Alpha-amylase

Details

Name
Alpha-amylase
Synonyms
  • 1,4-alpha-D-glucan glucanohydrolase
  • 3.2.1.1
Gene Name
amy
Organism
Pseudoalteromonas haloplanktis
Amino acid sequence
>lcl|BSEQ0011154|Alpha-amylase
MKLNKIITTAGLSLGLLLPSIATATPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSP
PNEHITGSQWWTRYQPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGT
GTAGNSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASNYVQNTI
AAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQEVIDQGGEAVGASEYLS
TGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGFMPSSSAVVFVDNHDNQRGHGGAGNVI
TFEDGRLYDLANVFMLAYPYGYPKVMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCE
HRWSYIAGGVDFRNNTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDM
ASGQYCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLNTSSASSTE
SDWQRTVIFINAQTQSGQDMFIRGGIDHAYANANLGRNCQTSNFECAMPIRHNNLKNVTT
SPWKANDNYLDWYGIENGQSSEAEGSATDWTTNVWPAGWGAEKTVNTDGFGVTPLNIWGE
HYWMLDVDMDCSKAVNGWFELKAFIKNGQGWETAIAQDNAPYTSTNHMAQCGKINKFEFN
NSGVVIRSF
Number of residues
669
Molecular Weight
73267.4
Theoretical pI
4.7
GO Classification
Functions
alpha-amylase activity / metal ion binding
Processes
carbohydrate metabolic process
General Function
Metal ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0003223|2010 bp
ATGAAACTCAATAAAATAATCACCACCGCAGGTTTAAGCCTAGGGTTGCTCTTACCTAGC
ATTGCGACTGCTACGCCCACCACATTTGTACATTTGTTTGAATGGAATTGGCAAGATGTA
GCGCAAGAATGTGAGCAATACCTAGGACCAAAAGGCTACGCTGCAGTACAGGTCTCGCCA
CCTAATGAGCACATTACAGGAAGCCAATGGTGGACACGTTATCAGCCAGTAAGTTATGAA
CTGCAAAGTCGTGGCGGAAACCGTGCACAGTTTATCGATATGGTAAATCGCTGTAGTGCA
GCTGGGGTTGATATTTACGTTGATACGCTTATTAACCATATGGCAGCAGGAAGTGGCACA
GGCACGGCGGGAAATAGCTTTGGTAATAAAAGCTTTCCTATTTATAGCCCACAAGATTTT
CATGAAAGTTGTACCATTAATAACTCTGATTATGGCAACGATCGCTACCGAGTACAAAAC
TGTGAACTAGTTGGACTTGCCGATTTAGATACCGCTTCAAACTATGTGCAAAATACCATT
GCAGCATATATTAACGACTTACAAGCTATTGGCGTAAAAGGCTTTCGGTTTGATGCTTCT
AAACATGTTGCAGCAAGCGATATCCAAAGTTTAATGGCCAAAGTAAATGGCTCGCCAGTG
GTTTTTCAAGAAGTGATCGATCAAGGTGGGGAGGCTGTTGGTGCCTCTGAATATTTAAGC
ACAGGTTTAGTAACTGAATTTAAATATAGCACTGAGCTTGGTAACACTTTTAGAAACGGC
TCGCTTGCATGGCTGAGTAATTTTGGCGAAGGGTGGGGCTTTATGCCAAGCTCTTCTGCG
GTGGTTTTTGTAGACAATCACGACAATCAGCGCGGGCACGGCGGCGCTGGCAATGTTATT
ACCTTTGAAGATGGCCGCTTATATGACTTAGCCAATGTATTTATGTTGGCTTATCCGTAC
GGTTATCCAAAAGTAATGTCGAGTTATGATTTTCATGGTGATACAGATGCTGGTGGGCCA
AATGTACCGGTACATAATAATGGTAACTTAGAGTGTTTTGCGAGTAATTGGAAGTGTGAG
CATCGCTGGTCATATATTGCAGGCGGGGTCGATTTTAGAAATAACACCGCCGACAACTGG
GCAGTAACAAATTGGTGGGATAACACAAATAATCAAATTTCATTTGGCCGAGGTAGCTCG
GGTCATATGGCTATTAACAAAGAAGACTCAACACTTACTGCAACTGTGCAAACCGATATG
GCGTCAGGGCAATACTGTAATGTGCTAAAAGGCGAACTGTCAGCTGATGCTAAAAGTTGT
AGTGGTGAGGTTATAACGGTTAATTCCGACGGTACTATTAATCTTAATATTGGCGCTTGG
GATGCGATGGCAATTCATAAAAATGCCAAGTTAAATACCAGTTCTGCCTCAAGCACTGAA
AGTGACTGGCAGCGAACGGTTATTTTTATTAATGCACAAACACAAAGCGGACAAGATATG
TTTATCCGTGGTGGAATTGACCACGCTTATGCAAACGCAAACCTTGGTCGAAATTGCCAA
ACAAGTAATTTTGAGTGTGCAATGCCTATTCGTCATAACAATTTAAAAAATGTCACAACA
AGCCCTTGGAAAGCAAATGATAACTACCTTGATTGGTATGGTATAGAAAATGGGCAAAGT
AGCGAAGCAGAAGGTTCTGCTACCGACTGGACAACGAACGTTTGGCCAGCAGGTTGGGGC
GCTGAAAAAACGGTAAACACAGATGGTTTTGGTGTGACACCTTTAAATATATGGGGCGAA
CACTATTGGATGCTTGATGTAGATATGGATTGCAGTAAAGCGGTTAATGGATGGTTTGAA
CTAAAAGCATTCATTAAAAATGGCCAAGGATGGGAGACTGCCATTGCACAAGACAATGCA
CCTTATACAAGTACTAATCATATGGCGCAATGCGGAAAAATTAATAAATTTGAGTTTAAT
AATTCAGGTGTAGTAATTCGTAGTTTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP29957
UniProtKB Entry NameAMY_PSEHA
GenBank Protein ID2879820
GenBank Gene IDX58627
General References
  1. Feller G, Lonhienne T, Deroanne C, Libioulle C, Van Beeumen J, Gerday C: Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J Biol Chem. 1992 Mar 15;267(8):5217-21. [Article]
  2. Feller G, D'Amico S, Benotmane AM, Joly F, Van Beeumen J, Gerday C: Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis. J Biol Chem. 1998 May 15;273(20):12109-15. [Article]
  3. Aghajari N, Feller G, Gerday C, Haser R: Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 1998 Mar;7(3):564-72. [Article]
  4. Aghajari N, Roth M, Haser R: Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase. Biochemistry. 2002 Apr 2;41(13):4273-80. [Article]
  5. Aghajari N, Feller G, Gerday C, Haser R: Structural basis of alpha-amylase activation by chloride. Protein Sci. 2002 Jun;11(6):1435-41. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails
DB041644,6-Dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxo-2-cyclohexen-1-yl]amino}-α-D-xylo-hex-5-enopyranoseexperimentalunknownDetails