Q6B8T1 (ODPB_GRATL) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 45.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit beta EC=1.2.4.1 | ||||||
| Gene names |
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| Encoded on | Plastid; Chloroplast | ||||||
| Organism | Gracilaria tenuistipitata var. liui (Red alga) | ||||||
| Taxonomic identifier | 285951 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Rhodophyta › Florideophyceae › Gracilariales › Gracilariaceae › Gracilaria › ![]() |
Protein attributes
| Sequence length | 323 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 By similarity. |
| 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 |
| 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)
Sequences
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References
| [1] | "Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids." Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C. J. Mol. Evol. 59:464-477(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY673996 Genomic DNA. Translation: AAT79704.1. |
| RefSeq | YP_063629.1. NC_006137.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1W88 based on UniProtKB P21874. |
| ProteinModelPortal | Q6B8T1. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2943994. |
Phylogenomic databases | |
| ProtClustDB | CHL00144. |
Family and domain databases | |
| Gene3D | 3.40.50.920. 1 hit. |
| InterPro | IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view] |
| Pfam | PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| SUPFAM | SSF52922. Transketo_C_like. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODPB_GRATL | ||||||||
| Accession | Primary (citable) accession number: Q6B8T1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with
