O66932 (PHSG_AQUAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 68.
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: Glycogen phosphorylase EC=2.4.1.1 | ||||
| Gene names |
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| Organism | Aquifex aeolicus (strain VF5) | ||||
| Taxonomic identifier | 224324 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex |
Protein attributes
| Sequence length | 692 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties By similarity. |
| Catalytic activity | (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Sequence similarities | Belongs to the glycogen phosphorylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glycogen metabolism |
| Ligand | Pyridoxal phosphate |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000657 Genomic DNA. Translation: AAC06896.1. |
| PIR | H70362. |
| RefSeq | NP_213492.1. NC_000918.1. |
3D structure databases | |
| ProteinModelPortal | O66932. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GT35. Glycosyltransferase Family 35. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1193381. |
| GenomeReviews | Gene locus aq_717 in contig AE000657_GR. |
| KEGG | aae:aq_717. |
| NMPDR | fig|224324.1.peg.507. |
| PATRIC | 20958888. VBIAquAeo85532_0575. |
Phylogenomic databases | |
| HOGENOM | HBG302557. |
| OMA | GWWPEAC. |
| PhylomeDB | O66932. |
Enzyme and pathway databases | |
| BioCyc | AAEO224324:AQ_717-MONOMER. |
| BRENDA | 2.4.1.1. 396. |
Family and domain databases | |
| InterPro | IPR011834. Agluc_phsphrylas. IPR000811. Glyco_trans_35. IPR024517. Glycogen_phosphorylase_DUF3417. [Graphical view] |
| KO | K00688. |
| PANTHER | PTHR11468. Glyco_trans_35. 1 hit. |
| Pfam | PF11897. DUF3417. 1 hit. PF00343. Phosphorylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000460. Pprylas_GlgP. 1 hit. |
| TIGRFAMs | TIGR02094. More_P_ylases. 1 hit. |
| PROSITE | PS00102. PHOSPHORYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PHSG_AQUAE | ||||||||
| Accession | Primary (citable) accession number: O66932 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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