Beta-hexosaminidase
Details
- Name
- Beta-hexosaminidase
- Synonyms
- 3.2.1.52
- Beta-N-acetylhexosaminidase
- N-acetyl-beta-glucosaminidase
- N-acetylglucosaminidase
- ORF1
- ybbD
- yzbA
- Gene Name
- nagZ
- Organism
- Bacillus subtilis (strain 168)
- Amino acid sequence
>lcl|BSEQ0012986|Beta-hexosaminidase MRPVFPLILSAVLFLSCFFGARQTEASASKRAIDANQIVNRMSLDEKLGQMLMPDFRNWQ KEGESSPQALTKMNDEVASLVKKYQFGGIILFAENVKTTKQTVQLTDDYQKASPKIPLML SIDQEGGIVTRLGEGTNFPGNMALGAARSRINAYQTGSIIGKELSALGINTDFSPVVDIN NNPDNPVIGVRSFSSNRELTSRLGLYTMKGLQRQDIASALKHFPGHGDTDVDSHYGLPLV SHGQERLREVELYPFQKAIDAGADMVMTAHVQFPAFDDTTYKSKLDGSDILVPATLSKKV MTGLLRQEMGFNGVIVTDALNMKAIADHFGQEEAVVMAVKAGVDIALMPASVTSLKEEQK FARVIQALKEAVKNGDIPEQQINNSVERIISLKIKRGMYPARNSDSTKEKIAKAKKIVGS KQHLKAEKKLAEKAVTVLKNEQHTLPFKPKKGSRILIVAPYEEQTASIEQTIHDLIKRKK IKPVSLSKMNFASQVFKTEHEKQVKEADYIITGSYVVKNDPVVNDGVIDDTISDSSKWAT VFPRAVMKAALQHNKPFVLMSLRNPYDAANFEEAKALIAVYGFKGYANGRYLQPNIPAGV MAIFGQAKPKGTLPVDIPSVTKPGNTLYPLGYGLNIKTGRPL
- Number of residues
- 642
- Molecular Weight
- 70579.905
- Theoretical pI
- 9.94
- GO Classification
- Functionsbeta-N-acetylhexosaminidase activityProcessescarbohydrate metabolic process / cell wall organization / peptidoglycan biosynthetic process / peptidoglycan turnover / regulation of cell shapeComponentscell wall / extracellular region / plasma membrane
- General Function
- Beta-n-acetylhexosaminidase activity
- Specific 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. Cleaves muropeptides, but not peptidoglycan.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0012987|Beta-hexosaminidase (nagZ) ATGAGACCTGTCTTTCCGCTTATCCTTTCAGCCGTTCTCTTTCTTTCATGCTTTTTCGGG GCCAGACAGACAGAAGCCTCTGCATCCAAACGTGCAATCGATGCCAATCAGATTGTCAAT CGTATGTCGTTAGATGAAAAACTCGGCCAGATGCTGATGCCTGATTTTAGAAATTGGCAA AAGGAAGGCGAGTCCTCTCCGCAAGCCCTTACAAAAATGAATGATGAAGTCGCCAGCCTC GTCAAGAAATATCAATTCGGAGGCATCATCCTTTTTGCAGAAAATGTAAAAACAACAAAA CAAACTGTCCAACTGACAGACGATTACCAAAAGGCAAGTCCAAAAATCCCGCTCATGCTG AGTATTGATCAGGAAGGCGGCATTGTAACGAGGTTAGGGGAGGGCACTAATTTCCCAGGG AATATGGCGCTGGGCGCAGCCAGAAGCAGAATCAATGCGTATCAGACCGGCAGCATCATC GGAAAAGAGCTCTCTGCCTTAGGCATCAATACAGATTTCAGCCCTGTCGTGGACATTAAC AATAATCCTGATAATCCTGTAATCGGCGTACGGTCATTCAGCTCCAATCGAGAACTGACA TCACGCCTCGGTTTATATACGATGAAAGGGTTGCAGCGGCAGGATATCGCGTCTGCCCTC AAACATTTCCCGGGACATGGAGACACGGACGTTGACAGCCATTATGGACTGCCGCTCGTT TCCCATGGCCAAGAACGGCTTCGTGAGGTCGAGCTTTATCCTTTTCAAAAAGCAATTGAT GCTGGTGCTGATATGGTGATGACAGCCCATGTTCAGTTTCCCGCCTTTGATGACACCACT TACAAAAGCAAACTCGATGGATCGGACATTCTGGTTCCAGCTACACTTTCAAAAAAAGTG ATGACAGGTCTTCTTCGTCAGGAAATGGGCTTTAATGGGGTCATCGTTACCGATGCGCTC AATATGAAGGCAATCGCAGATCATTTCGGACAGGAAGAGGCTGTGGTCATGGCCGTAAAA GCTGGTGTCGATATTGCATTAATGCCAGCCTCAGTCACTTCATTGAAAGAAGAACAGAAA TTCGCACGTGTTATTCAAGCTTTGAAAGAAGCCGTGAAAAACGGGGATATTCCTGAACAA CAAATCAACAATTCAGTTGAAAGAATCATTTCCCTGAAAATAAAACGCGGCATGTATCCA GCGCGAAACAGCGACAGTACAAAAGAAAAAATAGCCAAAGCCAAAAAAATCGTAGGAAGC AAGCAGCACCTGAAAGCAGAGAAAAAATTAGCTGAAAAAGCAGTAACTGTATTAAAAAAT GAACAGCACACTTTGCCGTTCAAGCCTAAAAAAGGCAGCCGAATCTTAATTGTGGCACCT TACGAAGAACAAACTGCTTCAATCGAACAAACCATTCACGATCTCATCAAGCGAAAGAAA ATCAAACCCGTATCCCTCAGCAAAATGAACTTTGCCAGCCAAGTATTTAAGACCGAGCAT GAAAAACAAGTAAAAGAGGCTGATTATATCATTACCGGCTCCTATGTCGTCAAAAATGAC CCTGTCGTCAACGACGGTGTCATCGACGACACAATATCAGATTCAAGCAAATGGGCCACC GTGTTTCCGAGAGCTGTCATGAAAGCCGCACTGCAGCACAACAAACCATTTGTCTTAATG AGCCTGCGCAACCCCTATGACGCAGCCAATTTCGAAGAAGCAAAAGCACTGATTGCAGTC TATGGCTTTAAAGGATACGCAAATGGCCGTTATCTTCAACCTAATATTCCGGCCGGAGTG ATGGCGATATTCGGCCAGGCAAAACCTAAAGGCACACTTCCAGTTGACATTCCGTCAGTC ACGAAACCAGGGAACACCCTTTACCCACTTGGCTACGGATTAAATATCAAAACGGGAAGA CCGCTTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P40406 UniProtKB Entry Name NAGZ_BACSU GenBank Protein ID 438455 GenBank Gene ID L19954 - General References
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- Liu H, Haga K, Yasumoto K, Ohashi Y, Yoshikawa H, Takahashi H: Sequence and analysis of a 31 kb segment of the Bacillus subtilis chromosome in the area of the rrnH and rrnG operons. Microbiology. 1997 Aug;143 ( Pt 8):2763-7. [Article]
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- Litzinger S, Duckworth A, Nitzsche K, Risinger C, Wittmann V, Mayer C: Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase. J Bacteriol. 2010 Jun;192(12):3132-43. doi: 10.1128/JB.01256-09. Epub 2010 Apr 16. [Article]
- Litzinger S, Fischer S, Polzer P, Diederichs K, Welte W, Mayer C: Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J Biol Chem. 2010 Nov 12;285(46):35675-84. doi: 10.1074/jbc.M110.131037. Epub 2010 Sep 7. [Article]
- Bacik JP, Whitworth GE, Stubbs KA, Vocadlo DJ, Mark BL: Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion. Chem Biol. 2012 Nov 21;19(11):1471-82. doi: 10.1016/j.chembiol.2012.09.016. [Article]