A5A6I5 (ALDOA_PANTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 43.
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: Fructose-bisphosphate aldolase A EC=4.1.2.13 Alternative name(s): Muscle-type aldolase | ||
| Gene names |
| ||
| Organism | Pan troglodytes (Chimpanzee) [Reference proteome] | ||
| Taxonomic identifier | 9598 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan![]() |
Protein attributes
| Sequence length | 364 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein By similarity. |
| Catalytic activity | D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. |
| Pathway | |
| Subunit structure | Homotetramer. Interacts with SNX9 and WAS By similarity. |
| Miscellaneous | In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain. |
| Sequence similarities | Belongs to the class I fructose-bisphosphate aldolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Schiff base |
| Molecular function | Lyase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerizationInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | fructose-bisphosphate aldolase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 364 | 363 | Fructose-bisphosphate aldolase A | PRO_0000295307 | |||||
Sites | |||||||||
| Active site | 188 | 1 | Proton acceptor By similarity | ||||||
| Active site | 230 | 1 | Schiff-base intermediate with dihydroxyacetone-P | ||||||
| Binding site | 56 | 1 | Substrate | ||||||
| Binding site | 147 | 1 | Substrate | ||||||
| Site | 364 | 1 | Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate | ||||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 5 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 9 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 13 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 36 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 37 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 39 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 42 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 46 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 65 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 108 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 111 | 1 | N6-malonyllysine By similarity | ||||||
| Modified residue | 204 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 223 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 235 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 241 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 312 | 1 | N6-malonyllysine By similarity | ||||||
| Modified residue | 330 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 354 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 356 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 364 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome." Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M. Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB222113 mRNA. Translation: BAF62358.1. |
| RefSeq | NP_001138305.1. NM_001144833.1. |
| UniGene | Ptr.406. |
3D structure databases | |
| ProteinModelPortal | A5A6I5. |
| SMR | A5A6I5. Positions 2-364. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9598.ENSPTRP00000055755. |
Proteomic databases | |
| PRIDE | A5A6I5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 454362. |
| KEGG | ptr:454362. |
Organism-specific databases | |
| CTD | 226. |
Phylogenomic databases | |
| eggNOG | COG3588. |
| HOGENOM | HOG000220876. |
| HOVERGEN | HBG002386. |
| InParanoid | A5A6I5. |
| KO | K01623. |
| OrthoDB | EOG4X3H1J. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00183. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| InterPro | IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view] |
| PANTHER | PTHR11627. PTHR11627. 1 hit. |
| Pfam | PF00274. Glycolytic. 1 hit. [Graphical view] |
| PROSITE | PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20836037. |
Entry information
| Entry name | ALDOA_PANTR | ||||||||
| Accession | Primary (citable) accession number: A5A6I5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
