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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   19-FEB-2014, entry version 27.
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: 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.
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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; MGSYPER; -.
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   ACT_SITE    244    244       By 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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