NAGZ_VIBFU
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-AUG-2022, entry version 99.
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; Proteobacteria; 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}.
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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; -; 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 Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; SSF51445; 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
