Q92407 (HXKG_ASPNG) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 61.
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: Glucokinase EC=2.7.1.2 Alternative name(s): Glucose kinase Short name=GLK | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 495 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The enzyme has great affinity for glucose. Mannose, 2-deoxyglucose and glucosamine can serve as substrates. |
| Catalytic activity | ATP + D-glucose = ADP + D-glucose 6-phosphate. |
| Subunit structure | Monomer Probable. |
| Sequence similarities | Belongs to the hexokinase family. |
| Biophysicochemical properties | pH dependence: Activity is relatively constant from pH 7.5 to 9.0. Below pH 7.5, activity decreases with pH. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Gene Ontology (GO) | |
| Biological_process | glucose 6-phosphate metabolic process Inferred from electronic annotation. Source: GOC glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glucokinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and biochemical characterisation of an Aspergillus niger glucokinase. Evidence for the presence of separate glucokinase and hexokinase enzymes." Panneman H., Ruijter G.J.G., van den Broeck H.C., Driever E.T.M., Visser J. Eur. J. Biochem. 240:518-525(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X99626 Genomic DNA. Translation: CAA67949.1. |
| PIR | S74210. |
3D structure databases | |
| ProteinModelPortal | Q92407. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG5026. |
Family and domain databases | |
| InterPro | IPR001312. Hexokinase. IPR022673. Hexokinase_C. IPR019807. Hexokinase_CS. IPR022672. Hexokinase_N. [Graphical view] |
| PANTHER | PTHR19443. PTHR19443. 1 hit. |
| Pfam | PF00349. Hexokinase_1. 1 hit. PF03727. Hexokinase_2. 1 hit. [Graphical view] |
| PRINTS | PR00475. HEXOKINASE. |
| PROSITE | PS00378. HEXOKINASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HXKG_ASPNG | ||||||||
| Accession | Primary (citable) accession number: Q92407 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
