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Database: UniProt/TrEMBL
Entry: D4I112_ERWAC
LinkDB: D4I112_ERWAC
Original site: D4I112_ERWAC 
ID   D4I112_ERWAC            Unreviewed;       339 AA.
AC   D4I112;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   11-JUN-2014, entry version 29.
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=EAMY_1487;
OS   Erwinia amylovora (strain CFBP1430).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Erwinia.
OX   NCBI_TaxID=665029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP1430;
RX   PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA   Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia
RT   amylovora CFBP 1430 and comparison to other Erwinia spp.";
RL   Mol. Plant Microbe Interact. 23:384-393(2010).
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 (By 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.
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DR   EMBL; FN434113; CBA20437.1; -; Genomic_DNA.
DR   RefSeq; YP_003530845.1; NC_013961.1.
DR   ProteinModelPortal; D4I112; -.
DR   EnsemblBacteria; CBA20437; CBA20437; EAMY_1487.
DR   GeneID; 8914089; -.
DR   KEGG; eam:EAMY_1487; -.
DR   PATRIC; 35407112; VBIErwAmy142366_1447.
DR   HOGENOM; HOG000248526; -.
DR   KO; K01207; -.
DR   OMA; YTEADPR; -.
DR   BioCyc; EAMY665029:GCM3-1541-MONOMER; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-HAMAP.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP.
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; 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.
FT   REGION      159    160       Substrate binding (By similarity).
FT   ACT_SITE    172    172       Proton donor/acceptor (By
FT                                similarity){EA3}.
FT   ACT_SITE    244    244       Nucleophile (By similarity){EA3}.
FT   BINDING      58     58       Substrate (By similarity){EA3}.
FT   BINDING      66     66       Substrate (By similarity){EA3}.
FT   BINDING     129    129       Substrate (By similarity){EA3}.
FT   SITE        170    170       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   339 AA;  37374 MW;  3DB54FB9309C6469 CRC64;
     MLDVLGCELD AEEREILQHP LTGGLILFSR NYHDPVQLRE LVRQIRSASR HRLLVAVDQE
     GGRVQRFRQG FSRLPAMQAF AALNPSPEAE KLAQQAGWLM ASEMIAMDID ISFAPVLDIG
     HGSAAIGERS FHQDPAVALQ MARCFIRGMR DAGMKTTGKH FPGHGAVSAD SHKETPRDTR
     SEAEIRQQDM PIFQQLIAEQ ALDAIMPAHV IYTQVDPRPA SGSPHWLKSV LRQELGYDGV
     IFSDDLSMEG AAIMGSYPER ARSALEAGCD MILVCNNRPG AVSVLDNLPA MASARAARLF
     HRGKVTRQQL IDSPRWKETS AALARLQDRW LAHKADAGS
//
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