FDH1_ORYSJ
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 03-AUG-2022, entry version 120.
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}.
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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 RefSeq; XP_015643973.1; XM_015788487.1.
DR AlphaFoldDB; Q9SXP2; -.
DR SMR; Q9SXP2; -.
DR STRING; 4530.OS06T0486800-01; -.
DR CarbonylDB; Q9SXP2; -.
DR PaxDb; Q9SXP2; -.
DR PRIDE; Q9SXP2; -.
DR EnsemblPlants; Os06t0486800-01; Os06t0486800-01; Os06g0486800.
DR GeneID; 4341069; -.
DR Gramene; Os06t0486800-01; Os06t0486800-01; Os06g0486800.
DR KEGG; osa:4341069; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_0_0_1; -.
DR InParanoid; Q9SXP2; -.
DR OMA; HYTDRHR; -.
DR OrthoDB; 700058at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q9SXP2; baseline and differential.
DR Genevisible; Q9SXP2; OS.
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..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
