Q2UPQ4 (EGLB_ASPOR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
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: Probable endo-beta-1,4-glucanase B Short name=Endoglucanase B EC=3.2.1.4 Alternative name(s): Carboxymethylcellulase B Cellulase B | ||||||
| Gene names |
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| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome] | ||||||
| Taxonomic identifier | 510516 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › ![]() |
Protein attributes
| Sequence length | 333 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 5 (cellulase A) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cellulase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||
| Chain | 18 – 333 | 316 | Probable endo-beta-1,4-glucanase B | PRO_0000394057 | |||||
Sites | |||||||||
| Active site | 160 | 1 | Proton donor By similarity | ||||||
| Active site | 267 | 1 | Nucleophile By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 37 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 100 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 145 | 1 | G → E in BAD72778. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and overexpression of a novel cellulase gene, celE, from Aspergillus oryzae KBN616." Yasuda-Yoshino S., Kitamoto N. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KBN616. |
| [2] | "Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H.Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB195229 Genomic DNA. Translation: BAD72778.1. AP007151 Genomic DNA. Translation: BAE56461.1. |
| RefSeq | XP_001818463.1. XM_001818411.1. |
3D structure databases | |
| ProteinModelPortal | Q2UPQ4. |
| SMR | Q2UPQ4. Positions 30-332. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5062.CADAORAP00003359. |
Protein family/group databases | |
| CAZy | GH5. Glycoside Hydrolase Family 5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADAORAT00003416; CADAORAP00003359; CADAORAG00003416. |
| GeneID | 5990408. |
| KEGG | aor:AOR_1_2698174. |
Phylogenomic databases | |
| eggNOG | COG2730. |
| HOGENOM | HOG000111120. |
| KO | K01179. |
| OrthoDB | EOG43NBNF. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Pfam | PF00150. Cellulase. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | EGLB_ASPOR | ||||||||
| Accession | Primary (citable) accession number: Q2UPQ4 Secondary accession number(s): Q5TKT6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
