[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; PubMed=2941757 [NCBI, ExPASy, EBI, Israel, Japan] Zinoni F., Birkmann A., Stadtman T.C., Boeck A.; "Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli."; Proc. Natl. Acad. Sci. U.S.A. 83:4650-4654(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."; Nucleic Acids Res. 21:5408-5417(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	PROTEIN SEQUENCE OF 1-12, AND CHARACTERIZATION. PubMed=2211698 [NCBI, ExPASy, EBI, Israel, Japan] Axley M.J., Grahame D.A., Stadtman T.C.; "Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component."; J. Biol. Chem. 265:18213-18218(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SELENOCYSTEINE AT SEC-140. DOI=10.1126/science.275.5304.1305; PubMed=9036855 [NCBI, ExPASy, EBI, Israel, Japan] Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D.; "Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster."; Science 275:1305-1308(1997).

Comments

FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.
CATALYTIC ACTIVITY: Formate + NAD⁺ = CO₂ + NADH.
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) per subunit.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
COFACTOR: Binds 1 molybdenum ion per subunit.
SUBUNIT: Consists of two separable enzymatic activities: a formate dehydrogenase component (FDH-H) and hydrogenase-3.
INDUCTION: By formate. Repressed by oxygen, nitrate, nitrite, and other electron acceptors.
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

M13563; AAA23754.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43173.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAD13462.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78081.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24145; DEECFS.

RefSeq

AP_004580.1; -.
NP_418503.1; -.

3D structure databases

PDB

1AA6; X-ray; 2.30 A; A=1-715.	[ExPASy / RCSB / EBI]
1FDI; X-ray; 2.90 A; A=1-715.	[ExPASy / RCSB / EBI]
1FDO; X-ray; 2.80 A; A=1-715.	[ExPASy / RCSB / EBI]
2IV2; X-ray; 2.27 A; X=1-715.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AA6; -.
1FDI; -.
1FDO; -.
2IV2; -.

ModBase

P07658.

Enzyme and pathway databases

BioCyc

EcoCyc:FORMATEDEHYDROGH-MON; -.
MetaCyc:FORMATEDEHYDROGH-MON; -.

Organism-specific databases

EchoBASE

EB0281; -.

EcoGene

EG10285; fdhF.

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:0008430;	Molecular function: selenium 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.

Genome annotation databases

GeneID

948584; -.

GenomeReviews

U00096_GR; b4079.
AP009048_GR; JW4040.

KEGG

ecj:JW4040; -.
eco:b4079; -.

Phylogenomic databases

HOGENOM

P07658; -.

Other

LinkHub

P07658; -.

Genome annotation databases

CMR

P07658; b4079.

Other

UniRef

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

Keywords

3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 715`	`715`	`Formate dehydrogenase H.`	`PRO_0000063221`
`METAL`	`8 8`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`11 11`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`15 15`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`42 42`		`Iron-sulfur (4Fe-4S) (By similarity).`
`NON_STD`	`140 140`		`Selenocysteine.`
`CONFLICT`	`19 19`		`L -> V (in Ref. 1; AAA23754).`
`STRAND`	`2 7`	`6`
`STRAND`	`9 11`	`3`
`STRAND`	`16 22`	`7`
`STRAND`	`25 31`	`7`
`TURN`	`35 39`	`5`
`HELIX`	`43 47`	`5`
`HELIX`	`50 53`	`4`
`STRAND`	`57 59`	`3`
`HELIX`	`80 98`	`19`
`HELIX`	`100 102`	`3`
`STRAND`	`103 106`	`4`
`HELIX`	`114 126`	`13`
`STRAND`	`143 145`	`3`
`HELIX`	`148 152`	`5`
`HELIX`	`161 166`	`6`
`STRAND`	`168 174`	`7`
`HELIX`	`177 180`	`4`
`HELIX`	`182 193`	`12`
`STRAND`	`197 201`	`5`
`HELIX`	`207 210`	`4`
`STRAND`	`213 216`	`4`
`HELIX`	`223 236`	`14`
`HELIX`	`242 248`	`7`
`HELIX`	`252 260`	`9`
`HELIX`	`265 267`	`3`
`HELIX`	`268 271`	`4`
`HELIX`	`275 287`	`13`
`STRAND`	`288 296`	`9`
`HELIX`	`299 301`	`3`
`STRAND`	`302 304`	`3`
`HELIX`	`305 318`	`14`
`STRAND`	`322 324`	`3`
`STRAND`	`328 332`	`5`
`HELIX`	`338 343`	`6`
`HELIX`	`352 354`	`3`
`HELIX`	`360 369`	`10`
`HELIX`	`383 385`	`3`
`HELIX`	`386 391`	`6`
`STRAND`	`397 402`	`6`
`HELIX`	`405 408`	`4`
`STRAND`	`409 411`	`3`
`HELIX`	`412 421`	`10`
`STRAND`	`422 431`	`10`
`HELIX`	`434 437`	`4`
`STRAND`	`440 445`	`6`
`STRAND`	`453 456`	`4`
`STRAND`	`460 465`	`6`
`STRAND`	`472 474`	`3`
`HELIX`	`478 488`	`11`
`HELIX`	`498 508`	`11`
`TURN`	`510 514`	`5`
`HELIX`	`517 520`	`4`
`TURN`	`521 523`	`3`
`STRAND`	`526 528`	`3`
`STRAND`	`541 543`	`3`
`STRAND`	`571 573`	`3`
`STRAND`	`575 579`	`5`
`HELIX`	`592 594`	`3`
`HELIX`	`596 599`	`4`
`STRAND`	`607 611`	`5`
`HELIX`	`612 618`	`7`
`STRAND`	`625 629`	`5`
`STRAND`	`634 645`	`12`
`STRAND`	`649 652`	`4`
`STRAND`	`681 687`	`7`
`HELIX`	`691 713`	`23`

Sequence information

Length: 715 AA [This is the length of the unprocessed precursor]

Molecular weight: 79374 Da [This is the MW of the unprocessed precursor]

CRC64: C7C86F6F704A142D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD FINDTQILTP 

        70         80         90        100        110        120 
RLKTPMIRRQ RGGKLEPVSW DEALNYVAER LSAIKEKYGP DAIQTTGSSR GTGNETNYVM 

       130        140        150        160        170        180 
QKFARAVIGT NNVDCCARVU HGPSVAGLHQ SVGNGAMSNA INEIDNTDLV FVFGYNPADS 

       190        200        210        220        230        240 
HPIVANHVIN AKRNGAKIIV CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY 

       250        260        270        280        290        300 
DKAFVASRTE GFEEYRKIVE GYTPESVEDI TGVSASEIRQ AARMYAQAKS AAILWGMGVT 

       310        320        330        340        350        360 
QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT YPGYQYVKDP 

       370        380        390        400        410        420 
ANREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI MGEDPLQTDA ELSAVRKAFE 

       430        440        450        460        470        480 
DLELVIVQDI FMTKTASAAD VILPSTSWGE HEGVFTAADR GFQRFFKAVE PKWDLKTDWQ 

       490        500        510        520        530        540 
IISEIATRMG YPMHYNNTQE IWDELRHLCP DFYGATYEKM GELGFIQWPC RDTSDADQGT 

       550        560        570        580        590        600 
SYLFKEKFDT PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA 

       610        620        630        640        650        660 
LADEPGYAQI NTEDAKRLGI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI YMTYQWWIGA 

       670        680        690        700        710 
CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID EYNKLKTRLR EAALA

P07658 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