Beta-fructosidase

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	None
Molecular Weight	49841.065
Theoretical pI	5.1
GO Classification	Functions sucrose alpha-glucosidase activity Processes carbohydrate metabolic process Components
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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	O33833
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	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. [9720201 ] 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. [10360571 ] 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. [14973124 ] 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. [16411890 ]

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