F4EM25 (F4EM25_BACAM) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 10.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: 2-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169 EC=1.2.4.2 HAMAP-Rule MF_01169 Alternative name(s): Alpha-ketoglutarate dehydrogenase HAMAP-Rule MF_01169 | ||||
| Gene names |
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| Organism | Bacillus amyloliquefaciens (Bacillus velezensis) | ||||
| Taxonomic identifier | 1390 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 944 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Catalytic activity | 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Cofactor | Thiamine pyrophosphate By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. HAMAP-Rule MF_01169 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Ligand | Thiamine pyrophosphate HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Molecular function | Oxidoreductase HAMAP-Rule MF_01169 SAAS SAAS023784 |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamine pyrophosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Complete Genome Sequence of Bacillus amyloliquefaciens LL3, Which Exhibits Glutamic Acid-Independent Production of Poly-{gamma}-Glutamic Acid." Geng W., Cao M., Song C., Xie H., Liu L., Yang C., Feng J., Zhang W., Jin Y., Du Y., Wang S. J. Bacteriol. 193:3393-3394(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: LL3 EMBL AEB63646.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002634 Genomic DNA. Translation: AEB63646.1. |
| RefSeq | YP_005545874.1. NC_017190.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEB63646; AEB63646; LL3_02109. |
| GeneID | 12203139. |
| KEGG | bql:LL3_02109. |
| PATRIC | 54316465. VBIBacAmy188832_2077. |
Phylogenomic databases | |
| KO | K00164. |
Family and domain databases | |
| HAMAP | MF_01169. SucA_OdhA. |
| InterPro | IPR011603. 2oxoglutarate_DH_E1. IPR023784. 2oxoglutarate_DH_E1_bac. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view] |
| PANTHER | PTHR23152. PTHR23152. 1 hit. |
| Pfam | PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view] |
| PIRSF | PIRSF000157. Oxoglu_dh_E1. 1 hit. |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | F4EM25_BACAM | ||||||||
| Accession | Primary (citable) accession number: F4EM25 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
