ID NAGZ_SHEON Reviewed; 342 AA. AC Q8EEW2; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 109. 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=SO_2250; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014299; AAN55290.1; -; Genomic_DNA. DR RefSeq; NP_717846.1; NC_004347.2. DR RefSeq; WP_011072263.1; NZ_CP053946.1. DR AlphaFoldDB; Q8EEW2; -. DR SMR; Q8EEW2; -. DR STRING; 211586.SO_2250; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR PaxDb; 211586-SO_2250; -. DR KEGG; son:SO_2250; -. DR PATRIC; fig|211586.12.peg.2166; -. DR eggNOG; COG1472; Bacteria. DR HOGENOM; CLU_008392_0_0_6; -. DR OrthoDB; 9786661at2; -. DR PhylomeDB; Q8EEW2; -. DR BioCyc; SONE211586:G1GMP-2055-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000008186; 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; IBA:GO_Central. 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..342 FT /note="Beta-hexosaminidase" FT /id="PRO_0000210798" FT ACT_SITE 177 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT ACT_SITE 249 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT BINDING 164..165 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT SITE 175 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" SQ SEQUENCE 342 AA; 37193 MW; AB603E9104D16065 CRC64; MSYLMLDLLS LDVSEAEAEM LRHPQVGGLI LFSRNFTSRE QLIALVQQIR QIRPEILIAV DHEGGRVQRF REGFTLIPAM GDILPAAKGD MALAKRWACE LGFLMAIELL ACDIDLSFAP VLDLNGISQV IGKRSFSANP DEVIALARSF IEGMAQAGMG AVGKHFPGHG SVAADSHIAQ PIDEREGEVI FNQDILPFKE LIFNGKLSGI MPAHVIYPKV DPNPAGFSSY WLKQILRKEL GFNGVIFSDD LGMKGASFAG DYVGRAKAAL DAGCDMILVC NDNPGVMTLL NGFVWPEAAP QHPASLLKPN MAQTALALEN SARWENAKQL AEQIQLAQQA KV //