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 31-MAY-2011, entry version 41. DE RecName: Full=Beta-hexosaminidase; DE EC=3.2.1.52; DE AltName: Full=Beta-N-acetylhexosaminidase; DE AltName: Full=N-acetyl-beta-glucosaminidase; GN Name=nagZ; OrderedLocusNames=IL0915; OS Idiomarina loihiensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=135577; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L2-TR / ATCC BAA-735 / DSM 15497; 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: Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides (By CC similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl- CC D-hexosamine residues in N-acetyl-beta-D-hexosaminides. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ CC subfamily. 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; YP_155304.1; NC_006512.1. DR ProteinModelPortal; Q5QUZ5; -. DR SMR; Q5QUZ5; 1-327. DR GeneID; 3173409; -. DR GenomeReviews; AE017340_GR; IL0915. DR KEGG; ilo:IL0915; -. DR NMPDR; fig|283942.3.peg.773; -. DR HOGENOM; HBG617255; -. DR OMA; DLTMEGA; -. DR ProtClustDB; PRK05337; -. DR BioCyc; ILOI283942:IL0915-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00364; NagZ; 1; -. DR InterPro; IPR022956; Beta_hexosaminidase. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Gene3D; G3DSA:3.20.20.300; Glyco_hydro_3_N; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR SUPFAM; SSF51445; Glyco_hydro_cat; 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. FT CHAIN 1 330 Beta-hexosaminidase. FT /FTId=PRO_0000234914. FT ACT_SITE 246 246 By similarity. 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 //