ID   FDH_HORVU               Reviewed;         377 AA.
AC   Q9ZRI8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Formate dehydrogenase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:9489019};
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};
DE   Flags: Precursor;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ehimehadaka No.1; TISSUE=Root;
RX   PubMed=9489019; DOI=10.1104/pp.116.2.725;
RA   Suzuki K., Itai R., Suzuki K., Nakanishi H., Nishizawa N.K., Yoshimura E.,
RA   Mori S.;
RT   "Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by
RT   iron deficiency in barley roots.";
RL   Plant Physiol. 116:725-732(1998).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC       dioxide. Involved in the cell stress response. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-Rule:MF_03210}.
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DR   EMBL; D88272; BAA36181.1; -; mRNA.
DR   AlphaFoldDB; Q9ZRI8; -.
DR   SMR; Q9ZRI8; -.
DR   IntAct; Q9ZRI8; 1.
DR   PRIDE; Q9ZRI8; -.
DR   ExpressionAtlas; Q9ZRI8; baseline and differential.
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; IEA:UniProtKB-UniRule.
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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   CHAIN           30..377
FT                   /note="Formate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000007194"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         255..259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         307
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         331..334
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   SITE            283
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
SQ   SEQUENCE   377 AA;  41546 MW;  E28C1FE24E9225C7 CRC64;
     MAAMWRAAAR QLVDRAVGSR AAHTSAGSKK IVGVFYQAGE YADKNPNFVG CVEGALGIRD
     WLESKGHHYI VTDDKEGFNS ELEKHIEDMH VLITTPFHPA YVTAEKIKKA KTPELLLTAG
     IGSDHIDLPA AAAAGLTVAR VTGSNTVSVA EDELMRILIL LRNFLPGYQQ VVKGEWNVAG
     IAHRAYDLEG KTVGTVGAGR YGRLLLQRLK PFNCNLLYHD RLQINPELEK EIGAKFEEDL
     DAMLPKCDVV VINTPLTEKT RGMFNKEKIA KMKKGVIIVN NARGAIMDTQ AVADACSSGH
     IAGYGGDVWF PQPAPKDHPW RYMPNHAMTP HISGTTIDAQ LRYAAGVKDM LDRYFKGEEF
     PVENYIVKEG ELASQYK