Endo-beta-1,4-xylanase Xyn10C
Details
- Name
- Endo-beta-1,4-xylanase Xyn10C
- Kind
- protein
- Synonyms
- 3.2.1.8
- Xylanase 10C
- XYLF
- xynF
- Gene Name
- xyn10C
- UniProtKB Entry
- Q59675Swiss-Prot
- Organism
- Cellvibrio japonicus
- NCBI Taxonomy ID
- 155077
- Amino acid sequence
>lcl|BSEQ0012147|Endo-beta-1,4-xylanase Xyn10C MKKIQQLLMLSLISSTLIACGGGGGGGSTPTTSSSPQSSSPASTPSSASSSSIISSSSLS SSLSSSSLSSSSLSSSSASSVSSSSVAASEGNVVIEVDMANGWRGNASGSTSHSGITYSA DGVTFAALGDGVGAVFDIARPTTLEDAVIAMVVNVSAEFKASEANLQIFAQLKEDWSKGE WDCLAASSELTADTDLTLTCTIDEDDDKFNQTARDVQVGIQAKGTPAGTITIKSVTITLA QEAYSANVDHLRDLAPSDFPIGVAVSNTDSATYNLLTNSREQAVVKKHFNHLTAGNIMKM SYMQPTEGNFNFTNADAFVDWATENNMTVHGHALVWHSDYQVPNFMKNWAGSAEDFLAAL DTHITTIVDHYEAKGNLVSWDVVNEAIDDNSPANFRTTDSAFYVKSGNSSVYIERAFQTA RAADPAVILYYNDYNIEQNNAKTTKMVDMVKDFQARSIPIDGVGFQMHVCMNYPSIANIS AAMKKVVDLGLLVKITELDVAVNQPHCDAYPANKINPLTEAAQLAQKKRYCDVVKAYLDT VPVNQRGGISVWGTTDANTWLDGLYREQFEDEKISWPLLFDNNYNDKPALRGFADALIGT QCTNTH
- Number of residues
- 606
- Molecular Weight
- 64883.385
- Theoretical pI
- 4.48
- GO Classification
- Functionsendo-1,4-beta-xylanase activityProcessesxylan catabolic processComponentscell outer membrane
- General Function
- Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan, the arabinoxylans from wheat and rye, and glucuronoxylan. Also displays very low activity against xylooligosaccharides. During the xylan degradation process, Xyn10C may act on the soluble xylans and long xylooligosaccharides products released by the secreted xylanases Xyn11A, Xyn11B and Xyn10A.
- Specific Function
- endo-1,4-beta-xylanase activity
- Pfam Domain Function
- Signal Regions
- 1-19
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell outer membrane
- Gene sequence
>lcl|BSEQ0005993|1821 bp ATGAAAAAGATCCAGCAACTCCTCATGCTCTCCCTGATTAGCTCAACACTAATTGCCTGT GGCGGCGGTGGAGGGGGCGGTTCAACACCAACCACCAGCAGCTCACCCCAATCCTCTAGT CCAGCATCGACGCCATCCAGTGCTTCATCCTCATCGATCATATCCTCCTCATCGCTATCA TCATCGCTGTCTTCCTCATCACTATCCTCGTCATCGCTGTCTTCTTCATCGGCGAGCAGT GTTAGCAGCTCCAGTGTCGCTGCCAGCGAGGGCAATGTTGTTATAGAGGTGGACATGGCA AATGGCTGGAGAGGCAACGCATCAGGCAGTACCAGCCATTCCGGTATTACCTACAGTGCC GATGGCGTTACCTTTGCCGCACTGGGTGATGGCGTGGGCGCTGTTTTTGATATTGCCCGA CCAACCACACTGGAAGATGCTGTGATAGCAATGGTTGTTAATGTCAGCGCTGAATTTAAG GCCAGTGAAGCCAACTTGCAGATATTTGCCCAGTTAAAAGAAGACTGGTCAAAGGGCGAA TGGGATTGTCTGGCGGCCAGCAGCGAACTCACTGCGGATACTGACCTAACCCTGACCTGC ACCATTGATGAAGACGACGATAAATTCAACCAAACGGCGCGCGATGTACAAGTCGGTATC CAGGCCAAGGGAACACCCGCCGGAACTATCACCATTAAAAGCGTCACCATTACACTCGCA CAGGAAGCCTATTCAGCCAATGTCGATCACCTGCGCGACCTGGCCCCCAGCGATTTCCCC ATTGGCGTCGCCGTGTCCAATACCGACTCCGCCACTTACAACCTGCTCACCAACAGCAGA GAGCAGGCTGTGGTTAAAAAGCACTTCAATCATTTAACTGCCGGTAACATCATGAAGATG AGTTACATGCAACCTACCGAGGGCAATTTTAACTTCACCAACGCCGACGCCTTTGTGGAT TGGGCCACTGAAAATAATATGACGGTGCACGGCCACGCCCTGGTATGGCATTCCGATTAC CAGGTTCCCAACTTTATGAAAAACTGGGCAGGCAGTGCAGAAGACTTTTTAGCGGCCTTG GACACACATATCACCACCATTGTCGATCACTACGAAGCCAAGGGTAACCTCGTCAGTTGG GACGTCGTTAACGAAGCCATCGACGACAACAGTCCGGCAAACTTCCGCACGACGGATTCT GCGTTTTATGTGAAGAGCGGAAACAGCTCTGTCTATATTGAGCGCGCCTTCCAGACCGCG CGCGCGGCAGATCCCGCTGTGATCCTCTACTACAACGACTACAACATTGAGCAGAACAAT GCCAAGACCACCAAAATGGTCGATATGGTCAAGGACTTCCAGGCGCGCAGTATCCCGATT GACGGTGTGGGCTTCCAGATGCATGTCTGTATGAACTATCCATCCATCGCCAACATTTCT GCCGCGATGAAGAAAGTGGTCGACCTTGGCTTGCTGGTAAAAATTACCGAACTGGATGTT GCCGTCAACCAGCCCCATTGCGATGCGTATCCGGCCAACAAAATCAATCCGCTGACCGAA GCGGCGCAATTGGCCCAGAAAAAACGCTACTGCGACGTAGTGAAGGCCTATCTGGATACA GTCCCGGTGAATCAGCGCGGCGGTATCAGCGTCTGGGGAACTACCGATGCCAACACCTGG CTTGATGGCCTGTACAGAGAACAGTTTGAGGATGAAAAAATTTCCTGGCCCTTGCTGTTC GACAACAACTACAACGACAAACCTGCACTGCGCGGTTTTGCCGATGCGTTAATCGGTACG CAATGTACTAATACACATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q59675 UniProtKB Entry Name XY10C_CELJA GenBank Gene ID Z48928 PDB ID(s) 1GNY, 1US2, 1US3 - General References
- Millward-Sadler SJ, Davidson K, Hazlewood GP, Black GW, Gilbert HJ, Clarke JH: Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus. Biochem J. 1995 Nov 15;312 ( Pt 1):39-48. [Article]
- Emami K, Nagy T, Fontes CM, Ferreira LM, Gilbert HJ: Evidence for temporal regulation of the two Pseudomonas cellulosa xylanases belonging to glycoside hydrolase family 11. J Bacteriol. 2002 Aug;184(15):4124-33. [Article]
- Szabo L, Jamal S, Xie H, Charnock SJ, Bolam DN, Gilbert HJ, Davies GJ: Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation. J Biol Chem. 2001 Dec 28;276(52):49061-5. Epub 2001 Oct 11. [Article]
- Pell G, Szabo L, Charnock SJ, Xie H, Gloster TM, Davies GJ, Gilbert HJ: Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases. J Biol Chem. 2004 Mar 19;279(12):11777-88. Epub 2003 Dec 11. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details alpha-D-Xylopyranose experimental unknown target Details