Reviewed,
UniProtKB/Swiss-Prot Q07WU7 (FRDA_SHEFN)
Last modified
November 25, 2008.
Version 18.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fumarate reductase flavoprotein subunit EC=1.3.99.1 Alternative name(s): Flavocytochrome c Flavocytochrome c3 Short name=Fcc3 | ||||||
| Gene names |
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| Organism | Shewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 318167 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella |
Protein attributes
| Sequence length | 596 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional By similarity. |
| Catalytic activity | Succinate + acceptor = fumarate + reduced acceptor. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | PeriplasmBy similarity. |
| Induction | By anaerobiosis and fumarate. |
| Sequence similarities | In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. Contains 1 cytochrome c domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | FAD Flavoprotein Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | |||||||
| Chain | 26 – 596 | 571 | Fumarate reductase flavoprotein subunit | PRO_0000269231 | |||||
Regions | |||||||||
| Domain | 26 – 142 | 117 | Cytochrome c | ||||||
| Nucleotide binding | 154 – 168 | 15 | FAD Potential | ||||||
| Nucleotide binding | 157 – 168 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 181 – 182 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 189 – 190 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 194 – 196 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 574 – 575 | 2 | FAD By similarity | ||||||
| Region | 143 – 596 | 454 | Flavoprotein-like | ||||||
Sites | |||||||||
| Active site | 427 | 1 | Proton donor By similarity | ||||||
| Metal binding | 33 | 1 | Iron (heme 2 axial ligand) | ||||||
| Metal binding | 43 | 1 | Iron (heme 1 axial ligand) | ||||||
| Metal binding | 65 | 1 | Iron (heme 2 axial ligand) | ||||||
| Metal binding | 83 | 1 | Iron (heme 3 axial ligand) | ||||||
| Metal binding | 86 | 1 | Iron (heme 4 axial ligand) | ||||||
| Metal binding | 97 | 1 | Iron (heme 3 axial ligand) | ||||||
| Metal binding | 100 | 1 | Iron (heme 1 axial ligand) | ||||||
| Metal binding | 111 | 1 | Iron (heme 4 axial ligand) | ||||||
| Binding site | 39 | 1 | Heme 1 (covalent) | ||||||
| Binding site | 42 | 1 | Heme 1 (covalent) | ||||||
| Binding site | 61 | 1 | Heme 2 (covalent) | ||||||
| Binding site | 64 | 1 | Heme 2 (covalent) | ||||||
| Binding site | 93 | 1 | Heme 3 (covalent) | ||||||
| Binding site | 96 | 1 | Heme 3 (covalent) | ||||||
| Binding site | 107 | 1 | Heme 4 (covalent) | ||||||
| Binding site | 110 | 1 | Heme 4 (covalent) | ||||||
| Binding site | 390 | 1 | Substrate By similarity | ||||||
| Binding site | 402 | 1 | Substrate By similarity | ||||||
| Binding site | 529 | 1 | Substrate By similarity | ||||||
| Binding site | 569 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria." Pealing S.L., Black A.C., Manson F.D.C., Ward F.B., Chapman S.K., Reid G.A. Biochemistry 31:12132-12140(1992) [PubMed: 1333793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-38. |
| [2] | "Complete sequence of Shewanella frigidimarina NCIMB 400." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. Richardson P.Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| L04283 Genomic DNA. Translation: AAA70385.1. CP000447 Genomic DNA. Translation: ABI73517.1. Different initiation. | |
| RefSeq | YP_752356.1. |
3D structure databases | |
| SMR | Q07WU7. Positions 26-593. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4280583. |
| GenomeReviews | Gene locus Sfri_3690 in contig CP000447_GR. |
| KEGG | sfr:Sfri_3690. |
| NMPDR | fig|318167.10.peg.3515. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q07WU7. |
Family and domain databases | |
| InterPro | IPR003953. FAD_bind2_N. IPR012286. Fcc3_N_cyt. IPR010960. Flavocytochrome_c. IPR011031. Multihaem_cyt. [Graphical view] |
| Gene3D | G3DSA:1.10.1130.10. Fcc3_N_cyt. 1 hit. |
| Pfam | PF00890. FAD_binding_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01813. flavo_cyto_c. 1 hit. |
| PROSITE | PS51008. MULTIHEME_CYTC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FRDA_SHEFN | ||||||||
| Accession | Primary (citable) accession number: Q07WU7 Secondary accession number(s): Q02469, Q9X969 | ||||||||
| 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


