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Q9S7E4 (FDH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formate dehydrogenase, mitochondrial

EC=1.2.1.2
Alternative name(s):
NAD-dependent formate dehydrogenase
Short name=FDH
Gene names
Name:FDH1
Synonyms:FDH
Ordered Locus Names:At5g14780
ORF Names:T9L3_80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Subcellular location

Mitochondrion Ref.7.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 384357Formate dehydrogenase, mitochondrial
PRO_0000007193

Regions

Nucleotide binding207 – 2082NAD By similarity
Nucleotide binding288 – 2903NAD By similarity
Nucleotide binding338 – 3414NAD By similarity

Sites

Active site2901 By similarity
Active site3381Proton donor By similarity
Binding site3141NAD By similarity

Secondary structure

...................................................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S7E4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A12BA423019D862B

FASTA38442,410
        10         20         30         40         50         60 
MAMRQAAKAT IRACSSSSSS GYFARRQFNA SSGDSKKIVG VFYKANEYAT KNPNFLGCVE 

        70         80         90        100        110        120 
NALGIRDWLE SQGHQYIVTD DKEGPDCELE KHIPDLHVLI STPFHPAYVT AERIKKAKNL 

       130        140        150        160        170        180 
KLLLTAGIGS DHIDLQAAAA AGLTVAEVTG SNVVSVAEDE LMRILILMRN FVPGYNQVVK 

       190        200        210        220        230        240 
GEWNVAGIAY RAYDLEGKTI GTVGAGRIGK LLLQRLKPFG CNLLYHDRLQ MAPELEKETG 

       250        260        270        280        290        300 
AKFVEDLNEM LPKCDVIVIN MPLTEKTRGM FNKELIGKLK KGVLIVNNAR GAIMERQAVV 

       310        320        330        340        350        360 
DAVESGHIGG YSGDVWDPQP APKDHPWRYM PNQAMTPHTS GTTIDAQLRY AAGTKDMLER 

       370        380 
YFKGEDFPTE NYIVKDGELA PQYR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT51423.
RefSeqNP_196982.1. NM_121482.3.
UniGeneAt.23637.
At.6781.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9S7E4.
SMRQ9S7E4. Positions 34-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16607. 1 interaction.
IntActQ9S7E4. 1 interaction.

Proteomic databases

PaxDbQ9S7E4.
PRIDEQ9S7E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G14780.1; AT5G14780.1; AT5G14780.
GeneID831330.
KEGGath:AT5G14780.

Organism-specific databases

TAIRAT5G14780.

Phylogenomic databases

eggNOGCOG1052.
HOGENOMHOG000136703.
InParanoidQ9S7E4.
KOK00122.
OMAKANEYAT.
PhylomeDBQ9S7E4.

Enzyme and pathway databases

BioCycARA:AT5G14780-MONOMER.

Gene expression databases

GenevestigatorQ9S7E4.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ9S7E4.

Entry information

Entry nameFDH_ARATH
AccessionPrimary (citable) accession number: Q9S7E4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names