FDH_SOLTU
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 03-AUG-2022, entry version 127.
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}.
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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.PGSC0003DMT400001303; -.
DR iPTMnet; Q07511; -.
DR PRIDE; Q07511; -.
DR GeneID; 102577429; -.
DR KEGG; sot:102577429; -.
DR eggNOG; KOG0069; Eukaryota.
DR InParanoid; Q07511; -.
DR OrthoDB; 700058at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q07511; baseline.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
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 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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 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
