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
Functions
cellulose 1,4-beta-cellobiosidase activity / endo-1,4-beta-xylanase activity / polysaccharide binding
Processes
cellulose 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
ResourceLink
UniProtKB IDP07986
UniProtKB Entry NameGUX_CELFI
GenBank Protein ID144425
GenBank Gene IDM15824
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01921Xylose-derived lactam oximeexperimentalunknownDetails
DB02374Xylose-Derived ImidazoleexperimentalunknownDetails
DB03389alpha-D-XylopyranoseexperimentalunknownDetails
DB037173-Hydroxy-4-(3,4,5-trihydroxy-tetrahydro-pyran-2-yloxy)-piperidin-2-oneexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails
DB042822-deoxy-2-fluoro-α-D-glucoseexperimentalunknownDetails