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Database: UniProt
Entry: Q9SXP2
LinkDB: Q9SXP2
Original site: Q9SXP2 
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   16-JAN-2019, entry version 108.
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; Magnoliophyta; 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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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
CC       carbon dioxide. Involved in the cell stress response.
CC       {ECO:0000255|HAMAP-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-
CC       Rule:MF_03210}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
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   UniGene; Os.4156; -.
DR   ProteinModelPortal; Q9SXP2; -.
DR   SMR; Q9SXP2; -.
DR   STRING; 39947.LOC_Os06g29180.1; -.
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   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136703; -.
DR   InParanoid; Q9SXP2; -.
DR   KO; K00122; -.
DR   OMA; EVTYCNS; -.
DR   OrthoDB; 700058at2759; -.
DR   Proteomes; UP000059680; Chromosome 6.
DR   ExpressionAtlas; Q9SXP2; differential.
DR   Genevisible; Q9SXP2; OS.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
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   Complete proteome; Direct protein sequencing; Mitochondrion; NAD;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     20       Mitochondrion.
FT                                {ECO:0000269|PubMed:14681440}.
FT   CHAIN        21    376       Formate dehydrogenase 1, mitochondrial.
FT                                /FTId=PRO_0000007195.
FT   NP_BIND     199    200       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     254    258       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     330    333       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   REGION       29    144       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      145    331       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      332    375       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     120    120       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     144    144       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     145    145       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     219    219       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     280    280       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     306    306       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        282    282       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        330    330       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   CONFLICT    316    317       DH -> GP (in Ref. 1; BAA77337).
FT                                {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
//
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