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

Comments

FUNCTION: Catalyzes the oxidation of formate.
CATALYTIC ACTIVITY: Formate + NAD⁺ = CO₂ + NADH.
COFACTOR: Molybdenum (molybdopterin).
COFACTOR: Zinc.
COFACTOR: FAD.
COFACTOR: Binds 1 4Fe-4S cluster (Potential).
SUBUNIT: Dimer of alpha and beta chains.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02581; AAA72182.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24698; A24698.

3D structure databases

HSSP

P07658; 1AA6. [HSSP ENTRY / PDB]

ModBase

P06131.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009010; Asp_de-COase-like_fold.
IPR006478; Formate_DHase_asu.
IPR006656; Mopterin_OxRdtase.
IPR006963; Mopterin_OxRdtase_Fe4S4.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.

Pfam

PF04879; Molybdop_Fe4S4; 1.
PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01591; Fdh-alpha; 1.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; 1.
PS00490; MOLYBDOPTERIN_PROK_2; 1.
PS00932; MOLYBDOPTERIN_PROK_3; 1.

Other

P06131; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 684`	`684`	`Formate dehydrogenase alpha chain.`	`PRO_0000063225`
`METAL`	`10 10`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`13 13`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`17 17`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`45 45`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 684 AA [This is the length of the unprocessed precursor]

Molecular weight: 75717 Da [This is the MW of the unprocessed precursor]

CRC64: 38D37CF86BFF06E2 [This is a checksum on the sequence]

        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

P06131 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools