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Q934F5 (FDHA_DESGI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 subunit alpha

Short name=FDH subunit alpha
EC=1.2.1.2
Alternative name(s):
Formate dehydrogenase large subunit
Gene names
Name:fdhA
OrganismDesulfovibrio gigas
Taxonomic identifier879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha chain of the formate dehydrogenase (FDH) catalyze the reversible two-electron oxidation of formate to carbon dioxide. FDH loses activity in the presence of air, but this activity can be restored. The alpha subunit of formate dehydrogenase forms the active site.

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Cofactor

Binds 1 4Fe-4S cluster per subunit. Ref.1 Ref.4

Binds 1 tungsten-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit. Ref.1 Ref.4

Subunit structure

Heterodimer of alpha (FdhA) and beta (FdhB) subunits. Ref.1 Ref.3 Ref.4

Subcellular location

Periplasm.

Post-translational modification

The disulfide bond is likely to be broken in the active form of this enzyme. Ref.1

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5-8.0.

Temperature dependence:

Optimum temperature is 56 degrees Celsius.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   Coding sequence diversitySelenocysteine
   DomainSignal
   Ligand4Fe-4S
Calcium
Iron
Iron-sulfur
Metal-binding
NAD
Tungsten
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellular respiration

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

periplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

formate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

molybdenum ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535Tat-type signal Ref.1
Chain36 – 1012977Formate dehydrogenase subunit alpha Ref.1
PRO_0000019149

Regions

Domain45 – 103594Fe-4S Mo/W bis-MGD-type
Calcium binding394 – 3985 Ref.1

Sites

Metal binding521Iron-sulfur (4Fe-4S) Ref.1
Metal binding551Iron-sulfur (4Fe-4S) Ref.1
Metal binding591Iron-sulfur (4Fe-4S) Ref.1
Metal binding891Iron-sulfur (4Fe-4S) Ref.1
Metal binding1931Tungsten Ref.1

Amino acid modifications

Non-standard residue1931Selenocysteine
Disulfide bond852 ↔ 879 Ref.1

Secondary structure

................................................................................................................................................................................ 1012
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q934F5 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 23CDC4594334D51F

FASTA1,012113,271
        10         20         30         40         50         60 
MLIKRRAFLK LTAAGATLSA FGGLGVDLAP AKAQAATMAL KTVDAKQTTS VCCYCSVGCG 

        70         80         90        100        110        120 
LIVHTDKKTN RAINVEGDPD HPINEGSLCA KGASTWQLAE NERRPANPLY RAPGSDQWEE 

       130        140        150        160        170        180 
KSWDWMLDTI AERVAKTREA TFVTKNAKGQ VVNRCDGIAS VGSAAMDNEE CWIYQAWLRS 

       190        200        210        220        230        240 
LGLFYIEHQA RIUHSATVAA LAESYGRGAM TNHWIDLKNS DVILMMGSNP AENHPISFKW 

       250        260        270        280        290        300 
VMRAKDKGAT LIHVDPRYTR TSTKCDLYAP LRSGSDIAFL NGMTKYILEK ELYFKDYVVN 

       310        320        330        340        350        360 
YTNASFIVGE GFAFEEGLFA GYNKETRKYD KSKWGFERDE NGNPKRDETL KHPRCVFQIM 

       370        380        390        400        410        420 
KKHYERYDLD KISAICGTPK ELILKVYDAY CATGKPDKAG TIMYAMGWTQ HTVGVQNIRA 

       430        440        450        460        470        480 
MSINQLLLGN IGVAGGGVNA LRGEANVQGS TDHGLLMHIY PGYLGTARAS IPTYEEYTKK 

       490        500        510        520        530        540 
FTPVSKDPQS ANWWSNFPKY SASYIKSMWP DADLNEAYGY LPKGEDGKDY SWLTLFDDMF 

       550        560        570        580        590        600 
QGKIKGFFAW GQNPACSGAN SNKTREALTK LDWMVNVNIF DNETGSFWRG PDMDPKKIKT 

       610        620        630        640        650        660 
EVFFLPCAVA IEKEGSISNS GRWMQWRYVG PEPRKNAIPD GDLIVELAKR VQKLLAKTPG 

       670        680        690        700        710        720 
KLAAPVTKLK TDYWVNDHGH FDPHKIAKLI NGFALKDFKV GDVEYKAGQQ IATFGHLQAD 

       730        740        750        760        770        780 
GSTTSGCWIY TGSYTEKGNM AARRDKTQTD MQAKIGLYPG WTWAWPVNRR IIYNRASVDL 

       790        800        810        820        830        840 
NGKPYAPEKA VVEWNAAEKK WVGDVPDGPW PPQADKEKGK RAFIMKPEGY AYLYGPGRED 

       850        860        870        880        890        900 
GPLPEYYEPM ECPVIEHPFS KTLHNPTALH FATEEKAVCD PRYPFICSTY RVTEHWQTGL 

       910        920        930        940        950        960 
MTRNTPWLLE AEPQMFCEMS EELATLRGIK NGDKVILESV RGKLWAKAII TKRIKPFAIQ 

       970        980        990       1000       1010 
GQQVHMVGIP WHYGWSFPKN GGDAANILTP SVGDPNTGIP ETKAFMVNVT KA 

« Hide

References

[1]"Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., Bursakov S., Huber R., Moura J.J.G., Moura I., Romao M.J.
Structure 10:1261-1272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, COFACTOR, DISULFIDE BOND, CALCIUM-BINDING, METAL-BINDING, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FDHB.
Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
[2]"Properties of formate dehydrogenase from Desulfivibrio gigas."
Riederer-Henderson M.A., Peck H.D. Jr.
Can. J. Microbiol. 32:430-435(1986)
Cited for: CHARACTERIZATION.
[3]"Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
Almendra M.J., Brondino C.D., Gavel O., Pereira A.S., Tavares P., Bursakov S., Duarte R., Caldeira J., Moura J.J.G., Moura I.
Biochemistry 38:16366-16372(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBUNIT.
Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
[4]"Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal identification and preliminary structural data by multi-wavelength crystallography."
Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D., Moura I., Moura J.J.G., Romao M.J.
J. Biol. Inorg. Chem. 6:398-404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ318781 Genomic DNA. Translation: CAC86667.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80A/K36-1012[»]
ProteinModelPortalQ934F5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.2.2.1. 1907.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate_DH_asu_anaerob.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR01553. formate-DH-alph. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ934F5.

Entry information

Entry nameFDHA_DESGI
AccessionPrimary (citable) accession number: Q934F5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references