Escherichia coli K-12 substr. MG1655 Enzyme: β-N-acetylhexosaminidase

Gene: nagZ Accession Numbers: G6567 (EcoCyc), b1107, ECK1093

Synonyms: ycfO, hexosaminidase

Regulation Summary Diagram: ?

Regulation summary diagram for nagZ

β-N-Acetylglucosaminidase is a cytoplasmic enzyme involved in murein tripeptide recycling. N-Acetylglucosamine is released from murein-lipoprotein complexes, glycopeptide monomers and glycopeptide dimers. It is specific for the β-linkage. The enzyme cleaves anhydromuropeptides and is also active with muropeptides. [Cheng00, Yem76, Votsch00]

Review: [Park08]

Locations: cytosol

Map Position: [1,163,318 -> 1,164,343] (25.07 centisomes, 90°)
Length: 1026 bp / 341 aa

Molecular Weight of Polypeptide: 37.595 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003737 , EchoBASE:EB3207 , EcoGene:EG13433 , EcoliWiki:b1107 , ModBase:P75949 , OU-Microarray:b1107 , PortEco:nagZ , PR:PRO_000023341 , Pride:P75949 , Protein Model Portal:P75949 , RefSeq:NP_415625 , RegulonDB:G6567 , SMR:P75949 , String:511145.b1107 , Swiss-Model:P75949 , UniProt:P75949

Relationship Links: CAZy:IN-FAMILY:GH3 , InterPro:IN-FAMILY:IPR001764 , InterPro:IN-FAMILY:IPR017853 , InterPro:IN-FAMILY:IPR019800 , InterPro:IN-FAMILY:IPR022956 , Pfam:IN-FAMILY:PF00933 , Prosite:IN-FAMILY:PS00775

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009254 - peptidoglycan turnover Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA06, Park01]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0008360 - regulation of cell shape Inferred by computational analysis [UniProtGOA11a]
GO:0009252 - peptidoglycan biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0051301 - cell division Inferred by computational analysis [UniProtGOA11a]
GO:0071555 - cell wall organization Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004553 - hydrolase activity, hydrolyzing O-glycosyl compounds Inferred by computational analysis [GOA01]
GO:0004563 - beta-N-acetylhexosaminidase activity Inferred by computational analysis [GOA06, GOA01a, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism central intermediary metabolism murein turnover, recycling

Essentiality data for nagZ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Enzymatic reaction of: glcNAc-1,6-anhMurNAcaminidase (β-N-acetylhexosaminidase)

EC Number:

N-acetyl-β-D-glucosamine(anhydrous)-N-acetylmuramate + H2O <=> N-acetyl-β-D-glucosamine + 1,6-anhydro-N-acetyl-β-muramate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: anhydromuropeptides recycling

Enzymatic reaction of: β-N-acetylglucosaminidase (β-N-acetylhexosaminidase)

EC Number:

an N-acetyl-β-D-hexosaminide + H2O <=> an N-acetyl-β-D-hexosamine + an alcohol

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Inhibitors (Unknown Mechanism): a bulgecin [Votsch00] , N-acetylglucosaminolactone , N-acetylmuramate [Comment 5] , N-acetyl-β-D-glucosamine [Comment 5]

Sequence Features

Protein sequence of beta-N-acetylhexosaminidase with features indicated

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 62
UniProt: Substrate.
Amino-Acid-Sites-That-Bind 70
UniProt: Substrate.
Amino-Acid-Sites-That-Bind 133
UniProt: Substrate.
Protein-Segment 163 -> 164
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Site 174
UniProt: Important for catalytic activity; Sequence Annotation Type: site.
Active-Site 176
UniProt: Proton donor/acceptor.
Active-Site 248
UniProt: Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Cheng00: Cheng Q, Li H, Merdek K, Park JT (2000). "Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling." J Bacteriol 2000;182(17);4836-40. PMID: 10940025

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Park01: Park JT (2001). "Identification of a dedicated recycling pathway for anhydro-N-acetylmuramic acid and N-acetylglucosamine derived from Escherichia coli cell wall murein." J Bacteriol 183(13);3842-7. PMID: 11395446

Park08: Park JT, Uehara T (2008). "How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)." Microbiol Mol Biol Rev 72(2);211-27, table of contents. PMID: 18535144

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-08 released on 2014-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Votsch00: Votsch W, Templin MF (2000). "Characterization of a beta -N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta -lactamase induction." J Biol Chem 2000;275(50);39032-8. PMID: 10978324

Yem76: Yem DW, Wu HC (1976). "Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli." J Bacteriol 1976;125(1);324-31. PMID: 1377

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 13, 2015, BIOCYC11A.