Endo-1,4-beta-xylanase
Details
- Name
- Endo-1,4-beta-xylanase
- Synonyms
- EC 3.2.1.8
- Endo-1,4-beta-xylanase precursor
- Gene Name
- xyl
- Organism
- Pseudoalteromonas haloplanktis
- Amino acid sequence
>lcl|BSEQ0016977|Endo-1,4-beta-xylanase MKVFFKITTLLLILISYQSLAAFNNNPSSVGAYSSGTYRNLAQEMGKTNIQQKVNSTFDN MFGYNNTQQLYYPYTENGVYKAHYIKAINPDEGDDIRTEGQSWGMTAAVMLNKQEEFDNL WRFAKAYQKNPDNHPDAKKQGVYAWKLKLNQNGFVYKVDEGPAPDGEEYFAFALLNASAR WGNSGEFNYYNDAITMLNTIKNKLMENQIIRFSPYIDNLTDPSYHIPAFYDYFANNVTNQ ADKNYWRQVATKSRTLLKNHFTKVSGSPHWNLPTFLSRLDGSPVIGYIFNGQANPGQWYE FDAWRVIMNVGLDAHLMGAQAWHKSAVNKALGFLSYAKTNNSKNCYEQVYSYGGAQNRGC AGEGQKAANAVALLASTNAGQANEFFNEFWSLSQPTGDYRYYNGSLYMLAMLHVSGNFKF YNNTFN
- Number of residues
- 426
- Molecular Weight
- 48406.805
- Theoretical pI
- 8.67
- GO Classification
- Functionsendo-1,4-beta-xylanase activityProcessesxylan catabolic process
- General Function
- Endo-1,4-beta-xylanase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Glyco_hydro_8 (PF01270)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0006002|1281 bp ATGAAAGTATTTTTTAAAATAACAACTTTATTGTTAATACTAATAAGCTATCAATCACTT GCTGCATTTAATAATAACCCATCGAGTGTAGGCGCCTACAGTTCAGGGACATACCGTAAC CTCGCACAAGAAATGGGTAAAACAAATATACAGCAAAAGGTGAATAGTACTTTTGACAAT ATGTTTGGCTATAACAACACACAACAACTTTACTACCCGTACACCGAAAACGGTGTTTAT AAAGCACACTACATAAAAGCAATTAACCCAGACGAAGGCGACGATATAAGAACAGAAGGG CAATCGTGGGGAATGACCGCCGCTGTCATGCTTAATAAACAAGAAGAATTTGATAACCTA TGGCGCTTTGCAAAAGCGTATCAAAAAAATCCAGACAATCACCCTGATGCTAAAAAACAA GGCGTTTACGCGTGGAAACTAAAGCTTAATCAAAACGGCTTTGTTTATAAAGTGGATGAG GGCCCCGCTCCCGATGGCGAAGAGTACTTTGCGTTTGCACTACTTAATGCCTCTGCTCGT TGGGGGAATTCGGGTGAGTTTAACTACTACAACGATGCCATTACCATGTTAAACACAATT AAAAATAAGCTGATGGAAAACCAAATAATCCGCTTTTCACCTTACATTGATAACCTAACA GACCCTTCTTACCATATACCTGCGTTTTACGACTACTTTGCAAATAACGTAACTAACCAA GCAGACAAAAATTACTGGCGACAAGTAGCCACAAAAAGTAGAACCTTACTTAAAAACCAT TTTACAAAAGTAAGTGGTAGCCCGCATTGGAACTTACCTACATTTTTATCGCGCTTAGAT GGCAGCCCTGTTATTGGCTACATTTTTAACGGCCAAGCAAACCCAGGTCAATGGTATGAA TTTGATGCATGGCGCGTAATTATGAATGTGGGTTTAGACGCGCATTTAATGGGTGCTCAA GCGTGGCATAAAAGTGCAGTTAATAAAGCACTGGGCTTTTTAAGTTATGCAAAAACAAAC AACAGTAAAAACTGTTACGAGCAAGTGTATTCGTACGGTGGAGCGCAAAACAGAGGCTGT GCAGGCGAAGGTCAAAAAGCCGCGAATGCAGTAGCGTTACTTGCTTCAACAAATGCTGGG CAAGCAAATGAGTTTTTTAACGAATTTTGGTCTTTATCGCAACCAACGGGTGACTACCGT TACTATAATGGTTCGTTATATATGTTAGCTATGCTGCATGTATCGGGCAATTTTAAGTTT TATAACAACACGTTTAATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8RJN8 UniProtKB Entry Name Q8RJN8_PSEHA GenBank Gene ID AJ427921 - General References
- Van Petegem F, Collins T, Meuwis MA, Gerday C, Feller G, Van Beeumen J: The structure of a cold-adapted family 8 xylanase at 1.3 A resolution. Structural adaptations to cold and investgation of the active site. J Biol Chem. 2003 Feb 28;278(9):7531-9. Epub 2002 Dec 9. [Article]
- Collins T, De Vos D, Hoyoux A, Savvides SN, Gerday C, Van Beeumen J, Feller G: Study of the active site residues of a glycoside hydrolase family 8 xylanase. J Mol Biol. 2005 Nov 25;354(2):425-35. Epub 2005 Oct 10. [Article]
- De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J: Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product. Biochemistry. 2006 Apr 18;45(15):4797-807. [Article]