NAGZ_NEIMF
ID NAGZ_NEIMF Reviewed; 361 AA.
AC A1KSD9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=NMC0469;
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09769.1; -; Genomic_DNA.
DR RefSeq; WP_002219713.1; NC_008767.1.
DR AlphaFoldDB; A1KSD9; -.
DR SMR; A1KSD9; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblBacteria; CAM09769; CAM09769; NMC0469.
DR KEGG; nmc:NMC0469; -.
DR HOGENOM; CLU_008392_0_0_4; -.
DR OMA; WQMAAEM; -.
DR OrthoDB; 949956at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002286; 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; -; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis.
FT CHAIN 1..361
FT /note="Beta-hexosaminidase"
FT /id="PRO_1000005657"
FT ACT_SITE 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 174..175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 185
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ SEQUENCE 361 AA; 39062 MW; 7952FBFA5051F32C CRC64;
MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAVGGIILFR RNFQNIEQLK TLTAEIKALR
TPELIIAVDH EGGRVQRFIE GFTRLPAMST LGEIWDKDGA SAAETAAGQV GRVLATELSA
CGIDLSFTPV LDLDWGNCPV IGNRSFHHNP EAVAHLALAL QKGLAKGGMK SCGKHFPGHG
FVEGDSHLVL PEDRRSLSEL EAADLAPFHI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW
LKQILRRDIG FKGVIFSDDL TMEGACGVGG LKERARISFE AGCDIVLVCN RPDLVDELRE
DFRIPDNPAL AQRWQYMANT LGSAAAQAVM QTADFQEAQA FVAGLASPQD TAGGVKVGEA
F