Beta-hexosaminidase
Details
- Name
- Beta-hexosaminidase
- Kind
- protein
- Synonyms
- 3.2.1.52
- Beta-N-acetylhexosaminidase
- N-acetyl-beta-glucosaminidase
- Gene Name
- nagZ
- UniProtKB Entry
- Q9KU37Swiss-Prot
- Organism
- Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
- NCBI Taxonomy ID
- 243277
- Amino acid sequence
>lcl|BSEQ0020716|Beta-hexosaminidase MGPLWLDVAGYELSAEDREILQHPTVGGVILFGRNYHDNQQLLALNKAIRQAAKRPILIG VDQEGGRVQRFREGFSRIPPAQYYARAENGVELAEQGGWLMAAELIAHDVDLSFAPVLDM GFACKAIGNRAFGEDVQTVLKHSSAFLRGMKAVGMATTGKHFPGHGAVIADSHLETPYDE RETIAQDMAIFRAQIEAGVLDAMMPAHVVYPHYDAQPASGSSYWLKQVLREELGFKGIVF SDDLSMEGAAVMGGPVERSHQALVAGCDMILICNKREAAVEVLDNLPIMEVPQAEALLKK QQFSYSELKRLERWQQASANMQRLIEQFSE
- Number of residues
- 330
- Molecular Weight
- 36465.365
- Theoretical pI
- 5.24
- GO Classification
- Functionsbeta-N-acetylhexosaminidase activityProcessescarbohydrate metabolic process / cell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / peptidoglycan turnover / peptidoglycan-based cell wall biogenesis / regulation of cell shape / response to antibioticComponentscytoplasm
- General Function
- Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.
- Specific Function
- beta-N-acetylhexosaminidase activity
- Pfam Domain Function
- Glyco_hydro_3 (PF00933)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020717|Beta-hexosaminidase (nagZ) ATGGGACCGCTTTGGTTGGATGTGGCCGGTTACGAACTGAGTGCCGAAGATCGCGAAATT CTGCAGCACCCTACAGTGGGTGGTGTGATTCTGTTTGGTCGCAACTATCACGATAACCAG CAATTGCTGGCACTCAATAAAGCGATCCGTCAAGCGGCGAAAAGACCGATTTTGATTGGT GTCGATCAAGAAGGTGGCCGCGTGCAGCGTTTCCGTGAAGGCTTTTCTCGCATTCCCCCT GCGCAGTATTACGCGCGTGCTGAGAATGGCGTTGAGCTTGCTGAGCAGGGCGGTTGGTTG ATGGCGGCAGAGCTGATTGCACACGATGTTGATTTAAGTTTTGCGCCTGTGCTCGATATG GGCTTTGCGTGTAAAGCGATTGGCAACCGTGCTTTTGGTGAAGATGTTCAAACTGTACTT AAGCACAGCAGTGCTTTTCTGCGCGGCATGAAAGCCGTCGGCATGGCGACCACAGGCAAA CATTTCCCCGGCCATGGCGCGGTGATTGCCGATTCGCATTTAGAGACCCCTTACGATGAG CGGGAGACGATTGCGCAAGATATGGCGATTTTCCGTGCGCAAATTGAGGCTGGAGTGCTA GATGCCATGATGCCAGCGCATGTGGTGTATCCGCATTACGATGCTCAACCTGCGAGCGGT TCGAGCTACTGGCTAAAACAAGTGTTACGTGAAGAACTCGGCTTTAAAGGCATCGTATTT TCGGATGATTTGAGCATGGAAGGCGCAGCCGTAATGGGGGGGCCAGTTGAGCGCTCCCAT CAAGCTTTGGTCGCCGGTTGTGACATGATTTTGATCTGTAACAAGCGTGAGGCGGCGGTC GAAGTGCTGGATAACCTTCCGATCATGGAAGTACCACAAGCTGAAGCACTGCTGAAAAAG CAGCAATTTAGCTACAGTGAGCTGAAGCGTTTAGAGCGTTGGCAGCAAGCGTCAGCCAAT ATGCAGCGCTTAATCGAGCAGTTCTCCGAATAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9KU37 UniProtKB Entry Name NAGZ_VIBCH GenBank Protein ID 9654392 GenBank Gene ID AE003852 PDB ID(s) 1TR9, 1Y65, 2OXN, 3GS6, 3GSM KEGG ID vch:VC0692 NCBI Gene ID 2615481 - General References
- Heidelberg JF, Eisen JA, Nelson WC, Clayton RA, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Umayam L, Gill SR, Nelson KE, Read TD, Tettelin H, Richardson D, Ermolaeva MD, Vamathevan J, Bass S, Qin H, Dragoi I, Sellers P, McDonald L, Utterback T, Fleishmann RD, Nierman WC, White O, Salzberg SL, Smith HO, Colwell RR, Mekalanos JJ, Venter JC, Fraser CM: DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature. 2000 Aug 3;406(6795):477-83. [Article]
- Stubbs KA, Bacik JP, Perley-Robertson GE, Whitworth GE, Gloster TM, Vocadlo DJ, Mark BL: The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams. Chembiochem. 2013 Oct 11;14(15):1973-81. doi: 10.1002/cbic.201300395. Epub 2013 Sep 5. [Article]
- Stubbs KA, Balcewich M, Mark BL, Vocadlo DJ: Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance. J Biol Chem. 2007 Jul 20;282(29):21382-91. Epub 2007 Apr 16. [Article]
- Balcewich MD, Stubbs KA, He Y, James TW, Davies GJ, Vocadlo DJ, Mark BL: Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 2009 Jul;18(7):1541-51. doi: 10.1002/pro.137. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details [[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamate experimental unknown target Details [[(3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-(pentanoylamino)oxan-2-ylidene]amino] N-phenylcarbamate experimental unknown target Details