NAGZ_NEIG2
ID NAGZ_NEIG2 Reviewed; 361 AA.
AC B4RQ67;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=NGK_0181;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF28879.1; -; Genomic_DNA.
DR RefSeq; WP_003690594.1; NC_011035.1.
DR AlphaFoldDB; B4RQ67; -.
DR SMR; B4RQ67; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PRIDE; B4RQ67; -.
DR EnsemblBacteria; ACF28879; ACF28879; NGK_0181.
DR GeneID; 66752401; -.
DR KEGG; ngk:NGK_0181; -.
DR HOGENOM; CLU_008392_0_0_4; -.
DR OMA; WQMAAEM; -.
DR OrthoDB; 949956at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002564; 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_1000121064"
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; 39211 MW; 437CCCBD9167CA90 CRC64;
MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAIGGIILFR RNFQNIEQLK TLTAEIKALR
TPELIIAVDH EGGRVQRFIE GFTRLPAMST LGEIWDSEGA ETAETHAEHI GWVLATELSA
CGIDLSFTPV LDLDWGNCAV IGNRSFHRNP EAVARLALAL QKGLAKGGMK SCGKHFPGHG
FVEGDSHLVL PEDGRSLDEL EAADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW
LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIILVCN RPDLVDELRD
GFTIPDNQDL AGRWQYMENS LGHEAVQAVI QTTGFQAAQA FVAGLASPQD TAGGVKVGEA
F