Exoglucanase/xylanase
Details
- Name
- Exoglucanase/xylanase
- Synonyms
- xynB
- Gene Name
- cex
- Organism
- Cellulomonas fimi
- Amino acid sequence
>lcl|BSEQ0010934|Exoglucanase/xylanase MPRTTPAPGHPARGARTALRTTRRRAATLVVGATVVLPAQAATTLKEAADGAGRDFGFAL DPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYG HTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGDGPPQDS AFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDC VGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQ ACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYAKKPAYAAVMEAFGASPTPT PTTPTPTPTTPTPTPTSGPAGCQVLWGVNQWNTGFTANVTVKNTSSAPVDGWTLTFSFPS GQQVTQAWSSTVTQSGSAVTVRNAPWNGSIPAGGTAQFGFNGSHTGTNAAPTAFSLNGTP CTVG
- Number of residues
- 484
- Molecular Weight
- 51290.845
- Theoretical pI
- 6.62
- GO Classification
- Functionscellulose 1,4-beta-cellobiosidase activity / endo-1,4-beta-xylanase activity / polysaccharide bindingProcessescellulose catabolic process / xylan catabolic process
- General Function
- Polysaccharide binding
- Specific Function
- Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity.The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0002658|1455 bp ATGCCTAGGACCACGCCCGCACCCGGCCACCCGGCCCGCGGCGCCCGCACCGCTCTGCGC ACGACGCGCCGCCGCGCGGCGACGCTCGTCGTCGGCGCCACGGTCGTGCTGCCCGCCCAG GCCGCGACCACGCTCAAGGAGGCCGCCGACGGCGCCGGCCGGGACTTCGGCTTCGCGCTC GACCCCAACCGGCTCTCGGAGGCGCAGTACAAGGCGATCGCCGACAGCGAGTTCAACCTC GTCGTCGCCGAGAACGCGATGAAGTGGGACGCCACCGAGCCCTCGCAGAACAGCTTCTCC TTCGGCGCGGGCGACCGCGTCGCGAGCTACGCCGCCGACACCGGCAAGGAGCTGTACGGC CACACGCTCGTCTGGCACTCGCAGCTGCCCGACTGGGCGAAGAACCTCAACGGCTCCGCG TTCGAGAGCGCGATGGTCAACCACGTGACGAAGGTCGCCGACCACTTCGAGGGCAAGGTC GCGTCGTGGGACGTCGTCAACGAGGCGTTCGCCGACGGCGACGGCCCGCCGCAGGACTCG GCGTTCCAGCAGAAGCTCGGCAACGGCTACATCGAGACCGCGTTCCGGGCGGCACGTGCG GCGGACCCGACCGCCAAGCTGTGCATCAACGACTACAACGTCGAGGGCATCAACGCGAAG AGCAACTCGCTCTACGACCTCGTCAAGGACTTCAAGGCGCGCGGCGTCCCGCTCGACTGC GTCGGGTTCCAGTCGCACCTCATCGTCGGCCAGGTGCCGGGCGACTTCCGGCAGAACCTG CAGCGGTTCGCGGACCTGGGCGTGGACGTGCGCATCACCGAGCTCGACATCCGCATGCGG ACGCCCTCCGACGCGACCAAGCTCGCGACCCAGGCGGCCGACTACAAGAAGGTCGTGCAG GCCTGCATGCAGGTGACCCGCTGCCAGGGCGTGACCGTCTGGGGCATCACCGACAAGTAC TCGTGGGTGCCGGACGTCTTCCCGGGCGAGGGGGCCGCGCTGGTGTGGGACGCGAGCTAC GCCAAGAAGCCGGCCTACGCCGCCGTGATGGAGGCCTTCGGCGCGAGCCCGACGCCGACG CCCACCACGCCGACCCCGACGCCCACGACGCCGACGCCGACCCCGACGTCCGGTCCGGCC GGGTGCCAGGTGCTGTGGGGCGTCAACCAGTGGAACACCGGCTTCACCGCGAACGTCACC GTGAAGAACACGTCCTCCGCTCCGGTCGACGGCTGGACGCTCACGTTCAGCTTCCCGTCC GGCCAGCAGGTCACCCAGGCGTGGAGCTCGACGGTCACGCAGTCCGGCTCGGCCGTGACG GTCCGCAACGCCCCGTGGAACGGCTCGATCCCGGCGGGCGGCACCGCGCAGTTCGGCTTC AACGGCTCGCACACGGGCACCAACGCCGCGCCGACGGCGTTCTCGCTCAACGGCACGCCC TGCACGGTCGGCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P07986 UniProtKB Entry Name GUX_CELFI GenBank Protein ID 144425 GenBank Gene ID M15824 - General References
- O'Neill G, Goh SH, Warren RA, Kilburn DG, Miller RC Jr: Structure of the gene encoding the exoglucanase of Cellulomonas fimi. Gene. 1986;44(2-3):325-30. [Article]
- Tull D, Withers SG, Gilkes NR, Kilburn DG, Warren RA, Aebersold R: Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi. J Biol Chem. 1991 Aug 25;266(24):15621-5. [Article]
- Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr: Structural and functional relationships in two families of beta-1,4-glycanases. Eur J Biochem. 1991 Dec 5;202(2):367-77. [Article]
- White A, Withers SG, Gilkes NR, Rose DR: Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi. Biochemistry. 1994 Oct 25;33(42):12546-52. [Article]
- White A, Tull D, Johns K, Withers SG, Rose DR: Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. Nat Struct Biol. 1996 Feb;3(2):149-54. [Article]
- Notenboom V, Birsan C, Warren RA, Withers SG, Rose DR: Exploring the cellulose/xylan specificity of the beta-1,4-glycanase cex from Cellulomonas fimi through crystallography and mutation. Biochemistry. 1998 Apr 7;37(14):4751-8. [Article]
- Notenboom V, Birsan C, Nitz M, Rose DR, Warren RA, Withers SG: Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants. Nat Struct Biol. 1998 Sep;5(9):812-8. [Article]
- Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS: Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy. Biochemistry. 1995 May 30;34(21):6993-7009. [Article]
- MacLeod AM, Lindhorst T, Withers SG, Warren RA: The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants. Biochemistry. 1994 May 24;33(20):6371-6. [Article]
- Notenboom V, Williams SJ, Hoos R, Withers SG, Rose DR: Detailed structural analysis of glycosidase/inhibitor interactions: complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-sugars. Biochemistry. 2000 Sep 26;39(38):11553-63. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01921 Xylose-derived lactam oxime experimental unknown Details DB02374 Xylose-Derived Imidazole experimental unknown Details DB03389 alpha-D-Xylopyranose experimental unknown Details DB03717 3-Hydroxy-4-(3,4,5-trihydroxy-tetrahydro-pyran-2-yloxy)-piperidin-2-one experimental unknown Details DB02379 Beta-D-Glucose experimental unknown Details DB04282 2-deoxy-2-fluoro-α-D-glucose experimental unknown Details