AC   MF_00364;
DC   Protein; auto
TR   HAMAP; MF_00364; -; 1; level=0
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Names: NagZ
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ID   NAGZ
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
GN   Name=nagZ;
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CC   -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC       terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC       linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC       acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
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DR   Pfam; PF00933; Glyco_hydro_3; 1; trigger=no
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1; trigger=no
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KW   Cell cycle
KW   Cell division
KW   Cell shape
KW   Cell wall biogenesis/degradation
KW   Cytoplasm
KW   Glycosidase
KW   Hydrolase
KW   Peptidoglycan synthesis
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GO   GO:0004563; F:beta-N-acetylhexosaminidase activity
GO   GO:0009254; P:peptidoglycan turnover
GO   GO:0005737; C:cytoplasm
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FT   From: NAGZ_SALTY (Q8ZQ06)
FT   BINDING         163..164
FT                   /ligand="substrate"
FT   Condition: K-H
FT   ACT_SITE        176
FT                   /note="Proton donor/acceptor"
FT   Condition: H
FT   ACT_SITE        248
FT                   /note="Nucleophile"
FT   Condition: D
FT   BINDING         62
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         70
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         133
FT                   /ligand="substrate"
FT   Condition: R
FT   SITE            174
FT                   /note="Important for catalytic activity"
FT   Condition: D
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Size: 300-400;
Related: None;
Template: P75949; Q8ZQ06; Q9KU37;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.30 2023/01/26
//