Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C8ZHD6 (FDH1_YEAS8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 24. 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 1

EC=1.2.1.2
Alternative name(s):
NAD-dependent formate dehydrogenase 1
Gene names
Name:FDH1
ORF Names:EC1118_1O4_6403g
OrganismSaccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) [Complete proteome]
Taxonomic identifier643680 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Subcellular location

Cytoplasm By similarity.

Induction

Induced by formate.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain1 – 376376Formate dehydrogenase 1
PRO_0000393442

Regions

Nucleotide binding176 – 1772NAD By similarity
Nucleotide binding270 – 2723NAD By similarity
Nucleotide binding325 – 3284NAD By similarity

Sites

Active site2721 By similarity
Active site3251Proton donor By similarity
Binding site2961NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C8ZHD6 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 67ECDA6F9DDC2A02

FASTA37641,714
        10         20         30         40         50         60 
MSKGKVLLVL YEGGKHAEEQ EKLLGCIENE LGIRNFIEEQ GYELVTTIDK DPEPTSTVDR 

        70         80         90        100        110        120 
ELKDAEIVIT TPFFPAYISR NRIAEAPNLK LCVTAGVGSD HVDLEAANER KITVTEVTGS 

       130        140        150        160        170        180 
NVVSVAEHVM ATILVLIRNY NGGHQQAING EWDIAGVAKN EYDLEDKIIS TVGAGRIGYR 

       190        200        210        220        230        240 
VLERLVAFNP KKLLYYDYQE LPAEAINRLN EASKLFNGRG DIVQRVEKLE DMVAQSDVVT 

       250        260        270        280        290        300 
INCPLHKDSR GLFNKKLISH MKDGAYLVNT ARGAICVAED VAEAVKSGKL AGYGGDVWDK 

       310        320        330        340        350        360 
QPAPKDHPWR TMDNKDHVGN AMTVHISGTS LDAQKRYAQG VKNILNSYFS KKFDYRPQDI 

       370 
IVQNGSYATR AYGQKK 

« Hide

References

[1]"Eukaryote-to-eukaryote gene transfer events revealed by the genome sequence of the wine yeast Saccharomyces cerevisiae EC1118."
Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B., Legras J.-L., Wincker P., Casaregola S., Dequin S.
Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lalvin EC1118 / Prise de mousse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN394216 Genomic DNA. Translation: CAY86665.1.

3D structure databases

ProteinModelPortalC8ZHD6.
SMRC8ZHD6. Positions 4-367.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG769ZV3.

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 nameFDH1_YEAS8
AccessionPrimary (citable) accession number: C8ZHD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: November 3, 2009
Last modified: February 19, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families