Xanthan lyase
Details
- Name
- Xanthan lyase
- Synonyms
- 4.2.2.12
- Gene Name
- xly
- UniProtKB Entry
- Q9AQS0Swiss-Prot
- Organism
- Bacillus sp. (strain GL1)
- NCBI Taxonomy ID
- 84635
- Amino acid sequence
>lcl|BSEQ0017050|Xanthan lyase MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKL AQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADL KEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDT IDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYAD GSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKG AMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSF YGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSY ESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSS WTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNR KLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKRE ARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADP AIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVS DPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDT SGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFT PNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAG SGGSVTIRNDALGSPDGYVVADAVKFVAVG
- Number of residues
- 930
- Molecular Weight
- 99312.455
- Theoretical pI
- 4.74
- GO Classification
- Functionscalcium ion binding / mannose binding / xanthan lyase activityProcessespolysaccharide metabolic processComponentsextracellular space
- General Function
- Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.
- Specific Function
- calcium ion binding
- Pfam Domain Function
- Signal Regions
- 1-25
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0006412|2793 bp ATGCTGTCGGGCATCCTGATCGCTGCGCTGCTGATGACGCTGTGGGGAGGCTGGCAGCCG GACATTGCGCACGCATCGGATGAATTCGACGCGCTTCGAATCAAGTGGGCGACGCTGCTG ACCGGAGGCCCGGCGCTGGATCCGGCGGATTCGGATATCGCAGCGCGGACGGACAAGCTT GCCCAAGATGCGAACGACTATTGGGAAGACATGGACTTGTCCTCTTCGCGCACGTACATC TGGTACGCGCTCCGCGGCAACGGCACTTCGGACAATGTAAACGCGGTTTACGAGCGTCTG CGGACGATGGCTTTGGCGGCGACGACCGTCGGCTCCAGCCTTTACGGCAACGCGGACCTC AAGGAAGACATTCTGGATGCGCTCGACTGGCTGTACGTCAACAGCTACAACAGCACGCGA AGCCGCTCCGCGTACAACTGGTGGCATTGGCAGCTTGGCATCCCGATGAGCCTGAACGAC ATCGCGGTGCTGCTGTACGACGATATAAGCGCAGCGCGGATGGCGACCTATATGGACACC ATCGATTATTTTACGCCTTCGATCGGACTCACGGGCGCGAACCGGGCGTGGCAGGCGATC GTCGTCGGCGTGCGCGCGGTCATCGTCAAGGACGCGGTCAAGCTGGCCGCGGCGCGCAAC GGCTTGTCCGGCACAGGCATATTCCCGTACGCGACGGGCGGCGATGGCTTCTATGCGGAC GGCTCCTTCGTCCAGCATACCACTTTCGCCTATACCGGCGGATACGGCAGCTCCGTGCTG GAAACGACGGCCAACCTGATGTACTTGCTGTCGGGCTCTACCTGGTCGGTATCCGATCCG AACCAGAGCAACGTTTGGCAGTGGATCTACGAAGCCTATCGGCCGCTGCTGTACAAGGGC GCGATGATGGACATGGTGCGCGGACGGGAGATTTCCCGCAGCTACGCGCAGGATCATGCG GTCGGGCACGGCATCGTCGCGAGCATCGTGCGGCTTGCCCAGTTCGCGCCGGCGCCGCAT GCAGCCGCCTTCAAACAGATTGCGAAGCGCGTGATTCAGGAAGATACGTTCAGCAGCTTC TACGGCGACGTATCGACCGACACGATCCGCCTTGCCAAGGCGATCGTTGACGATCCGTCC ATAGCGCCCGCCGCGGCGCCGAATCTTTACAAGCAGTACGCTGCGATGGACCGGGCCGTC CTGCAGCGGCCCGGTTTCGCTCTGGGACTCGCCTTGTATTCGACGCGGATCAGCAGCTAC GAATCGATCAATAGCGAGAACGGGCGGGGCTGGTATACGGGAGCGGGCGCGACCTATCTG TACAATCAGGACCTTGCGCAATACAGCGAGGACTATTGGCCGACCGTGGATGCCTACCGG ATCCCGGGGACGACGGTCGCCTCTGGGACGCCGATCGCGAGCGGGACCGGCACGTCGAGC TGGACGGGCGGCGTATCGCTTGCGGGACAGTACGGCGCCAGCGGCATGGATCTCTCCTAC GGCGCTTACAATCTGAGCGCGCGCAAATCCTGGTTCATGTTCGACGACGAGATCGTCGCG CTCGGATCAGGCATATCCAGCACGGCAGGCATCCCGATCGAGACCGTCGTCGACAATCGC AAGCTGAACGGGGCCGGCGACAATGCCTGGACGGCGAACGGAGCGGCGCTGTCCACCGGT CTGGGCGTCGCGCAGACGCTGACCGGCGTCAATTGGGTGCACCTGGCGGGCAATACCGCC GACGGCTCGGACATCGGCTACTACTTTCCTGGAGGCGCGACGCTGCAGACGAAGCGGGAA GCGCGCACGGGTACCTGGAAGCAGATCAACAATCGCCCGGCCACGCCCTCTACCGCCGTC ACGCGCAACTACGAGACGATGTGGATCGACCACGGCACGAATCCTTCGGGTGCGTCGTAC GGGTATGTGCTGCTGCCGAACAAGACGAGCGCGCAGGTCGGCGCCTACGCCGCCGATCCC GCGATCGAGATCGTCGTCAATACGAGCGGCGTACAGTCGGTCAAGGAAAAAACGCTCGGA CTGGTCGGCGCGAACTTCTGGACGGATACGACGCAGACGGCCGATCTGATCACGTCGAAC AAAAAGGCGTCGGTGATGACCCGCGAGATCGCGGACGAGCGCCTCGAGGCGTCGGTGTCC GATCCGACGCAAGCGAACAACGGCACCATCGCGATCGAACTGGCGCGCTCGGCCGAGGGC TACAGCGCGGATCCGGGCATTACGGTCACGCAGCTCGCTCCGACGATCAAATTCACCGTT AACGTGAACGGCGCGAAGGGCAAATCGTTTCACGCGTCGTTCCAGCTGGGCGAAGATACG AGCGGACCGGTCGATCCGGGAGAGCCCGAACTGCCGTCCGTCATCGTGGACAATGCCGAT TCGGCGGGTGTGACCAGGACGGGGACGTGGAAAACTGCCAGCACGCAGACGGACCGTTAC GGCGCGAATTATTTGCATGACGACAACGCCGGCAAAGGAACGAAAAGCGTGACTTTTACG CCGAATCTGCCGATCGCCGGCTCATATGAGGTGTATCTGATGTGGCCGGCCCATTTTAAT CGGGAGGATGCGGTGCAGGTCGATGTCGGCCATGCATCGGGGACGACGCGCACGGCGGTC GATCAGCGTTCGGGCGGCGGGGTCTGGCATTCGATCGGGACATACGAATTTTTGGCCGGA TCGGGCGGCAGCGTCACGATCCGCAACGACGCGCTCGGGTCTCCCGACGGTTACGTCGTC GCCGACGCGGTCAAGTTCGTGGCCGTCGGCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9AQS0 UniProtKB Entry Name XANLY_BACGL GenBank Gene ID AB037178 PDB ID(s) 1J0M, 1J0N, 1X1H, 1X1I, 1X1J, 2E22, 2E24 - General References
- Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K: Polysaccharide lyase: molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1. Appl Environ Microbiol. 2001 Feb;67(2):713-20. [Article]
- Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K: Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains. Appl Environ Microbiol. 1998 Oct;64(10):3765-8. [Article]
- Nankai H, Hashimoto W, Miki H, Kawai S, Murata K: Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1. Appl Environ Microbiol. 1999 Jun;65(6):2520-6. [Article]
- Hashimoto W, Nankai H, Mikami B, Murata K: Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan. J Biol Chem. 2003 Feb 28;278(9):7663-73. Epub 2002 Dec 9. [Article]
- Maruyama Y, Hashimoto W, Mikami B, Murata K: Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism. J Mol Biol. 2005 Jul 29;350(5):974-86. [Article]
- Maruyama Y, Mikami B, Hashimoto W, Murata K: A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan. Biochemistry. 2007 Jan 23;46(3):781-91. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Xanthan lyase (Bacillus sp. (strain GL1)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 4,6-O-(1-Carboxyethylidene)-Beta-D-Glucose experimental unknown target Details 4-O-{4,6-O-[(1S)-1-Carboxyethylidene]-β-D-mannopyranosyl}-D-glucopyranuronic acid experimental unknown target Details [4,6-O-(1-CARBOXYETHYLIDENE)-BETA-D-MANNOSE] experimental unknown target Details