P29408 (PGK1_MACEU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 73.
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: Phosphoglycerate kinase 1 EC=2.7.2.3 | ||||
| Gene names |
| ||||
| Organism | Macropus eugenii (Tammar wallaby) | ||||
| Taxonomic identifier | 9315 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Diprotodontia › Macropodidae › Macropus![]() |
Protein attributes
| Sequence length | 417 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)
| Catalytic activity | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the phosphoglycerate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoglycerate kinase activityInferred 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 – 417 | 416 | Phosphoglycerate kinase 1 | PRO_0000145833 | |||||
Regions | |||||||||
| Nucleotide binding | 373 – 376 | 4 | ATP By similarity | ||||||
| Region | 24 – 26 | 3 | Substrate binding By similarity | ||||||
| Region | 63 – 66 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | Substrate By similarity | ||||||
| Binding site | 123 | 1 | Substrate By similarity | ||||||
| Binding site | 171 | 1 | Substrate By similarity | ||||||
| Binding site | 220 | 1 | ATP By similarity | ||||||
| Binding site | 313 | 1 | ATP; via carbonyl oxygen By similarity | ||||||
| Binding site | 344 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 11 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 75 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 76 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 86 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 97 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 131 | 1 | N6-acetyllysine; alternate By similarity | ||||||
| Modified residue | 131 | 1 | N6-malonyllysine; alternate By similarity | ||||||
| Modified residue | 146 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 196 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 199 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 203 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 267 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 291 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 390 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "PCR derived cDNA clones for X-linked phosphoglycerate kinase-1 in a marsupial, the tammar wallaby (Macropus eugenii)." Zehavi-Feferman T., Cooper D.W. Biochem. Biophys. Res. Commun. 187:26-31(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X64296 mRNA. Translation: CAA45574.1. |
| PIR | PC1118. |
3D structure databases | |
| ProteinModelPortal | P29408. |
| SMR | P29408. Positions 2-417. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P29408. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG008177. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00185. |
Family and domain databases | |
| Gene3D | 3.40.50.1260. 1 hit. 3.40.50.1270. 1 hit. |
| InterPro | IPR001576. Phosphoglycerate_kinase. IPR015901. Phosphoglycerate_kinase_C. IPR015911. Phosphoglycerate_kinase_CS. IPR015824. Phosphoglycerate_kinase_N. [Graphical view] |
| PANTHER | PTHR11406. PTHR11406. 1 hit. |
| Pfam | PF00162. PGK. 1 hit. [Graphical view] |
| PIRSF | PIRSF000724. Pgk. 1 hit. |
| PRINTS | PR00477. PHGLYCKINASE. |
| SUPFAM | SSF53748. PGK. 1 hit. |
| PROSITE | PS00111. PGLYCERATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PGK1_MACEU | ||||||||
| Accession | Primary (citable) accession number: P29408 | ||||||||
| Entry history |
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| 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
