P58067 (NAGZ_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-hexosaminidase EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase N-acetyl-beta-glucosaminidase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 341 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides By similarity. HAMAP MF_00364 |
| Catalytic activity | Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. HAMAP MF_00364 |
| Pathway | Cell wall biogenesis; peptidoglycan recycling. HAMAP MF_00364 |
| Subunit structure | Monomer Potential. |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00364. |
| Sequence similarities | Belongs to the glycosyl hydrolase 3 family. NagZ subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Cellular component | Cytoplasm |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell divisionInferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 341 | 341 | Beta-hexosaminidase HAMAP MF_00364 | PRO_0000210787 | |||||
Sites | |||||||||
| Active site | 248 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG55853.1. BA000007 Genomic DNA. Translation: BAB34908.1. |
| PIR | A85674. E90814. |
| RefSeq | NP_287241.1. NC_002655.2. NP_309512.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P58067. |
| SMR | P58067. Positions 1-325. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH3. Glycoside Hydrolase Family 3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000027083; EBESCP00000025976; EBESCG00000026135. EBESCT00000059942; EBESCP00000057770; EBESCG00000058989. |
| GeneID | 913266. 959459. |
| GenomeReviews | Gene locus Z1746 in contig AE005174_GR. Gene locus ECs1485 in contig BA000007_GR. |
| KEGG | ece:Z1746. ecs:ECs1485. |
| PATRIC | 18352211. VBIEscCol44059_1332. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000011903. |
| HOGENOM | HBG617255. |
| OMA | DLTMEGA. |
| ProtClustDB | PRK05337. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS1485-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00364. NagZ. [Tree] |
| InterPro | IPR022956. Beta_hexosaminidase. IPR019800. Glyco_hydro_3_AS. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.300. Glyco_hydro_3_N. 1 hit. |
| KO | K01207. |
| Pfam | PF00933. Glyco_hydro_3. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00775. GLYCOSYL_HYDROL_F3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NAGZ_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P58067 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with