B-N-acetylhexosaminidase
Details
- Name
- B-N-acetylhexosaminidase
- Synonyms
- Not Available
- Gene Name
- hex
- Organism
- Streptomyces plicatus
- Amino acid sequence
>lcl|BSEQ0022066|B-N-acetylhexosaminidase MTTGAAPDRKAPVRPTPLDRVIPAPASVDPGGAPYRITRGTHIRVDDSREARRVGDYLAD LLRPATGYRLPVTAHGHGGIRLRLAGGPYGDEGYRLDSGPAGVTITARKAAGLFHGVQTL RQLLPPAVEKDSAQPGPWLVAGGTIEDTPRYAWRSAMLDVSRHFFGVDEVKRYIDRVARY KYNKLHLHLSDDQGWRIAIDSWPRLATYGGSTEVGGGPGGYYTKAEYKEIVRYAASRHLE VVPEIDMPGHTNAALASYAELNCDGVAPPLYTGTKVGFSSLCVDKDVTYDFVDDVIGELA ALTPGRYLHIGGDEAHSTPKADFVAFMKRVQPIVAKYGKTVVGWHQLAGAEPVEGALVQY WGLDRTGDAEKAEVAEAARNGTGLILSPADRTYLDMKYTKDTPLGLSWAGYVEVQRSYDW DPAGYLPGAPADAVRGVEAPLWTETLSDPDQLDYMAFPRLPGVAELGWSPASTHDWDTYK VRLAAQAPYWEAAGIDFYRSPQVPWT
- Number of residues
- 506
- Molecular Weight
- 55193.595
- Theoretical pI
- 6.2
- GO Classification
- Functionsbeta-N-acetylhexosaminidase activityProcessescarbohydrate metabolic process
- General Function
- Beta-n-acetylhexosaminidase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0006191|1521 bp ATGACCACCGGCGCCGCCCCGGACCGGAAGGCGCCCGTCCGGCCGACGCCCCTCGACCGG GTGATCCCGGCCCCCGCCTCGGTCGACCCCGGCGGCGCGCCGTACCGCATCACGCGCGGC ACCCACATCCGCGTCGACGACTCGCGCGAGGCCCGCCGCGTCGGCGACTACCTCGCGGAC CTGCTGCGGCCCGCCACCGGCTACCGGCTCCCCGTCACCGCCCACGGCCACGGCGGCATA CGACTGCGCCTGGCGGGCGGCCCGTACGGCGACGAGGGCTACCGCCTCGACAGCGGCCCC GCAGGCGTCACCATCACCGCCCGCAAGGCCGCCGGACTCTTCCACGGCGTCCAGACCCTG CGTCAGCTGCTGCCCCCCGCCGTCGAGAAGGACTCCGCGCAGCCCGGCCCCTGGCTGGTC GCGGGCGGCACCATAGAGGACACGCCGCGCTACGCCTGGCGCAGCGCGATGCTCGACGTC TCCCGGCACTTCTTCGGCGTCGACGAGGTCAAGCGCTACATCGACCGCGTCGCCCGCTAC AAGTACAACAAGCTCCACCTGCACCTCAGCGACGACCAGGGCTGGCGCATCGCCATCGAC TCCTGGCCGCGCCTGGCGACGTACGGCGGCTCCACCGAGGTCGGCGGCGGCCCCGGCGGC TACTACACCAAGGCGGAGTACAAGGAGATCGTGCGTTACGCGGCCTCCCGCCACCTCGAG GTGGTCCCCGAGATCGACATGCCGGGCCACACCAACGCCGCCCTCGCCTCCTACGCCGAG CTGAACTGCGACGGTGTGGCGCCCCCGCTGTACACCGGCACCAAGGTCGGCTTCAGCTCG CTGTGCGTGGACAAGGACGTCACCTACGACTTCGTGGACGACGTCATCGGCGAACTCGCC GCGCTCACCCCCGGCCGCTACCTCCACATCGGCGGCGACGAGGCGCACTCCACGCCCAAG GCCGACTTCGTGGCGTTCATGAAGCGGGTGCAGCCGATCGTCGCCAAGTACGGCAAGACG GTCGTCGGCTGGCACCAGCTGGCCGGCGCGGAACCGGTCGAGGGCGCGCTCGTCCAGTAC TGGGGCCTGGACCGCACCGGCGACGCCGAGAAGGCCGAGGTCGCCGAGGCCGCCAGGAAC GGCACGGGGCTGATCCTCTCCCCGGCCGACCGGACGTACCTGGACATGAAGTACACCAAG GACACCCCGCTGGGCCTGTCCTGGGCGGGCTACGTCGAGGTGCAGCGGTCCTACGACTGG GACCCGGCCGGCTACCTGCCGGGCGCCCCGGCCGACGCGGTCCGCGGCGTCGAGGCCCCG CTGTGGACGGAGACCCTGTCCGACCCGGACCAGCTGGACTACATGGCCTTCCCGAGGCTG CCGGGCGTCGCCGAACTGGGCTGGTCCCCGGCGTCCACGCACGACTGGGACACCTACAAG GTGCGGCTCGCCGCGCAGGCCCCGTACTGGGAGGCGGCGGGGATCGACTTCTACCGCTCG CCGCAGGTGCCCTGGACCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O85361 UniProtKB Entry Name O85361_STRPL GenBank Gene ID AF063001 - General References
- Mark BL, Vocadlo DJ, Knapp S, Triggs-Raine BL, Withers SG, James MN: Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase. J Biol Chem. 2001 Mar 30;276(13):10330-7. Epub 2000 Dec 21. [Article]
- Mark BL, Vocadlo DJ, Zhao D, Knapp S, Withers SG, James MN: Biochemical and structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 beta-N-acetylhexosaminidase inhibitor. J Biol Chem. 2001 Nov 9;276(45):42131-7. Epub 2001 Aug 24. [Article]
- Williams SJ, Mark BL, Vocadlo DJ, James MN, Withers SG: Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J Biol Chem. 2002 Oct 18;277(42):40055-65. Epub 2002 Aug 8. [Article]