Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9S7E4

- FDH_ARATH

UniProt

Q9S7E4 - FDH_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 415Combined sources
Helixi47 – 515Combined sources
Turni59 – 613Combined sources
Helixi62 – 643Combined sources
Helixi66 – 716Combined sources
Beta strandi75 – 806Combined sources
Helixi88 – 925Combined sources
Turni93 – 953Combined sources
Beta strandi97 – 1015Combined sources
Helixi111 – 1166Combined sources
Beta strandi122 – 1287Combined sources
Helixi135 – 1406Combined sources
Beta strandi144 – 1474Combined sources
Turni149 – 1524Combined sources
Helixi153 – 16917Combined sources
Helixi171 – 1799Combined sources
Helixi185 – 1895Combined sources
Beta strandi199 – 2035Combined sources
Helixi207 – 21610Combined sources
Helixi217 – 2193Combined sources
Beta strandi222 – 2265Combined sources
Helixi233 – 2397Combined sources
Helixi247 – 2504Combined sources
Helixi251 – 2533Combined sources
Beta strandi255 – 2595Combined sources
Turni265 – 2695Combined sources
Helixi273 – 2786Combined sources
Beta strandi283 – 2875Combined sources
Helixi291 – 2933Combined sources
Helixi296 – 30510Combined sources
Beta strandi306 – 3149Combined sources
Beta strandi317 – 3204Combined sources
Helixi326 – 3283Combined sources
Helixi340 – 3423Combined sources
Helixi344 – 36320Combined sources
Helixi369 – 3713Combined sources
Beta strandi372 – 3754Combined sources
Helixi381 – 3833Combined sources

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.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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

        10         20         30         40         50
MAMRQAAKAT IRACSSSSSS GYFARRQFNA SSGDSKKIVG VFYKANEYAT
60 70 80 90 100
KNPNFLGCVE NALGIRDWLE SQGHQYIVTD DKEGPDCELE KHIPDLHVLI
110 120 130 140 150
STPFHPAYVT AERIKKAKNL KLLLTAGIGS DHIDLQAAAA AGLTVAEVTG
160 170 180 190 200
SNVVSVAEDE LMRILILMRN FVPGYNQVVK GEWNVAGIAY RAYDLEGKTI
210 220 230 240 250
GTVGAGRIGK LLLQRLKPFG CNLLYHDRLQ MAPELEKETG AKFVEDLNEM
260 270 280 290 300
LPKCDVIVIN MPLTEKTRGM FNKELIGKLK KGVLIVNNAR GAIMERQAVV
310 320 330 340 350
DAVESGHIGG YSGDVWDPQP APKDHPWRYM PNQAMTPHTS GTTIDAQLRY
360 370 380
AAGTKDMLER YFKGEDFPTE NYIVKDGELA PQYR
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.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 110 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