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
- Functionsalpha-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
Resource Link UniProtKB ID O33830 UniProtKB Entry Name AGLA_THEMA GenBank Gene ID AJ001089 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]