Beta-fructosidase

Details

Name
Beta-fructosidase
Synonyms
  • 3.2.1.26
  • Invertase
  • Sucrase
Gene Name
bfrA
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Amino acid sequence
>lcl|BSEQ0017039|Beta-fructosidase
MFKPNYHFFPITGWMNDPNGLIFWKGKYHMFYQYNPRKPEWGNICWGHAVSDDLVHWRHL
PVALYPDDETHGVFSGSAVEKDGKMFLVYTYYRDPTHNKGEKETQCVAMSENGLDFVKYD
GNPVISKPPEEGTHAFRDPKVNRSNGEWRMVLGSGKDEKIGRVLLYTSDDLFHWKYEGVI
FEDETTKEIECPDLVRIGEKDILIYSITSTNSVLFSMGELKEGKLNVEKRGLLDHGTDFY
AAQTFFGTDRVVVIGWLQSWLRTGLYPTKREGWNGVMSLPRELYVENNELKVKPVDELLA
LRKRKVFETAKSGTFLLDVKENSYEIVCEFSGEIELRMGNESEEVVITKSRDELIVDTTR
SGVSGGEVRKSTVEDEATNRIRAFLDSCSVEFFFNDSIAFSFRIHPENVYNILSVKSNQV
KLEVFELENIWL
Number of residues
432
Molecular Weight
49841.065
Theoretical pI
5.1
GO Classification
Functions
sucrose alpha-glucosidase activity
Processes
carbohydrate metabolic process
General Function
Sucrose alpha-glucosidase activity
Specific Function
Hydrolysis of sucrose, raffinose, inulin and levan. Specific for the fructose moiety and the beta-anomeric configuration of the glycosidic linkages of its substrates. The enzyme released fructose from sucrose and raffinose, and the fructose polymer inulin is hydrolyzed quantitatively in an exo-type fashion.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0017040|Beta-fructosidase (bfrA)
ATGTTCAAGCCGAATTATCACTTTTTCCCGATAACAGGCTGGATGAACGATCCGAACGGT
TTGATCTTCTGGAAGGGAAAATATCATATGTTCTATCAGTATAATCCCAGAAAACCTGAG
TGGGGAAACATCTGCTGGGGCCACGCGGTGAGCGACGATCTCGTTCACTGGAGACACCTT
CCCGTTGCTCTATATCCCGACGATGAAACACACGGAGTGTTCTCTGGAAGCGCTGTCGAG
AAAGATGGGAAAATGTTTCTCGTGTACACCTACTACCGCGATCCGACACACAACAAAGGA
GAAAAAGAAACCCAGTGTGTGGCTATGAGTGAAAACGGATTGGATTTCGTAAAGTACGAT
GGAAACCCGGTCATATCTAAACCCCCAGAGGAAGGGACGCACGCCTTCAGAGACCCGAAG
GTGAACAGAAGCAACGGTGAGTGGCGAATGGTACTGGGATCTGGTAAAGATGAGAAGATT
GGAAGAGTGCTTCTCTATACCTCAGATGACCTTTTTCACTGGAAGTACGAGGGTGTGATC
TTCGAAGATGAAACCACAAAAGAAATAGAGTGTCCCGATCTTGTGAGAATTGGAGAGAAA
GATATCCTCATATACTCGATAACGAGTACAAACAGCGTTCTGTTTTCCATGGGAGAGTTA
AAGGAAGGAAAACTGAATGTCGAAAAGCGGGGGCTTCTCGATCACGGAACGGATTTCTAC
GCTGCTCAAACTTTCTTTGGAACAGACAGAGTTGTAGTTATCGGATGGCTTCAAAGCTGG
TTGAGAACAGGGCTTTACCCGACAAAACGAGAAGGATGGAACGGTGTCATGAGTCTTCCT
AGGGAGCTGTATGTAGAAAACAACGAGTTGAAGGTGAAACCGGTGGATGAACTCTTGGCT
CTCAGAAAGAGAAAGGTTTTCGAAACTGCAAAGTCCGGAACATTTCTGCTGGATGTCAAG
GAAAACAGTTATGAAATTGTGTGTGAATTCAGCGGAGAAATCGAACTTCGAATGGGAAAT
GAATCTGAAGAAGTGGTGATAACGAAGAGTCGAGACGAATTAATCGTGGATACAACGAGA
TCTGGTGTTTCAGGTGGAGAAGTTAGAAAGTCGACAGTCGAAGATGAAGCTACAAATAGA
ATACGAGCTTTCTTGGATTCGTGTTCTGTAGAATTTTTCTTCAACGACTCCATAGCTTTT
TCCTTTAGGATCCATCCAGAGAACGTTTACAACATTCTTTCTGTCAAATCGAACCAAGTG
AAACTCGAAGTCTTTGAACTCGAGAACATATGGTTGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO33833
UniProtKB Entry NameBFRA_THEMA
GenBank Gene IDAJ001073
General References
  1. Liebl W, Brem D, Gotschlich A: Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli. Appl Microbiol Biotechnol. 1998 Jul;50(1):55-64. [Article]
  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. [Article]
  3. Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M: The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. [Article]
  4. Alberto F, Jordi E, Henrissat B, Czjzek M: Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochem J. 2006 May 1;395(3):457-62. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04272Citric acidapproved, nutraceutical, vet_approvedunknownDetails