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Q9ZRI8 (FDH_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processresponse to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

thylakoid

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

formate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion By similarity
Chain22 – 377356Formate dehydrogenase, mitochondrial
PRO_0000007194

Regions

Nucleotide binding200 – 2012NAD By similarity
Nucleotide binding281 – 2833NAD By similarity
Nucleotide binding331 – 3344NAD By similarity

Sites

Active site2831 By similarity
Active site3311Proton donor By similarity
Binding site2541NAD; via carbonyl oxygen By similarity
Binding site3071NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZRI8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E28C1FE24E9225C7

FASTA37741,546
        10         20         30         40         50         60 
MAAMWRAAAR QLVDRAVGSR AAHTSAGSKK IVGVFYQAGE YADKNPNFVG CVEGALGIRD 

        70         80         90        100        110        120 
WLESKGHHYI VTDDKEGFNS ELEKHIEDMH VLITTPFHPA YVTAEKIKKA KTPELLLTAG 

       130        140        150        160        170        180 
IGSDHIDLPA AAAAGLTVAR VTGSNTVSVA EDELMRILIL LRNFLPGYQQ VVKGEWNVAG 

       190        200        210        220        230        240 
IAHRAYDLEG KTVGTVGAGR YGRLLLQRLK PFNCNLLYHD RLQINPELEK EIGAKFEEDL 

       250        260        270        280        290        300 
DAMLPKCDVV VINTPLTEKT RGMFNKEKIA KMKKGVIIVN NARGAIMDTQ AVADACSSGH 

       310        320        330        340        350        360 
IAGYGGDVWF PQPAPKDHPW RYMPNHAMTP HISGTTIDAQ LRYAAGVKDM LDRYFKGEEF 

       370 
PVENYIVKEG ELASQYK 

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References

[1]"Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by iron deficiency in barley roots."
Suzuki K., Itai R., Suzuki K., Nakanishi H., Nishizawa N.K., Yoshimura E., Mori S.
Plant Physiol. 116:725-732(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Ehimehadaka No.1.
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88272 mRNA. Translation: BAA36181.1.

3D structure databases

ProteinModelPortalQ9ZRI8.
SMRQ9ZRI8. Positions 43-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9ZRI8. 1 interaction.

Proteomic databases

PRIDEQ9ZRI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ9ZRI8.

Gene expression databases

GenevestigatorQ9ZRI8.

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]
PROSITEPS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFDH_HORVU
AccessionPrimary (citable) accession number: Q9ZRI8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 1999
Last modified: March 19, 2014
This is version 71 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