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 24-JUL-2024, entry version 107. 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; Pseudomonadota; 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., Campbell S., RA 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 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; AE017340; AAV81755.1; -; Genomic_DNA. DR RefSeq; WP_011234166.1; NC_006512.1. DR AlphaFoldDB; Q5QUZ5; -. DR SMR; Q5QUZ5; -. DR STRING; 283942.IL0915; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR KEGG; ilo:IL0915; -. DR eggNOG; COG1472; Bacteria. DR HOGENOM; CLU_008392_0_0_6; -. DR OrthoDB; 9786661at2; -. 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-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: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; 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 InterPro; IPR050226; NagZ_Beta-hexosaminidase. 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..330 FT /note="Beta-hexosaminidase" FT /id="PRO_0000234914" FT ACT_SITE 176 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364" FT ACT_SITE 246 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 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 //