ID NAGZ_VIBFU Reviewed; 329 AA. AC P96157; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 03-MAY-2023, entry version 102. DE RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; GN Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364}; Synonyms=exo II; OS Vibrio furnissii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=29494; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP PATHWAY. RC STRAIN=7225; RX PubMed=8969206; DOI=10.1074/jbc.271.52.33433; RA Chitlaru E., Roseman S.; RT "Molecular cloning and characterization of a novel beta-N-acetyl-D- RT glucosaminidase from Vibrio furnissii."; RL J. Biol. Chem. 271:33433-33439(1996). RN [2] RP SEQUENCE REVISION TO 70-80. RA Chitlaru E., Roseman S.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. 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 (By CC similarity). Hydrolyzes rapidly p-nitrophenyl-N-acetyl-beta-D- CC glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, CC and slightly active on p-nitrophenyl-beta-GalNAc. May play a role in CC signal transduction between host and organism. {ECO:0000255|HAMAP- CC Rule:MF_00364, ECO:0000269|PubMed:8969206}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00364, CC ECO:0000269|PubMed:8969206}; CC -!- ACTIVITY REGULATION: Inhibited by GlcNAc, 2-acetamido-1-N-(4-L- CC aspartyl)-2-deoxy-beta-D-glucopyranosylamine (GlcNAc-Asn) and O-(2- CC acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate CC (PUGNAc). {ECO:0000269|PubMed:8969206}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:8969206}; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius. CC {ECO:0000269|PubMed:8969206}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_00364, ECO:0000269|PubMed:8969206}. CC -!- SUBUNIT: Monomer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00364}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U52818; AAC44686.2; -; Genomic_DNA. DR AlphaFoldDB; P96157; -. DR SMR; P96157; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR SABIO-RK; P96157; -. DR UniPathway; UPA00544; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1. DR HAMAP; MF_00364; NagZ; 1. DR InterPro; IPR022956; Beta_hexosaminidase_bac. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR036962; Glyco_hydro_3_N_sf. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1. DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; KW Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase; KW Peptidoglycan synthesis. FT CHAIN 1..329 FT /note="Beta-hexosaminidase" FT /id="PRO_0000210801" FT ACT_SITE 173 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT ACT_SITE 242 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 62 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 160..161 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT SITE 171 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" SQ SEQUENCE 329 AA; 36181 MW; 440C6A9B18143C34 CRC64; MGPLWLDVEG CELTAEDREI LAHPTVGGVI LFARNYHDNQ QLLALNTAIR QAAKRPILIG VDQEGGRVQR FRDGFSKIPA AQLYARSDNG TQLAEDGGWL MAAELIAHDI DLSFAPVLDK GFDCRAIGNR AFGDDVQTVL TYSSAYMRGM KSVGMATTGK HFPGHGAVIA DSHLETPYDE RDSIADDMTI FRAQIEAGIL DAMMPAHVIY PHYDAQPASG SPYWLKQVLR QELGFQGIVF SDDLSMEGAA IMGGPAERAQ QSLDAGCDMV LMCNKRESAV AVLDQLPISV VPQAQSLLKQ QQFTYRELKA TERWKQAYQA LQRLIDAHS //