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   16-JUN-2009, entry version 68.
DE   RecName: Full=Formate dehydrogenase, mitochondrial;
DE            EC=1.2.1.2;
DE   AltName: Full=NAD-dependent formate dehydrogenase;
DE            Short=FDH;
DE   Flags: Precursor;
GN   Name=FDH1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   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
RT   plants: isolation of three potato fdh genes fdh1, fdh2 and fdh3.";
RL   (er) Plant Gene Register PGR98-102.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-381, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. BF15; TISSUE=Tuber;
RX   MEDLINE=94105343; 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.
RC   STRAIN=cv. BF15; TISSUE=Tuber;
RX   PubMed=16668624;
RA   Colas des Francs-Small C., Ambard-Bretteville F., Darpas A.,
RA   Sallantin M., Huet J.-C., Pernollet J.-C., Remy R.;
RT   "Variation of the polypeptide composition of mitochondria isolated
RT   from different potato tissues.";
RL   Plant Physiol. 98:273-278(1992).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9490763; DOI=10.1104/pp.116.2.627;
RA   Hourton-Cabassa C., Ambard-Bretteville F., Moreau F.,
RA   Davy de Virville J., 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: Involved in formate-dependent oxygen uptake coupled to
CC       ATP synthesis.
CC   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Found at high levels in developing tubers, at
CC       intermediate level in stems, veins, stolons, and stamens, and at
CC       low level in leaves and roots.
CC   -!- INDUCTION: Induced very rapidly by wounding, and slower by
CC       darkness, chilling, drought, hypoxia, and treatments with formate,
CC       abscisic acid, serine, sarcosine, pyruvate, acetate, ethanol or
CC       methanol.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily.
CC   -!- CAUTION: There are two other putative pseudogenes, FDH2 and FDH3.
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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   HSSP; P33160; 2NAD.
DR   IntAct; Q07511; 1.
DR   BRENDA; 1.2.1.2; 296.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008863; F:formate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-O...; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 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   Transit peptide.
FT   TRANSIT       1     25       Mitochondrion.
FT   CHAIN        26    381       Formate dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007196.
FT   ACT_SITE    287    287       By similarity.
FT   ACT_SITE    335    335       Proton donor (By similarity).
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
//