ID   NAGZ_HAEDU              Reviewed;         344 AA.
AC   Q7VNI8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
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};
GN   OrderedLocusNames=HD_0542;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
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; AE017143; AAP95482.1; -; Genomic_DNA.
DR   RefSeq; WP_010944535.1; NC_002940.2.
DR   AlphaFoldDB; Q7VNI8; -.
DR   SMR; Q7VNI8; -.
DR   STRING; 233412.HD_0542; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; hdu:HD_0542; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_0_6; -.
DR   OrthoDB; 9786661at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001022; Chromosome.
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   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN           1..344
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000210788"
FT   ACT_SITE        175
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         162..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   SITE            173
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   344 AA;  38985 MW;  14F5BB166A559689 CRC64;
     MLIIDIKGTE ISQQEIEILS HPLVAGLILF SRNFVDKAQL TALIKEIRQK VTKPLLITID
     QEGGRVQRFR EGFTRLPAMQ AFGQLAKHPQ EAIIWAKQAG WLMAAEMFAL DIDLSFAPVL
     DLGHKCKAIG DRSFGEKVTQ ILPIAEGFID GMREIGMATT GKHFPGHGQV IADSHLETPF
     DERAKANIFN YDIQPFEYFI AKNKLSAIMP AHVVYTQCDP HPASGSTYWL QQVLRQQLQF
     KGIIFSDDLG MQGANLMGNF LQRSEQAINA GCDLLLLCNQ PEGVIEVLNG LTYQPNKLEQ
     QKYLTLKKRR TIDFQQLASS PRYQQTKQHL EQLHECWLEW QTTH
//