Reviewed,
UniProtKB/Swiss-Prot P0AC43 (DHSA_ECO57)
Last modified
February 9, 2010.
Version 38.
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 O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 588 AA. |
| Sequence status | Complete. |
| 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 | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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_0000158653 | |||||
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] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG55047.1. BA000007 Genomic DNA. Translation: BAB34171.1. |
| PIR | D90722. |
| RefSeq | NP_286439.1. NP_308775.1. |
3D structure databases | |
| SMR | P0AC43. Positions 1-588. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0AC43. |
Genome annotation databases | |
| GeneID | 917480. 957829. |
| GenomeReviews | Gene locus Z0877 in contig AE005174_GR. Gene locus ECs0748 in contig BA000007_GR. |
| KEGG | ece:Z0877. ecs:ECs0748. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG293998. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0748-MONOMER. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR003952. FRD_SDH_FAD_BS. IPR015939. Fum_Rdtase/Succ_DH_flav-like_C. 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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AC43 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


