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Q9S7E4

- FDH_ARATH

UniProt

Q9S7E4 - FDH_ARATH

Protein

Formate dehydrogenase, mitochondrial

Gene

FDH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Formate + NAD+ = CO2 + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei290 – 2901By similarity
    Binding sitei314 – 3141NADBy similarity
    Active sitei338 – 3381Proton donorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi207 – 2082NADBy similarity
    Nucleotide bindingi288 – 2903NADBy similarity
    Nucleotide bindingi338 – 3414NADBy similarity

    GO - Molecular functioni

    1. formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. response to cadmium ion Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciARA:AT5G14780-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenase, mitochondrial (EC:1.2.1.2)
    Alternative name(s):
    NAD-dependent formate dehydrogenase
    Short name:
    FDH
    Gene namesi
    Name:FDH1
    Synonyms:FDH
    Ordered Locus Names:At5g14780
    ORF Names:T9L3_80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G14780.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. mitochondrion Source: TAIR
    3. thylakoid Source: TAIR

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionBy similarityAdd
    BLAST
    Chaini28 – 384357Formate dehydrogenase, mitochondrialPRO_0000007193Add
    BLAST

    Proteomic databases

    PaxDbiQ9S7E4.
    PRIDEiQ9S7E4.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9S7E4.

    Interactioni

    Protein-protein interaction databases

    BioGridi16607. 1 interaction.
    IntActiQ9S7E4. 1 interaction.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 415
    Helixi47 – 515
    Turni59 – 613
    Helixi62 – 643
    Helixi66 – 716
    Beta strandi75 – 806
    Helixi88 – 925
    Turni93 – 953
    Beta strandi97 – 1015
    Helixi111 – 1166
    Beta strandi122 – 1287
    Helixi135 – 1406
    Beta strandi144 – 1474
    Turni149 – 1524
    Helixi153 – 16917
    Helixi171 – 1799
    Helixi185 – 1895
    Beta strandi199 – 2035
    Helixi207 – 21610
    Helixi217 – 2193
    Beta strandi222 – 2265
    Helixi233 – 2397
    Helixi247 – 2504
    Helixi251 – 2533
    Beta strandi255 – 2595
    Turni265 – 2695
    Helixi273 – 2786
    Beta strandi283 – 2875
    Helixi291 – 2933
    Helixi296 – 30510
    Beta strandi306 – 3149
    Beta strandi317 – 3204
    Helixi326 – 3283
    Helixi340 – 3423
    Helixi344 – 36320
    Helixi369 – 3713
    Beta strandi372 – 3754
    Helixi381 – 3833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JTMX-ray1.30A34-384[»]
    3N7UX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L34-384[»]
    3NAQX-ray1.70A/B28-384[»]
    ProteinModelPortaliQ9S7E4.
    SMRiQ9S7E4. Positions 34-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S7E4.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1052.
    HOGENOMiHOG000136703.
    InParanoidiQ9S7E4.
    KOiK00122.
    OMAiKANEYAT.
    PhylomeDBiQ9S7E4.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9S7E4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMRQAAKAT IRACSSSSSS GYFARRQFNA SSGDSKKIVG VFYKANEYAT    50
    KNPNFLGCVE NALGIRDWLE SQGHQYIVTD DKEGPDCELE KHIPDLHVLI 100
    STPFHPAYVT AERIKKAKNL KLLLTAGIGS DHIDLQAAAA AGLTVAEVTG 150
    SNVVSVAEDE LMRILILMRN FVPGYNQVVK GEWNVAGIAY RAYDLEGKTI 200
    GTVGAGRIGK LLLQRLKPFG CNLLYHDRLQ MAPELEKETG AKFVEDLNEM 250
    LPKCDVIVIN MPLTEKTRGM FNKELIGKLK KGVLIVNNAR GAIMERQAVV 300
    DAVESGHIGG YSGDVWDPQP APKDHPWRYM PNQAMTPHTS GTTIDAQLRY 350
    AAGTKDMLER YFKGEDFPTE NYIVKDGELA PQYR 384
    Length:384
    Mass (Da):42,410
    Last modified:May 1, 2000 - v1
    Checksum:iA12BA423019D862B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023897 mRNA. Translation: BAA88683.1.
    AF208028 mRNA. Translation: AAF19435.1.
    AF208029 mRNA. Translation: AAF19436.1.
    AF217195 mRNA. Translation: AAF67100.1.
    AL391149 Genomic DNA. Translation: CAC01877.1.
    CP002688 Genomic DNA. Translation: AED92076.1.
    AY054285 mRNA. Translation: AAL06944.1.
    AY039609 mRNA. Translation: AAK62664.1.
    AY081734 mRNA. Translation: AAL87387.1.
    PIRiT51423.
    RefSeqiNP_196982.1. NM_121482.3.
    UniGeneiAt.23637.
    At.6781.

    Genome annotation databases

    EnsemblPlantsiAT5G14780.1; AT5G14780.1; AT5G14780.
    GeneIDi831330.
    KEGGiath:AT5G14780.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023897 mRNA. Translation: BAA88683.1 .
    AF208028 mRNA. Translation: AAF19435.1 .
    AF208029 mRNA. Translation: AAF19436.1 .
    AF217195 mRNA. Translation: AAF67100.1 .
    AL391149 Genomic DNA. Translation: CAC01877.1 .
    CP002688 Genomic DNA. Translation: AED92076.1 .
    AY054285 mRNA. Translation: AAL06944.1 .
    AY039609 mRNA. Translation: AAK62664.1 .
    AY081734 mRNA. Translation: AAL87387.1 .
    PIRi T51423.
    RefSeqi NP_196982.1. NM_121482.3.
    UniGenei At.23637.
    At.6781.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JTM X-ray 1.30 A 34-384 [» ]
    3N7U X-ray 2.00 A/B/C/D/E/F/G/H/I/J/K/L 34-384 [» ]
    3NAQ X-ray 1.70 A/B 28-384 [» ]
    ProteinModelPortali Q9S7E4.
    SMRi Q9S7E4. Positions 34-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16607. 1 interaction.
    IntActi Q9S7E4. 1 interaction.

    Proteomic databases

    PaxDbi Q9S7E4.
    PRIDEi Q9S7E4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G14780.1 ; AT5G14780.1 ; AT5G14780 .
    GeneIDi 831330.
    KEGGi ath:AT5G14780.

    Organism-specific databases

    TAIRi AT5G14780.

    Phylogenomic databases

    eggNOGi COG1052.
    HOGENOMi HOG000136703.
    InParanoidi Q9S7E4.
    KOi K00122.
    OMAi KANEYAT.
    PhylomeDBi Q9S7E4.

    Enzyme and pathway databases

    BioCyci ARA:AT5G14780-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9S7E4.

    Gene expression databases

    Genevestigatori Q9S7E4.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Formate dehydrogenase cDNA from Arabidopsis thaliana."
      Nishikawa T., Fukusaki E., Kobayashi A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Arabidopsis thaliana mRNA for NAD-dependent formate dehydrogenas 1."
      Li R., Bonham-Smith P.C., King J.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Induction of leaf formate dehydrogenase by one-carbon metabolites."
      Markwell J., Osterman J.C., Olson B.J., Skavdahl M., Ramberg H., Germann M.C.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
      Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
      Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: cv. Landsberg erecta.

    Entry informationi

    Entry nameiFDH_ARATH
    AccessioniPrimary (citable) accession number: Q9S7E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3