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Database: UniProt
Entry: Q67U69
LinkDB: Q67U69
Original site: Q67U69 
ID   FDH2_ORYSJ              Reviewed;         378 AA.
AC   Q67U69; Q0DC42;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   13-FEB-2019, entry version 96.
DE   RecName: Full=Formate dehydrogenase 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03210};
DE            Short=FDH 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03210};
DE   Flags: Precursor;
GN   OrderedLocusNames=Os06g0486900, LOC_Os06g29220;
GN   ORFNames=OsJ_21395 {ECO:0000312|EMBL:EAZ37052.1}, P0404G03.13;
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 [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   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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; AP005656; BAD38302.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19581.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS97837.1; -; Genomic_DNA.
DR   EMBL; CM000143; EAZ37052.1; -; Genomic_DNA.
DR   EMBL; AK064610; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015642621.1; XM_015787135.1.
DR   UniGene; Os.14187; -.
DR   ProteinModelPortal; Q67U69; -.
DR   SMR; Q67U69; -.
DR   STRING; 39947.LOC_Os06g29220.1; -.
DR   PaxDb; Q67U69; -.
DR   PRIDE; Q67U69; -.
DR   EnsemblPlants; Os06t0486900-01; Os06t0486900-01; Os06g0486900.
DR   GeneID; 4341070; -.
DR   Gramene; Os06t0486900-01; Os06t0486900-01; Os06g0486900.
DR   KEGG; osa:4341070; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136703; -.
DR   InParanoid; Q67U69; -.
DR   KO; K00122; -.
DR   OMA; SPHVGGY; -.
DR   OrthoDB; 1378766at2759; -.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q67U69; 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.
PE   2: Evidence at transcript level;
KW   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     18       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   CHAIN        19    378       Formate dehydrogenase 2, mitochondrial.
FT                                /FTId=PRO_0000225339.
FT   NP_BIND     201    202       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     256    260       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     332    335       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   REGION       31    146       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      147    333       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      334    377       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     122    122       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     146    146       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     147    147       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     221    221       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     282    282       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     308    308       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        284    284       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        332    332       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   CONFLICT     41     41       E -> K (in Ref. 5; AK064610).
FT                                {ECO:0000305}.
SQ   SEQUENCE   378 AA;  41267 MW;  7DFE10FAABC0E2EF CRC64;
     MAMWRAPSAA GQLLGRALAS TAAQTSAGSK KVVGVFYKGG EYADKNPNFV GCVDSALGIR
     GWLESKGHRY IVTDDKEGIN CELEKHIEDA HVLITTPFHP AYITAERIKK AKNLELLLTA
     GVGSDHIDLP AAAAAGLTVA EITGSNTVSV AEDQLMRILL LLRNFLPGHH QIVNGEWNVA
     GIAHRTYDLE GKTVGTVGAG RIGRLLLQRL KPFNCNLMYH DRVKIDPELE KEIGAKYEED
     LDAMLPKCDV VVINMPLTEK TRGMFNKERI AKMKKGVTIV NNARGAIMDT QAVADACASG
     HVAGYGGDVW FPQPAPKDHP WRYMPNHAMT PHCSGTTIDG QLRYAAGVKD MLDRYFKGED
     FPAQNYIVKA GQLASQYQ
//
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