Endo-1,4-beta-xylanase A

Name	Endo-1,4-beta-xylanase A
Synonyms	1,4-beta-D-xylan xylanohydrolase A 3.2.1.8 Xylanase A
Gene Name	xlnA
Organism	Streptomyces lividans
Amino acid sequence	>lcl\|BSEQ0019328\|Endo-1,4-beta-xylanase A MGSYALPRSGVRRSIRVLLLALVVGVLGTATALIAPPGAHAAESTLGAAAAQSGRYFGTA IASGRLSDSTYTSIAGREFNMVTAENEMKIDATEPQRGQFNFSSADRVYNWAVQNGKQVR GHTLAWHSQQPGWMQSLSGSALRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARR DSNLQRSGNDWIEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPI DCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVTNDCLAVSR CLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDALNGGDSSEPPADGGQIKGVG SGRCLDVPDASTSDGTQLQLWDCHSGTNQQWAATDAGELRVYGDKCLDAAGTSNGSKVQI YSCWGGDNQKWRLNSDGSVVGVQSGLCLDAVGNGTANGTLIQLYTCSNGSNQRWTRT
Number of residues	None
Molecular Weight	51162.3
Theoretical pI	6.61
GO Classification	Functions carbohydrate binding endo-1,4-beta-xylanase activity Processes xylan catabolic process Components extracellular region
General Function	Endo-1,4-beta-xylanase activity
Specific Function	Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P26514
UniProtKB Entry Name
Cellular Location	Secreted
Gene sequence	>lcl\|BSEQ0005418\|1434 bp ATGGGCTCCTACGCCCTTCCCAGATCAGGTGTCCGCAGGAGCATTCGCGTCCTGCTGCTG GCGCTGGTCGTCGGCGTACTCGGCACGGCCACCGCACTGATCGCGCCGCCGGGGGCACAC GCCGCCGAGAGCACGCTCGGCGCCGCGGCGGCGCAGAGCGGCCGCTACTTCGGCACCGCC ATCGCCTCGGGCAGGCTGAGCGACTCGACGTACACGTCGATCGCGGGCCGTGAGTTCAAC ATGGTGACGGCCGAGAACGAGATGAAGATCGACGCCACCGAACCGCAGCGGGGCCAGTTC AACTTCAGCTCCGCCGACCGCGTCTACAACTGGGCGGTGCAGAACGGCAAGCAGGTGCGC GGCCACACCCTGGCCTGGCACTCCCAGCAGCCCGGCTGGATGCAGAGCCTCAGCGGCAGC GCGCTGCGCCAGGCGATGATCGACCACATCAACGGCGTGATGGCCCACTACAAGGGCAAG ATCGTCCAGTGGGACGTCGTGAACGAGGCCTTCGCCGACGGCAGTTCGGGAGCGCGGCGG GACTCCAACCTGCAACGCAGCGGCAACGACTGGATCGAGGTCGCCTTCCGCACCGCGCGC GCCGCCGACCCGTCCGCCAAGCTCTGCTACAACGACTACAACGTCGAGAACTGGACCTGG GCCAAGACCCAGGCCATGTACAACATGGTGCGGGACTTCAAGCAGCGCGGCGTGCCGATC GACTGCGTCGGCTTCCAGTCGCACTTCAACAGCGGCAGCCCCTACAACAGCAACTTCCGC ACCACACTGCAGAACTTCGCCGCCCTCGGCGTCGACGTGGCCATCACCGAGCTGGACATC CAGGGCGCCCCGGCCTCGACCTACGCCAACGTGACCAACGACTGCCTGGCCGTCTCGCGC TGCCTCGGCATCACCGTCTGGGGTGTGCGCGACAGCGACTCCTGGCGGTCGGAGCAGACG CCGTTGCTGTTCAACAACGACGGCAGCAAGAAGGCCGCGTACACCGCCGTCCTCGACGCA CTCAACGGCGGCGACTCCTCGGAGCCCCCCGCGGACGGGGGACAGATCAAGGGCGTCGGT TCGGGCCGCTGCCTCGACGTGCCCGACGCCAGCACCTCCGACGGCACCCAGCTCCAGCTG TGGGACTGCCACAGCGGCACCAACCAGCAGTGGGCCGCCACTGACGCGGGCGAGCTCAGG GTCTACGGCGACAAGTGCCTGGACGCCGCAGGCACCAGCAACGGCTCCAAGGTCCAGATC TACAGCTGCTGGGGCGGCGACAACCAGAAGTGGCGCCTCAACTCCGACGGGTCCGTCGTC GGCGTCCAGTCCGGCCTCTGCCTCGACGCCGTCGGGAACGGCACGGCCAACGGCACCCTG ATCCAGCTGTACACCTGCTCCAACGGCAGCAACCAACGCTGGACCCGCACCTGA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Shareck F, Roy C, Yaguchi M, Morosoli R, Kluepfel D: Sequences of three genes specifying xylanases in Streptomyces lividans. Gene. 1991 Oct 30;107(1):75-82. [1743521 ] Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS: Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. J Biol Chem. 1994 Aug 19;269(33):20811-4. [8063693 ] Notenboom V, Boraston AB, Williams SJ, Kilburn DG, Rose DR: High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding. Biochemistry. 2002 Apr 2;41(13):4246-54. [11914070 ]

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