P13670 (CHB_VIBHA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 104.
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: N,N'-diacetylchitobiase Short name=Chitobiase EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase N-acetyl-beta-glucosaminidase | ||
| Gene names |
| ||
| Organism | Vibrio harveyi (Beneckea harveyi) | ||
| Taxonomic identifier | 669 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 883 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Hydrolysis of terminal, non-reducing N-acetyl-beta-D-glucosamine residues in chitobiose and higher analogs, and in glycoproteins. |
| Catalytic activity | Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. |
| Pathway | |
| Subcellular location | |
| Induction | By chitobiose. |
| Post-translational modification | This protein is probably a lipoprotein, its processing is inhibited by globomycin. |
| Sequence similarities | Belongs to the glycosyl hydrolase 20 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Chitin degradation Polysaccharide degradation |
| Cellular component | Cell membrane Cell outer membrane Membrane |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Lipoprotein Palmitate |
| Gene Ontology (GO) | |
| Biological_process | chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway polysaccharide catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC polysaccharide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | |||||||||
| Chain | 18 – 883 | 866 | N,N'-diacetylchitobiase | PRO_0000012019 | |||||||
Sites | |||||||||||
| Active site | 537 | 1 | Proton donor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Lipidation | 18 | 1 | N-palmitoyl cysteine Probable | ||||||||
| Lipidation | 18 | 1 | S-diacylglycerol cysteine | ||||||||
| Disulfide bond | 54 ↔ 64 | By similarity | |||||||||
| Disulfide bond | 394 ↔ 402 | By similarity | |||||||||
| Disulfide bond | 502 ↔ 577 | By similarity | |||||||||
Sequences
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References
| [1] | "N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships." Soto-Gil R.W., Zysking J.W. J. Biol. Chem. 264:14778-14783(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J05004 Genomic DNA. Translation: AAA88682.1. |
| PIR | A36511. |
3D structure databases | |
| ProteinModelPortal | P13670. |
| SMR | P13670. Positions 25-882. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH20. Glycoside Hydrolase Family 20. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00349. |
Family and domain databases | |
| Gene3D | 2.60.40.290. 1 hit. 2.60.40.320. 1 hit. 3.20.20.80. 1 hit. |
| InterPro | IPR025705. Beta_hexosaminidase_sua/sub. IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR004866. CHB/HEX_N_dom. IPR004867. CHB_HEX_C_dom. IPR013812. Glyco_hydro_2/20_Ig-like. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. IPR014756. Ig_E-set. [Graphical view] |
| Pfam | PF03173. CHB_HEX. 1 hit. PF03174. CHB_HEX_C. 1 hit. PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view] |
| PRINTS | PR00738. GLHYDRLASE20. |
| SMART | SM01081. CHB_HEX. 1 hit. [Graphical view] |
| SUPFAM | SSF49384. Cellul_bind. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit. |
| PROSITE | PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHB_VIBHA | ||||||||
| Accession | Primary (citable) accession number: P13670 | ||||||||
| 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
