Reviewed,
UniProtKB/Swiss-Prot P0AC42 (DHSA_ECOL6)
Last modified
June 16, 2009.
Version 34.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Succinate dehydrogenase flavoprotein subunit EC=1.3.99.1 | ||||
| Gene names |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 588 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth By similarity. |
| Catalytic activity | Succinate + acceptor = fumarate + reduced acceptor. |
| Pathway | |
| Subunit structure | Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic anchor protein. The complex forms trimers By similarity. |
| Subcellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity. |
| Sequence similarities | Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport Tricarboxylic acid cycle |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro succinate dehydrogenase activityInferred 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 – 588 | 588 | Succinate dehydrogenase flavoprotein subunit | PRO_0000158654 | |||||
Regions | |||||||||
| Nucleotide binding | 37 – 52 | 16 | FAD By similarity | ||||||
Sites | |||||||||
| Active site | 286 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 242 | 1 | Substrate By similarity | ||||||
| Binding site | 254 | 1 | Substrate By similarity | ||||||
| Binding site | 354 | 1 | Substrate By similarity | ||||||
| Binding site | 399 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 45 | 1 | Tele-8alpha-FAD histidine By similarity | ||||||
| Modified residue | 267 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| AE014075 Genomic DNA. Translation: AAN79274.1. Different initiation. | |
| RefSeq | NP_752731.2. |
3D structure databases | |
| SMR | P0AC42. Positions 1-588. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1039505. |
| GenomeReviews | Gene locus c0801 in contig AE014075_GR. |
| KEGG | ecc:c0801. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AC42. |
| OMA | P0AC42. TLEFDNL. |
Enzyme and pathway databases | |
| BRENDA | 1.3.99.1. 292881. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR003952. FRD_SDH_FAD_BS. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_frdA_Gneg. [Graphical view] |
| Pfam | PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| TIGRFAMs | TIGR01816. sdhA_forward. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit. |
| PROSITE | PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHSA_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0AC42 Secondary accession number(s): P10444, P78282 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


