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Database: UniProt
Entry: Q9S7E4
LinkDB: Q9S7E4
Original site: Q9S7E4 
ID   FDH_ARATH               Reviewed;         384 AA.
AC   Q9S7E4;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 137.
DE   RecName: Full=Formate dehydrogenase, chloroplastic/mitochondrial {ECO:0000305};
DE            Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE            EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:11074273, ECO:0000269|Ref.7};
DE   AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210};
DE   Flags: Precursor;
GN   Name=FDH1; Synonyms=FDH {ECO:0000303|Ref.7};
GN   OrderedLocusNames=At5g14780; ORFNames=T9L3_80;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=16232936; DOI=10.1263/jbb.90.691;
RA   Fukusaki E., Ikeda T., Shiraishi T., Nishikawa T., Kobayashi A.;
RT   "Formate dehydrogenase gene of Arabidopsis thaliana is induced by
RT   formaldehyde and not by formic acid.";
RL   J. Biosci. Bioeng. 90:691-693(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=11074273; DOI=10.1016/S0168-9452(00)00337-X;
RA   Olson B.J., Skavdahl M., Ramberg H., Osterman J.C., Markwell J.;
RT   "Formate dehydrogenase in Arabidopsis thaliana: characterization and
RT   possible targeting to the chloroplast.";
RL   Plant Sci. 159:205-212(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   DOI=10.1139/b01-056;
RA   Li R., Bonham-Smith P.C., King J.;
RT   "Molecular characterization and regulation of formate dehydrogenase in
RT   Arabidopsis thaliana.";
RL   Can. J. Bot. 79:796-804(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   PROTEIN SEQUENCE OF 30-54, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   DOI=10.1016/S0176-1617(00)80186-8;
RA   Li R., Ziola B., King J.;
RT   "Purification and characterization of formate dehydrogenase from
RT   Arabidopsis thaliana.";
RL   J. Plant Physiol. 157:161-167(2000).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 34-384.
RA   Timofeev V.I., Shabalin I.G., Serov A.E., Polyakov K.M., Popov V.O.,
RA   Tishkov V.I., Kuranova I.P., Samigina V.R.;
RT   "Structure of recombinant formate dehydrogenase from Arabidopsis
RT   thaliana.";
RL   Submitted (SEP-2009) to the PDB data bank.
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-384 IN COMPLEX WITH NAD.
RA   Shabalin I.G., Polyakov K.M., Skirgello O.E., Tishkov V.I.,
RA   Popov V.O.;
RT   "Structures of the apo and holo forms of NAD-dependent formate
RT   dehydrogenase from the higher-plant Arabidopsis thaliana.";
RL   Submitted (MAY-2010) to the PDB data bank.
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, ECO:0000269|Ref.3}.
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, ECO:0000269|PubMed:11074273, ECO:0000269|Ref.7};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=104 mM for formate(at pH 7 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:11074273};
CC         KM=1.4 mM for formate (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|Ref.7};
CC         KM=65 uM for NAD (at pH 7. and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:11074273};
CC         KM=34 uM for NAD (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|Ref.7};
CC       pH dependence:
CC         Optimum pH is 6-8. {ECO:0000269|Ref.7};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210,
CC       ECO:0000269|Ref.7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03210, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.7}.
CC       Plastid, chloroplast {ECO:0000269|PubMed:11074273}.
CC   -!- INDUCTION: By one-carbon metabolites, such as methanol,
CC       formaldehyde, and formate (at protein level) (Ref.3). Strongest
CC       induced by formaldehyde (PubMed:16232936).
CC       {ECO:0000269|PubMed:16232936, ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
DR   EMBL; AB023897; BAA88683.1; -; mRNA.
DR   EMBL; AF217195; AAF67100.1; -; mRNA.
DR   EMBL; AF208028; AAF19435.1; -; mRNA.
DR   EMBL; AF208029; AAF19436.1; -; mRNA.
DR   EMBL; AL391149; CAC01877.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92076.1; -; Genomic_DNA.
DR   EMBL; AY054285; AAL06944.1; -; mRNA.
DR   EMBL; AY039609; AAK62664.1; -; mRNA.
DR   EMBL; AY081734; AAL87387.1; -; mRNA.
DR   PIR; T51423; T51423.
DR   RefSeq; NP_196982.1; NM_121482.4.
DR   UniGene; At.23637; -.
DR   UniGene; At.6781; -.
DR   PDB; 3JTM; X-ray; 1.30 A; A=34-384.
DR   PDB; 3N7U; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=34-384.
DR   PDB; 3NAQ; X-ray; 1.70 A; A/B=28-384.
DR   PDBsum; 3JTM; -.
DR   PDBsum; 3N7U; -.
DR   PDBsum; 3NAQ; -.
DR   ProteinModelPortal; Q9S7E4; -.
DR   SMR; Q9S7E4; -.
DR   BioGrid; 16607; 2.
DR   IntAct; Q9S7E4; 1.
DR   STRING; 3702.AT5G14780.1; -.
DR   iPTMnet; Q9S7E4; -.
DR   PaxDb; Q9S7E4; -.
DR   PRIDE; Q9S7E4; -.
DR   EnsemblPlants; AT5G14780.1; AT5G14780.1; AT5G14780.
DR   GeneID; 831330; -.
DR   Gramene; AT5G14780.1; AT5G14780.1; AT5G14780.
DR   KEGG; ath:AT5G14780; -.
DR   Araport; AT5G14780; -.
DR   TAIR; locus:2185500; AT5G14780.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136703; -.
DR   InParanoid; Q9S7E4; -.
DR   KO; K00122; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; Q9S7E4; -.
DR   BioCyc; ARA:AT5G14780-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G14780-MONOMER; -.
DR   EvolutionaryTrace; Q9S7E4; -.
DR   PRO; PR:Q9S7E4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9S7E4; baseline and differential.
DR   Genevisible; Q9S7E4; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
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   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
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   3D-structure; Chloroplast; Complete proteome;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT       1     29       Chloroplast and mitochondrion.
FT                                {ECO:0000269|Ref.7}.
FT   CHAIN        30    384       Formate dehydrogenase,
FT                                chloroplastic/mitochondrial.
FT                                /FTId=PRO_0000007193.
FT   NP_BIND     207    208       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   NP_BIND     262    266       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   NP_BIND     338    341       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   REGION       37    152       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      153    339       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      340    383       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     152    152       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     227    227       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   BINDING     288    288       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   BINDING     314    314       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.10}.
FT   SITE        290    290       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        338    338       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   STRAND       37     41       {ECO:0000244|PDB:3JTM}.
FT   HELIX        47     51       {ECO:0000244|PDB:3JTM}.
FT   TURN         59     61       {ECO:0000244|PDB:3JTM}.
FT   HELIX        62     64       {ECO:0000244|PDB:3JTM}.
FT   HELIX        66     71       {ECO:0000244|PDB:3JTM}.
FT   STRAND       75     80       {ECO:0000244|PDB:3JTM}.
FT   HELIX        88     92       {ECO:0000244|PDB:3JTM}.
FT   TURN         93     95       {ECO:0000244|PDB:3JTM}.
FT   STRAND       97    101       {ECO:0000244|PDB:3JTM}.
FT   HELIX       111    116       {ECO:0000244|PDB:3JTM}.
FT   STRAND      122    128       {ECO:0000244|PDB:3JTM}.
FT   HELIX       135    140       {ECO:0000244|PDB:3JTM}.
FT   STRAND      144    147       {ECO:0000244|PDB:3JTM}.
FT   TURN        149    152       {ECO:0000244|PDB:3JTM}.
FT   HELIX       153    169       {ECO:0000244|PDB:3JTM}.
FT   HELIX       171    179       {ECO:0000244|PDB:3JTM}.
FT   HELIX       185    189       {ECO:0000244|PDB:3JTM}.
FT   STRAND      199    203       {ECO:0000244|PDB:3JTM}.
FT   HELIX       207    216       {ECO:0000244|PDB:3JTM}.
FT   HELIX       217    219       {ECO:0000244|PDB:3JTM}.
FT   STRAND      222    226       {ECO:0000244|PDB:3JTM}.
FT   HELIX       233    239       {ECO:0000244|PDB:3JTM}.
FT   HELIX       247    250       {ECO:0000244|PDB:3JTM}.
FT   HELIX       251    253       {ECO:0000244|PDB:3JTM}.
FT   STRAND      255    259       {ECO:0000244|PDB:3JTM}.
FT   TURN        265    269       {ECO:0000244|PDB:3JTM}.
FT   HELIX       273    278       {ECO:0000244|PDB:3JTM}.
FT   STRAND      283    287       {ECO:0000244|PDB:3JTM}.
FT   HELIX       291    293       {ECO:0000244|PDB:3JTM}.
FT   HELIX       296    305       {ECO:0000244|PDB:3JTM}.
FT   STRAND      306    314       {ECO:0000244|PDB:3JTM}.
FT   STRAND      317    320       {ECO:0000244|PDB:3JTM}.
FT   HELIX       326    328       {ECO:0000244|PDB:3JTM}.
FT   HELIX       340    342       {ECO:0000244|PDB:3JTM}.
FT   HELIX       344    363       {ECO:0000244|PDB:3JTM}.
FT   HELIX       369    371       {ECO:0000244|PDB:3JTM}.
FT   STRAND      372    375       {ECO:0000244|PDB:3JTM}.
FT   HELIX       381    383       {ECO:0000244|PDB:3JTM}.
SQ   SEQUENCE   384 AA;  42410 MW;  A12BA423019D862B CRC64;
     MAMRQAAKAT IRACSSSSSS GYFARRQFNA SSGDSKKIVG VFYKANEYAT KNPNFLGCVE
     NALGIRDWLE SQGHQYIVTD DKEGPDCELE KHIPDLHVLI STPFHPAYVT AERIKKAKNL
     KLLLTAGIGS DHIDLQAAAA AGLTVAEVTG SNVVSVAEDE LMRILILMRN FVPGYNQVVK
     GEWNVAGIAY RAYDLEGKTI GTVGAGRIGK LLLQRLKPFG CNLLYHDRLQ MAPELEKETG
     AKFVEDLNEM LPKCDVIVIN MPLTEKTRGM FNKELIGKLK KGVLIVNNAR GAIMERQAVV
     DAVESGHIGG YSGDVWDPQP APKDHPWRYM PNQAMTPHTS GTTIDAQLRY AAGTKDMLER
     YFKGEDFPTE NYIVKDGELA PQYR
//
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