NAGZ_CROS8
ID NAGZ_CROS8 Reviewed; 341 AA.
AC A7MFT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-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=ESA_02237;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77486.1; -; Genomic_DNA.
DR RefSeq; WP_012125071.1; NC_009778.1.
DR AlphaFoldDB; A7MFT1; -.
DR SMR; A7MFT1; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblBacteria; ABU77486; ABU77486; ESA_02237.
DR KEGG; esa:ESA_02237; -.
DR PATRIC; fig|290339.8.peg.1998; -.
DR HOGENOM; CLU_008392_0_0_6; -.
DR OMA; WQMAAEM; -.
DR OrthoDB; 949956at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000260; 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..341
FT /note="Beta-hexosaminidase"
FT /id="PRO_1000005653"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 248
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 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 163..164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 174
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ SEQUENCE 341 AA; 37576 MW; FC244DFB713E6EE3 CRC64;
MGPVMLDVEG FELDAEEREI LAHPLVGGLI LFTRNYHDPE QLRELVRQIR SSARNHLVIA
VDQEGGRVQR FREGFTRLPA AQSFAALLGM DAGGKLAEEA GWLMACEMIA MDIDISFAPV
LDVGHLSAAI GERSFHEEPE NVLAMAKRFI TGMQSAGMKA TGKHFPGHGA VSADSHKETP
RDPRPAAEIR RHDMLPFREL ISYNMLDAVM PAHVVYSDVD PLPASGSPYW LKQVLRKELG
FDGVIFSDDL SMEGAAILGS YAERGQAALD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
TRLYHKGVIT RQELMASARW KQVSGELTAL HERWQTHKAG Q