Q2U9M7 (BGLH_ASPOR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 44.
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 beta-glucosidase H EC=3.2.1.21 Alternative name(s): Beta-D-glucoside glucohydrolase H Cellobiase H Gentiobiase H | ||||
| Gene names |
| ||||
| 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 | 827 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity. |
| Catalytic activity | Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. |
| Pathway | |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 3 family. Contains 1 PA14 domain. |
| Sequence caution | The sequence BAE61738.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | beta-glucosidase 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 – 827 | 827 | Probable beta-glucosidase H | PRO_0000394880 | |||||
Regions | |||||||||
| Domain | 424 – 519 | 96 | PA14 | ||||||
Sites | |||||||||
| Active site | 223 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 471 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 594 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 600 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 625 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "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 | AP007163 Genomic DNA. Translation: BAE61738.1. Sequence problems. |
| RefSeq | XP_001822871.2. XM_001822819.2. |
3D structure databases | |
| ProteinModelPortal | Q2U9M7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADAORAT00012146; CADAORAP00011903; CADAORAG00012146. |
| GeneID | 5994927. |
| KEGG | aor:AOR_1_130124. |
Phylogenomic databases | |
| eggNOG | COG1472. |
| HOGENOM | HOG000031215. |
| OrthoDB | EOG4RFQ1P. |
Enzyme and pathway databases | |
| UniPathway | UPA00696. |
Family and domain databases | |
| Gene3D | 3.20.20.300. 1 hit. 3.40.50.1700. 2 hits. |
| InterPro | IPR026891. Fn3-like. IPR026892. Glyco_hydro_3. IPR002772. Glyco_hydro_3_C. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. IPR011658. PA14. [Graphical view] |
| PANTHER | PTHR30620. PTHR30620. 1 hit. |
| Pfam | PF14310. Fn3-like. 1 hit. PF00933. Glyco_hydro_3. 1 hit. PF01915. Glyco_hydro_3_C. 1 hit. PF07691. PA14. 1 hit. [Graphical view] |
| PRINTS | PR00133. GLHYDRLASE3. |
| SMART | SM00758. PA14. 1 hit. [Graphical view] |
| SUPFAM | SSF52279. Glyco_hydro_3_C. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00775. GLYCOSYL_HYDROL_F3. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BGLH_ASPOR | ||||||||
| Accession | Primary (citable) accession number: Q2U9M7 | ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
