Endochitinase B1
Details
- Name
- Endochitinase B1
- Synonyms
- 3.2.1.14
- Chitinase B1
- Gene Name
- chiB1
- Organism
- Neosartorya fumigata
- Amino acid sequence
>lcl|BSEQ0012193|Endochitinase B1 MRFATSTIVKVALLLSSLCVDAAVMWNRDTSSTDLEARASSGYRSVVYFVNWAIYGRNHN PQDLPVERLTHVLYAFANVRPETGEVYMTDSWADIEKHYPGDSWSDTGNNVYGCIKQLYL LKKQNRNLKVLLSIGGWTYSPNFAPAASTDAGRKNFAKTAVKLLQDLGFDGLDIDWEYPE NDQQANDFVLLLKEVRTALDSYSAANAGGQHFLLTVASPAGPDKIKVLHLKDMDQQLDFW NLMAYDYAGSFSSLSGHQANVYNDTSNPLSTPFNTQTALDLYRAGGVPANKIVLGMPLYG RSFANTDGPGKPYNGVGQGSWENGVWDYKALPQAGATEHVLPDIMASYSYDATNKFLISY DNPQVANLKSGYIKSLGLGGAMWWDSSSDKTGSDSLITTVVNALGGTGVFEQSQNELDYP VSQYDNLRNGMQT
- Number of residues
- 433
- Molecular Weight
- 47621.75
- Theoretical pI
- 4.85
- GO Classification
- Functionschitinase activityProcesseschitin catabolic process / polysaccharide catabolic processComponentsextracellular region
- General Function
- Chitinase activity
- Specific Function
- Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity).
- Pfam Domain Function
- Glyco_hydro_18 (PF00704)
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0006117|1302 bp ATGCGCTTTGCAACTTCCACCATCGTCAAGGTCGCCCTTCTGCTTAGCAGTCTTTGTGTC GACGCCGCAGTGATGTGGAATCGTGATACCAGTAGTACTGATCTGGAGGCGCGCGCTAGC TCCGGTTATCGCTCGGTCGTCTACTTTGTCAACTGGGCAATTTACGGGCGCAACCATAAT CCCCAGGATCTTCCTGTCGAGAGGCTCACGCACGTGCTCTACGCCTTTGCAAATGTGCGC CCTGAAACGGGGGAAGTCTATATGACAGACTCTTGGGCTGATATTGAGAAACATTACCCC GGTGACTCCTGGTCTGATACTGGCAACAATGTCTATGGCTGTATCAAACAGTTGTATCTC TTGAAGAAGCAGAACCGTAACCTCAAGGTTCTCTTGTCCATTGGCGGGTGGACCTACTCT CCCAACTTTGCTCCGGCGGCTAGTACCGACGCTGGACGGAAGAACTTTGCGAAGACTGCG GTGAAGCTGCTGCAGGACCTGGGATTTGATGGACTGGATATTGATTGGGAGTACCCTGAA AACGACCAGCAAGCGAACGACTTTGTTCTGTTGCTGAAGGAAGTGAGAACTGCCCTCGAC AGTTACAGTGCTGCAAATGCGGGCGGCCAGCACTTCCTTCTGACGGTGGCTTCTCCAGCT GGTCCCGATAAGATCAAGGTCCTTCACCTCAAGGACATGGATCAGCAATTGGACTTCTGG AATCTCATGGCCTACGATTATGCTGGCAGTTTCTCCTCCCTCAGCGGCCATCAAGCGAAC GTCTACAACGACACCTCCAACCCGCTCTCCACACCATTCAACACCCAGACGGCACTCGAT CTGTATCGCGCCGGCGGAGTCCCCGCCAACAAAATCGTTCTAGGCATGCCTCTCTACGGC CGCTCATTCGCCAACACCGACGGACCTGGTAAGCCTTATAACGGCGTTGGCCAGGGTAGC TGGGAGAATGGAGTGTGGGACTACAAGGCGCTCCCTCAAGCTGGCGCCACGGAGCATGTC CTTCCCGACATCATGGCGAGCTACAGCTACGACGCGACAAACAAGTTCTTGATCAGCTAT GACAACCCTCAAGTGGCGAATCTGAAGTCTGGCTATATCAAGTCCTTGGGATTGGGAGGC GCCATGTGGTGGGACAGCAGCAGCGACAAGACCGGAAGTGATAGTCTGATTACCACGGTA GTAAATGCACTCGGAGGCACGGGAGTCTTCGAACAGAGTCAGAATGAATTGGACTATCCG GTGTCGCAGTATGATAACCTGCGCAATGGCATGCAAACCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q873X9 UniProtKB Entry Name CHIB1_ASPFM GenBank Gene ID AY217660 - General References
- Jaques AK, Fukamizo T, Hall D, Barton RC, Escott GM, Parkinson T, Hitchcock CA, Adams DJ: Disruption of the gene encoding the ChiB1 chitinase of Aspergillus fumigatus and characterization of a recombinant gene product. Microbiology. 2003 Oct;149(Pt 10):2931-9. [Article]
- Hu H, Wang G, Yang H, Zhou J, Mo L, Yang K, Jin C, Jin C, Rao Z: Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407. Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):939-40. Epub 2004 Apr 21. [Article]
- Taib M, Pinney JW, Westhead DR, McDowall KJ, Adams DJ: Differential expression and extent of fungal/plant and fungal/bacterial chitinases of Aspergillus fumigatus. Arch Microbiol. 2005 Oct;184(1):78-81. Epub 2005 Nov 3. [Article]
- Lu Y, Yang H, Hu H, Wang Y, Rao Z, Jin C: Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1. Glycoconj J. 2009 Jul;26(5):525-34. doi: 10.1007/s10719-008-9203-z. Epub 2008 Oct 31. [Article]
- Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, Shiomi K, Omura S, van Aalten DM: Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. Chem Biol. 2005 Jan;12(1):65-76. [Article]
- Rao FV, Andersen OA, Vora KA, Demartino JA, van Aalten DM: Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes. Chem Biol. 2005 Sep;12(9):973-80. [Article]
- Schuttelkopf AW, Andersen OA, Rao FV, Allwood M, Lloyd C, Eggleston IM, van Aalten DM: Screening-based discovery and structural dissection of a novel family 18 chitinase inhibitor. J Biol Chem. 2006 Sep 15;281(37):27278-85. Epub 2006 Jul 14. [Article]
- Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM: Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin. Chem Biol. 2008 Mar;15(3):295-301. doi: 10.1016/j.chembiol.2008.02.015. [Article]