Reviewed,
UniProtKB/Swiss-Prot P51267 (ODPA_PORPU)
Last modified
February 9, 2010.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit alpha EC=1.2.4.1 | ||||
| Gene names |
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| Encoded on | Plastid; Chloroplast | ||||
| Organism | Porphyra purpurea | ||||
| Taxonomic identifier | 2787 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Rhodophyta › Bangiophyceae › Bangiales › Bangiaceae › Porphyra |
Protein attributes
| Sequence length | 344 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Thiamine pyrophosphate. |
| Subunit structure | Heterodimer of an alpha and a beta chain By similarity. |
| Subcellular location |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Chloroplast Plastid |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) 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 – 344 | 344 | Pyruvate dehydrogenase E1 component subunit alpha | PRO_0000162215 | |||
Sequences
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References
| [1] | "Complete nucleotide sequence of the Porphyra purpurea chloroplast genome." Reith M.E., Munholland J. Plant Mol. Biol. Rep. 13:333-335(1995) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Avonport. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U38804 Genomic DNA. Translation: AAC08153.1. |
| PIR | S73188. |
| RefSeq | NP_053877.1. |
3D structure databases | |
| SMR | P51267. Positions 17-343. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 809896. |
Enzyme and pathway databases | |
| BRENDA | 1.2.4.1. 279956. |
Family and domain databases | |
| InterPro | IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view] |
| Pfam | PF00676. E1_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03182. PDH_E1_alph_y. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODPA_PORPU | ||||||||
| Accession | Primary (citable) accession number: P51267 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


