ID FDH_SOLTU Reviewed; 381 AA. AC Q07511; Q9ZR28; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 24-JAN-2024, entry version 132. DE RecName: Full=Formate dehydrogenase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|Ref.1}; DE Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210}; DE EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210}; DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:8278546}; DE Flags: Precursor; GN Name=FDH1 {ECO:0000303|Ref.1}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. BF15; RA Hourton-Cabassa C., Ambard-Bretteville F., Remy R., RA Colas des Francs-Small C.; RT "Evidence for multiple copies of formate dehydrogenase genes in plants: RT isolation of three potato fdh genes fdh1, fdh2 and fdh3."; RL (er) Plant Gene Register PGR98-102(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-381, PARTIAL PROTEIN SEQUENCE, FUNCTION, RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=cv. BF15; TISSUE=Tuber; RX PubMed=8278546; DOI=10.1104/pp.102.4.1171; RA Colas des Francs-Small C., Ambard-Bretteville F., Small I.D., Remy R.; RT "Identification of a major soluble protein in mitochondria from RT nonphotosynthetic tissues as NAD-dependent formate dehydrogenase."; RL Plant Physiol. 102:1171-1177(1993). RN [3] RP SEQUENCE REVISION TO N-TERMINUS. RC STRAIN=cv. BF15; TISSUE=Tuber; RA Colas des Francs-Small C.C.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 26-54, AND SUBCELLULAR LOCATION. RC STRAIN=cv. BF15; TISSUE=Tuber; RX PubMed=16668624; DOI=10.1104/pp.98.1.273; RA Colas des Francs-Small C., Ambard-Bretteville F., Darpas A., Sallantin M., RA Huet J.-C., Pernollet J.-C., Remy R.; RT "Variation of the polypeptide composition of mitochondria isolated from RT different potato tissues."; RL Plant Physiol. 98:273-278(1992). RN [5] RP FUNCTION, AND INDUCTION. RX PubMed=9490763; DOI=10.1104/pp.116.2.627; RA Hourton-Cabassa C., Ambard-Bretteville F., Moreau F., Davy de Virville J., RA Remy R., Colas des Francs-Small C.; RT "Stress induction of mitochondrial formate dehydrogenase in potato RT leaves."; RL Plant Physiol. 116:627-635(1998). CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon CC dioxide (PubMed:8278546). Involved in the cell stress response. CC Involved in formate-dependent oxygen uptake coupled to ATP synthesis CC (PubMed:9490763). {ECO:0000255|HAMAP-Rule:MF_03210, CC ECO:0000269|PubMed:8278546, ECO:0000269|PubMed:9490763}. CC -!- CATALYTIC ACTIVITY: CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03210, ECO:0000269|PubMed:8278546}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03210, CC ECO:0000269|PubMed:16668624, ECO:0000269|PubMed:8278546}. CC -!- TISSUE SPECIFICITY: Found at high levels in developing tubers, at CC intermediate level in stems, veins, stolons, and stamens, and at low CC level in leaves and roots. {ECO:0000269|PubMed:8278546}. CC -!- INDUCTION: Induced very rapidly by wounding, and slower by darkness, CC chilling, drought, hypoxia, and treatments with formate, abscisic acid, CC serine, sarcosine, pyruvate, acetate, ethanol or methanol. CC {ECO:0000269|PubMed:9490763}. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-Rule:MF_03210}. CC -!- CAUTION: There are two other putative pseudogenes, FDH2 and FDH3. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z99991; CAB17080.1; -; mRNA. DR EMBL; Z99992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z21493; CAA79702.2; -; mRNA. DR PIR; JQ2272; JQ2272. DR RefSeq; NP_001274827.1; NM_001287898.1. DR AlphaFoldDB; Q07511; -. DR SMR; Q07511; -. DR IntAct; Q07511; 1. DR STRING; 4113.Q07511; -. DR iPTMnet; Q07511; -. DR PaxDb; 4113-PGSC0003DMT400001303; -. DR GeneID; 102577429; -. DR KEGG; sot:102577429; -. DR eggNOG; KOG0069; Eukaryota. DR InParanoid; Q07511; -. DR OrthoDB; 946665at2759; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; Q07511; baseline and differential. DR GO; GO:0009507; C:chloroplast; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd05302; FDH; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR HAMAP; MF_03210; Formate_dehydrogenase; 1. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR033689; FDH_NAD-dep. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1. DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1..25 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:16668624" FT CHAIN 26..381 FT /note="Formate dehydrogenase, mitochondrial" FT /id="PRO_0000007196" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 204..205 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 224 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 259..263 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 285 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 311 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 335..338 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT SITE 287 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT SITE 335 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" SQ SEQUENCE 381 AA; 42038 MW; 920D351AC5A3A00E CRC64; MAMSRVASTA ARAITSPSSL VFTRELQASP GPKKIVGVFY KANEYAEMNP NFLGCAENAL GIREWLESKG HQYIVTPDKE GPDCELEKHI PDLHVLISTP FHPAYVTAER IKKAKNLQLL LTAGIGSDHV DLKAAAAAGL TVAEVTGSNT VSVAEDELMR ILILVRNFLP GHHQVINGEW NVAAIAHRAY DLEGKTVGTV GAGRIGRLLL QRLKPFNCNL LYHDRLKMDS ELENQIGAKF EEDLDKMLSK CDIVVINTPL TEKTKGMFDK ERIAKLKKGV LIVNNARGAI MDTQAVVDAC NSGHIAGYSG DVWYPQPAPK DHPWRYMPNQ AMTPHISGTT IDAQLRYAAG TKDMLDRYFK GEDFPAENYI VKDGELAPQY R //