFVSLPITKTSAVNGTLMQYFEWYTPNDGQHWKRLQNDAEH
LSDIGITAVWIPPAYKGLSQSDNGYGPYDLYDLGEFQQKGTVRTKYGTKSELQDAIGSLH
SRNVQVYGDVVLNHKAGADATEDVTAVEVNPANRNQETSEEYQIKAWTDFRFPGRGNTYS
DFKWHWYHFDGADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYADVDYDHPDVV
AETKKWGIWYANELSLDGFRIDAAKHIKFSFLRDWVQAVRQATGKEMFTVAEYWQNNAGK
LENYLNKTSFNQSVFDVPLHFNLQAASSQGGGYDMRRLLDGTVVSRHPEKAVTFVENHDT
QPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGTSPKEIPSLKDNIEPILK
ARKEYAYGPQHDYIDHPDVIGWTREGDSSAAKSGLAALITDGPGGSKRMYAGLKNAGETW
YDITGNRSDTVKIGSDGWGEFHVNDGSVSIYVQK
Number of residues
514
Molecular Weight
58402.605
Theoretical pI
6.04
GO Classification
Functions
alpha-amylase activity / calcium ion binding
Processes
carbohydrate metabolic process
Components
extracellular region
General Function
Calcium ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0003437|1545 bp
ATGATTCAAAAACGAAAGCGGACAGTTTCGTTCAGACTTGTGCTTATGTGCACGCTGTTA
TTTGTCAGTTTGCCGATTACAAAAACATCAGCCGTAAATGGCACGCTGATGCAGTATTTT
GAATGGTATACGCCGAACGACGGCCAGCATTGGAAACGATTGCAGAATGATGCGGAACAT
TTATCGGATATCGGAATCACTGCCGTCTGGATTCCTCCCGCATACAAAGGATTGAGCCAA
TCCGATAACGGATACGGACCTTATGATTTGTATGATTTAGGAGAATTCCAGCAAAAAGGG
ACGGTCAGAACGAAATACGGCACAAAATCAGAGCTTCAAGATGCGATCGGCTCACTGCAT
TCCCGGAACGTCCAAGTATACGGAGATGTGGTTTTGAATCATAAGGCTGGTGCTGATGCA
ACAGAAGATGTAACTGCCGTCGAAGTCAATCCGGCCAATAGAAATCAGGAAACTTCGGAG
GAATATCAAATCAAAGCGTGGACGGATTTTCGTTTTCCGGGCCGTGGAAACACGTACAGT
GATTTTAAATGGCATTGGTATCATTTCGACGGAGCGGACTGGGATGAATCCCGGAAGATC
AGCCGCATCTTTAAGTTTCGTGGGGAAGGAAAAGCGTGGGATTGGGAAGTATCAAGTGAA
AACGGCAACTATGACTATTTAATGTATGCTGATGTTGACTACGACCACCCTGATGTCGTG
GCAGAGACAAAAAAATGGGGTATCTGGTATGCGAATGAACTGTCATTAGACGGCTTCCGT
ATTGATGCCGCCAAACATATTAAATTTTCATTTCTGCGTGATTGGGTTCAGGCGGTCAGA
CAGGCGACGGGAAAAGAAATGTTTACGGTTGCGGAGTATTGGCAGAATAATGCCGGGAAA
CTCGAAAACTACTTGAATAAAACAAGCTTTAATCAATCCGTGTTTGATGTTCCGCTTCAT
TTCAATTTACAGGCGGCTTCCTCACAAGGAGGCGGATATGATATGAGGCGTTTGCTGGAC
GGTACCGTTGTGTCCAGGCATCCGGAAAAGGCGGTTACATTTGTTGAAAATCATGACACA
CAGCCGGGACAGTCATTGGAATCGACAGTCCAAACTTGGTTTAAACCGCTTGCATACGCC
TTTATTTTGACAAGAGAATCCGGTTATCCTCAGGTGTTCTATGGGGATATGTACGGGACA
AAAGGGACATCGCCAAAGGAAATTCCCTCACTGAAAGATAATATAGAGCCGATTTTAAAA
GCGCGTAAGGAGTACGCATACGGGCCCCAGCACGATTATATTGACCACCCGGATGTGATC
GGATGGACGAGGGAAGGTGACAGCTCCGCCGCCAAATCAGGTTTGGCCGCTTTAATCACG
GACGGACCCGGCGGATCAAAGCGGATGTATGCCGGCCTGAAAAATGCCGGCGAGACATGG
TATGACATAACGGGCAACCGTTCAGATACTGTAAAAATCGGATCTGACGGCTGGGGAGAG
TTTCATGTAAACGATGGGTCCGTCTCCATTTATGTTCAGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00692
UniProtKB Entry NameAMY_BACAM
GenBank Protein ID142429
GenBank Gene IDJ01542
General References
  1. Takkinen K, Pettersson RF, Kalkkinen N, Palva I, Soderlund H, Kaariainen L: Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem. 1983 Jan 25;258(2):1007-13. [Article]
  2. Palva I, Pettersson RF, Kalkkinen N, Lehtovaara P, Sarvas M, Soderlund H, Takkinen K, Kaariainen L: Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the alpha-amylase gene from Bacillus amyloliquefaciens. Gene. 1981 Oct;15(1):43-51. [Article]
  3. Ruohonen L, Hackman P, Lehtovaara P, Knowles JK, Keranen S: Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by [corrected] its own signal peptide from Saccharomyces cerevisiae host cells [corrected]. Gene. 1987;59(2-3):161-70. [Article]
  4. Chung H, Friedberg F: Sequence of the N-terminal half of Bacillus amyloliquefaciens alpha-amylase. Biochem J. 1980 Feb 1;185(2):387-95. [Article]
  5. Brzozowski AM, Lawson DM, Turkenburg JP, Bisgaard-Frantzen H, Svendsen A, Borchert TV, Dauter Z, Wilson KS, Davies GJ: Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes. Biochemistry. 2000 Aug 8;39(31):9099-107. [Article]
  6. Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ: Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):121-9. doi: 10.1107/S1744309109051938. Epub 2010 Jan 26. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03773alpha-D-quinovopyranoseexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails