Alpha-glucosidase

Details

Name
Alpha-glucosidase
Synonyms
  • 3.2.1.20
  • Maltase
Gene Name
aglA
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Amino acid sequence
>lcl|BSEQ0011811|Alpha-glucosidase
MPSVKIGIIGAGSAVFSLRLVSDLCKTPGLSGSTVTLMDIDEERLDAILTIAKKYVEEVG
ADLKFEKTMNLDDVIIDADFVINTAMVGGHTYLEKVRQIGEKYGYYRGIDAQEFNMVSDY
YTFSNYNQLKYFVDIARKIEKLSPKAWYLQAANPIFEGTTLVTRTVPIKAVGFCHGHYGV
MEIVEKLGLEEEKVDWQVAGVNHGIWLNRFRYNGGNAYPLLDKWIEEKSKDWKPENPFND
QLSPAAIDMYRFYGVMPIGDTVRNSSWRYHRDLETKKKWYGEPWGGADSEIGWKWYQDTL
GKVTEITKKVAKFIKENPSVRLSDLGSVLGKDLSEKQFVLEVEKILDPERKSGEQHIPFI
DALLNDNKARFVVNIPNKGIIHGIDDDVVVEVPALVDKNGIHPEKIEPPLPDRVVKYYLR
PRIMRMEMALEAFLTGDIRIIKELLYRDPRTKSDEQVEKVIEEILALPENEEMRKHYLKR
Number of residues
480
Molecular Weight
55046.815
Theoretical pI
5.75
GO Classification
Functions
alpha-1,4-glucosidase activity / maltose alpha-glucosidase activity / metal ion binding / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
General Function
Oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
Specific Function
Alpha-glycosidase with a very broad specificity. Hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch. AglA is not specific with respect to the configuration at the C-4 position of its substrates because glycosidic derivatives of D-galactose are also hydrolyzed. Does not cleave beta-glycosidic bonds.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0011812|Alpha-glucosidase (aglA)
ATGCCATCTGTGAAGATCGGTATCATCGGTGCGGGGAGCGCGGTGTTTTCTCTGAGGCTT
GTGAGTGATCTTTGCAAAACGCCGGGACTCTCTGGCAGCACGGTCACCCTCATGGATATC
GACGAAGAAAGACTCGACGCTATTCTGACCATCGCGAAAAAATACGTTGAAGAAGTGGGA
GCGGATCTGAAATTCGAAAAAACCATGAATTTAGATGACGTCATCATCGACGCGGATTTT
GTGATAAACACAGCGATGGTGGGTGGCCATACCTACTTGGAGAAGGTCAGACAGATCGGT
GAGAAATACGGCTACTACAGAGGAATAGACGCTCAGGAGTTTAACATGGTCTCCGACTAC
TACACCTTCTCCAACTACAACCAGCTCAAGTACTTCGTTGACATAGCAAGGAAGATAGAG
AAGCTCTCCCCAAAAGCCTGGTACTTGCAGGCAGCGAACCCCATTTTCGAGGGAACAACC
CTTGTGACAAGAACGGTTCCCATAAAGGCAGTGGGATTCTGCCATGGACACTACGGCGTG
ATGGAGATCGTAGAGAAACTGGGGCTGGAAGAAGAAAAAGTAGATTGGCAGGTCGCAGGA
GTGAACCACGGTATCTGGCTGAATAGGTTCAGATACAACGGGGGGAACGCGTATCCCCTC
CTTGACAAGTGGATCGAGGAAAAATCAAAAGATTGGAAACCAGAGAACCCCTTCAACGAC
CAGCTCTCTCCCGCCGCGATAGACATGTACAGATTCTACGGTGTGATGCCCATCGGTGAC
ACCGTGAGAAACTCTTCGTGGAGGTACCACAGGGATCTTGAAACCAAGAAGAAGTGGTAC
GGTGAACCCTGGGGAGGAGCAGATTCTGAAATAGGCTGGAAATGGTACCAAGACACGCTT
GGAAAGGTCACGGAGATCACAAAGAAGGTGGCAAAGTTCATCAAAGAAAATCCGTCCGTG
AGGCTCTCCGACCTTGGAAGTGTTCTGGGGAAAGACCTCTCAGAAAAGCAGTTTGTGCTC
GAAGTGGAGAAAATTCTCGATCCAGAAAGAAAGAGTGGAGAGCAGCACATCCCATTCATC
GATGCGCTGCTGAACGATAACAAGGCAAGATTCGTGGTGAACATACCAAATAAAGGTATC
ATTCACGGAATAGACGATGACGTGGTTGTTGAAGTCCCAGCCCTTGTGGACAAGAACGGA
ATCCATCCCGAGAAGATCGAACCACCGCTTCCAGATCGCGTGGTCAAGTACTACCTGAGA
CCCAGAATCATGAGGATGGAAATGGCTCTGGAGGCGTTTCTAACGGGTGACATAAGGATC
ATAAAAGAACTTCTCTACAGAGATCCAAGGACAAAGAGCGATGAACAGGTAGAAAAGGTG
ATCGAGGAGATCCTCGCACTTCCAGAAAACGAAGAGATGCGGAAACATTATCTGAAGAGA
TGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO33830
UniProtKB Entry NameAGLA_THEMA
GenBank Gene IDAJ001089
General References
  1. Bibel M, Brettl C, Gosslar U, Kriegshauser G, Liebl W: Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima. FEMS Microbiol Lett. 1998 Jan 1;158(1):9-15. [PubMed:9453151]
  2. Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [PubMed:10360571]
  3. Raasch C, Streit W, Schanzer J, Bibel M, Gosslar U, Liebl W: Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and thiol-dependent alpha-glucosidase. Extremophiles. 2000 Aug;4(4):189-200. [PubMed:10972187]
  4. Raasch C, Armbrecht M, Streit W, Hocker B, Strater N, Liebl W: Identification of residues important for NAD+ binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett. 2002 Apr 24;517(1-3):267-71. [PubMed:12062450]
  5. Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N: Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases. J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. [PubMed:12588867]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03323Maltoseexperimental, investigationalunknownDetails