ID NAGZ_IDILO Reviewed; 330 AA. AC Q5QUZ5; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 18-JUL-2018, entry version 81. 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=IL0915; OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=283942; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR; RX PubMed=15596722; DOI=10.1073/pnas.0407638102; RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., RA Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.; RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina RT loihiensis reveals amino acid fermentation as a source of carbon and RT energy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004). CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from CC peptide-linked peptidoglycan fragments, giving rise to free CC GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic CC acid-linked peptides. {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl- CC D-hexosamine residues in N-acetyl-beta-D-hexosaminides. CC {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 CC subfamily. {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; AE017340; AAV81755.1; -; Genomic_DNA. DR RefSeq; WP_011234166.1; NC_006512.1. DR ProteinModelPortal; Q5QUZ5; -. DR SMR; Q5QUZ5; -. DR STRING; 283942.IL0915; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAV81755; AAV81755; IL0915. DR KEGG; ilo:IL0915; -. DR eggNOG; ENOG4107QPA; Bacteria. DR eggNOG; COG1472; LUCA. DR HOGENOM; HOG000248526; -. DR KO; K01207; -. DR OMA; HKETPRD; -. DR OrthoDB; POG091H039J; -. DR BioCyc; ILOI283942:IL_RS04650-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000001171; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC. 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-UniPathway. 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; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Glycosidase; Hydrolase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 330 Beta-hexosaminidase. FT /FTId=PRO_0000234914. FT REGION 163 164 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT ACT_SITE 176 176 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00364}. FT ACT_SITE 246 246 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 62 62 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 70 70 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 133 133 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT SITE 174 174 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00364}. SQ SEQUENCE 330 AA; 36118 MW; D19231584F462851 CRC64; MAQLMIDIAG TELTAEDKKL LAAPAVNGLI LFTRNFASLE QLQELIREAR AAAAKPLLIA VDHEGGRVQR FREGFSAIPS MGSLQKIENE DERQRAARDL GWLMAAEVQA VGIDISFAPV LDVDDCSDVI GDRAFSAVPS EISKLASSFI EGMHEAGMAC TGKHFPGHGS VQADSHIAIP EDDRTLEQIR AHDLKPFLSL IQKLDGIMPA HVIYPQIDPQ PAGFSEFWLQ QILRSELQFN GTIFSDDLSM QGATVAGDME QRAVAALKAG CDMILVCNDR AGAVQVLDAD LPATEPESAQ RVNRMLMSSN AVSLEELKRT QRWEQAQRWL //