Reviewed,
UniProtKB/Swiss-Prot Q07511 (FDH_SOLTU)
Last modified
January 19, 2010.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Formate dehydrogenase, mitochondrial EC=1.2.1.2 Alternative name(s): NAD-dependent formate dehydrogenase Short name=FDH | ||
| Gene names |
| ||
| Organism | Solanum tuberosum (Potato) | ||
| Taxonomic identifier | 4113 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum |
Protein attributes
| Sequence length | 381 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 | Involved in formate-dependent oxygen uptake coupled to ATP synthesis. |
| Catalytic activity | Formate + NAD+ = CO2 + NADH. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Found at high levels in developing tubers, at intermediate level in stems, veins, stolons, and stamens, and at low level in leaves and roots. |
| Induction | Induced very rapidly by wounding, and slower by darkness, chilling, drought, hypoxia, and treatments with formate, abscisic acid, serine, sarcosine, pyruvate, acetate, ethanol or methanol. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily. |
| Caution | There are two other putative pseudogenes, FDH2 and FDH3. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro formate dehydrogenase activityInferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 25 | 25 | Mitochondrion Ref.4 | ||||||
| Chain | 26 – 381 | 356 | Formate dehydrogenase, mitochondrial | PRO_0000007196 | |||||
Regions | |||||||||
| Nucleotide binding | 204 – 205 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 285 – 287 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 335 – 338 | 4 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 287 | 1 | By similarity | ||||||
| Active site | 335 | 1 | Proton donor By similarity | ||||||
| Binding site | 258 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 311 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "Evidence for multiple copies of formate dehydrogenase genes in plants: isolation of three potato fdh genes fdh1, fdh2 and fdh3." Hourton-Cabassa C., Ambard-Bretteville F., Remy R., Colas des Francs-Small C. Plant Gene Register PGR98-102 Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. BF15. |
| [2] | "Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase." Colas des Francs-Small C., Ambard-Bretteville F., Small I.D., Remy R. Plant Physiol. 102:1171-1177(1993) [PubMed: 8278546] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-381, PARTIAL PROTEIN SEQUENCE. Strain: cv. BF15. Tissue: Tuber. |
| [3] | Colas des Francs-Small C.C. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS. Strain: cv. BF15. Tissue: Tuber. |
| [4] | "Variation of the polypeptide composition of mitochondria isolated from different potato tissues." Colas des Francs-Small C., Ambard-Bretteville F., Darpas A., Sallantin M., Huet J.-C., Pernollet J.-C., Remy R. Plant Physiol. 98:273-278(1992) [PubMed: 16668624] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-54. Strain: cv. BF15. Tissue: Tuber. |
| [5] | "Stress induction of mitochondrial formate dehydrogenase in potato leaves." Hourton-Cabassa C., Ambard-Bretteville F., Moreau F., Davy de Virville J., Remy R., Colas des Francs-Small C. Plant Physiol. 116:627-635(1998) [PubMed: 9490763] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z99991 mRNA. Translation: CAB17080.1. Z99992 Genomic DNA. No translation available. Z21493 mRNA. Translation: CAA79702.2. |
| PIR | JQ2272. |
3D structure databases | |
| SMR | Q07511. Positions 33-376. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q07511. 1 interaction. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.2. 296. |
Family and domain databases | |
| InterPro | IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FDH_SOLTU | ||||||||
| Accession | Primary (citable) accession number: Q07511 Secondary accession number(s): Q9ZR28 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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