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Reviewed, UniProtKB/Swiss-Prot P06131 (FDHA_METFO)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Formate dehydrogenase subunit alpha
    EC=1.2.1.2
Gene names
Name: fdhA
OrganismMethanobacterium formicicum
Taxonomic identifier2162 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobacterium

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the oxidation of formate.

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Cofactor

Molybdenum (molybdopterin).

Zinc.

FAD.

Binds 1 4Fe-4S cluster Potential.

Subunit structure

Dimer of an alpha and a beta subunit.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684Formate dehydrogenase subunit alpha
PRO_0000063225

Sites

Metal binding101Iron-sulfur (4Fe-4S) By similarity
Metal binding131Iron-sulfur (4Fe-4S) By similarity
Metal binding171Iron-sulfur (4Fe-4S) By similarity
Metal binding451Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P06131-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 38D37CF86BFF06E2

FASTA68475,717
        10         20         30         40         50         60 
MDIKYVPTIC PYCGVGCGMN LVVKDEKVVG VEPWKRHPVN EGKLCPKGNF CYEIIHREDR 

        70         80         90        100        110        120 
LTTPLIKENG EFREATWDEA YDLIASKLGA YDPNEIGFFC CARSPNENIY VNQKFARIVV 

       130        140        150        160        170        180 
GTHNIDHCAR LCHGPTVAGL AASFGSGAMT NSYASFEDAD LIFSIGANSL EAHPLVGRKL 

       190        200        210        220        230        240 
MRAKMNGAYF IVADPRYTPT AKQADQYIPF KTGTDVALMN AMMNVIISEG LEDKEFIEKR 

       250        260        270        280        290        300 
TKNYEELKEV VSKYTPEMAE EITQVPADVI RDIAIKYAKA DKAAIVYSLG ITEHSHGVDN 

       310        320        330        340        350        360 
VMQTANLAML TGNIGRLGTG VNPLRGQNNV QGACDMGALP TDYPGYRKVA DQEVMEDVTC 

       370        380        390        400        410        420 
TWGCSDLGCE PGLKIPEMID AAAKGDLKVL YITGEDPVIS DPDTHHVEEA LNNLDFFVVQ 

       430        440        450        460        470        480 
DIFMTDTAEF ADVVLPAACW AEQEGTFTNG ERRVQLIRKA VDAPGESKYD WEIFCDLAKK 

       490        500        510        520        530        540 
MGADPEMFTY ESAQDIFEEV RTVTPQYAGM NRERLDRPEA LHWPCPSEDH PGTAMMHIEK 

       550        560        570        580        590        600 
FAHPDGLGIF MPLEEQGPME TPDDEYPLIL TTTRLLFHYH AAMTRRAATL DREVPTGYVE 

       610        620        630        640        650        660 
INTEDAAELG IANKEKVKVK SRRGEIEIAA RVTDDIVKGI VNIPMHFREC SANILTNAAA 

       670        680 
IDPKSGMPEY KACAVAISKM EGSK 

« Hide

References

[1]"Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum."
Shuber A.P., Orr E.C., Recny M.A., Schendel P.F., May H.D., Schauer N.L., Ferry J.G.
J. Biol. Chem. 261:12942-12947(1986) [PubMed: 3531194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26.
Strain: JF-1.
[2]"Identification of formate dehydrogenase-specific mRNA species and nucleotide sequence of the fdhC gene of Methanobacterium formicicum."
White W.B., Ferry J.G.
J. Bacteriol. 174:4997-5004(1992) [PubMed: 1378430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
Strain: JF-1.

Cross-references

Sequence databases

J02581 Genomic DNA. Translation: AAA72182.1.
PIRA24698.

3D structure databases

HSSPHSSP built from PDB template 1AA6 based on UniProtKB P07658.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.2. 7357.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_fold.
IPR006478. Formate_DH_asu.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_Fe4S4.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006657. MPT_dinuc_bd.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR01591. Fdh-alpha. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFDHA_METFO
AccessionPrimary (citable) accession number: P06131
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents