ID FDH1_ORYSJ Reviewed; 376 AA. AC Q9SXP2; Q67U72; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 02-SEP-2026, entry version 134. DE RecName: Full=Formate dehydrogenase 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03210}; DE Short=FDH 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|Ref.1}; DE Flags: Precursor; GN OrderedLocusNames=Os06g0486800, LOC_Os06g29180; GN ORFNames=P0008F02.23, P0404G03.8; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Shiraishi T., Fukusaki E., Kobayashi A.; RT "NAD-dependent formate dehydrogenase."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [4] RP PROTEIN SEQUENCE OF 21-30. RC STRAIN=cv. Nipponbare; TISSUE=Callus; RX PubMed=14681440; DOI=10.1093/nar/gkh020; RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.; RT "Rice proteome database based on two-dimensional polyacrylamide gel RT electrophoresis: its status in 2003."; RL Nucleic Acids Res. 32:D388-D392(2004). 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}. 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; AB019533; BAA77337.1; -; mRNA. DR EMBL; AP003518; BAD37348.1; -; Genomic_DNA. DR EMBL; AP005656; BAD38299.1; -; Genomic_DNA. DR EMBL; AP014962; BAS97836.1; -; Genomic_DNA. DR AlphaFoldDB; Q9SXP2; -. DR SMR; Q9SXP2; -. DR FunCoup; Q9SXP2; 458. DR STRING; 39947.Q9SXP2; -. DR CarbonylDB; Q9SXP2; -. DR PaxDb; 39947-Q9SXP2; -. DR EnsemblPlants; Os06t0486800-01; Os06t0486800-01; Os06g0486800. DR Gramene; Os06t0486800-01; Os06t0486800-01; Os06g0486800. DR eggNOG; KOG0069; Eukaryota. DR HOGENOM; CLU_019796_0_0_1; -. DR InParanoid; Q9SXP2; -. DR OMA; HYTDRHR; -. DR OrthoDB; 1621027at2759; -. DR Proteomes; UP000059680; Chromosome 6. DR ExpressionAtlas; Q9SXP2; baseline and differential. 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 FunFam; 3.40.50.720:FF:000057; Formate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000862; Formate dehydrogenase chloroplastic/mitochondrial; 1. DR FunFam; 3.40.50.720:FF:001366; Formate dehydrogenase chloroplastic/mitochondrial; 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 NCBIfam; NF005750; PRK07574.1; 1. 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..20 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:14681440" FT CHAIN 21..376 FT /note="Formate dehydrogenase 1, mitochondrial" FT /id="PRO_0000007195" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 145 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 199..200 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 219 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 254..258 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 280 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 306 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT BINDING 330..333 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT SITE 282 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT SITE 330 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210" FT CONFLICT 316..317 FT /note="DH -> GP (in Ref. 1; BAA77337)" FT /evidence="ECO:0000305" SQ SEQUENCE 376 AA; 41341 MW; 9FE964AE572C585B CRC64; MAMWRAAAGH LLGRALGSRA AHTSAGSKKI VGVFYKGGEY ADKNPNFVGC VEGALGIREW LESKGHHYIV TDDKEGLNSE LEKHIEDMHV LITTPFHPAY VSAERIKKAK NLELLLTAGI GSDHIDLPAA AAAGLTVAEV TGSNTVSVAE DELMRILILL RNFLPGYQQV VHGEWNVAGI AYRAYDLEGK TVGTVGAGRI GRLLLQRLKP FNCNLLYHDR LKIDPELEKE IGAKYEEDLD AMLPKCDVIV INTPLTEKTR GMFNKERIAK MKKGVIIVNN ARGAIMDTQA VADACSSGQV AGYGGDVWFP QPAPKDHPWR YMPNHAMTPH ISGTTIDAQL RYAAGVKDML DRYFKGEDFP VQNYIVKEGQ LASQYQ //