[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-196. STRAIN=K12; PubMed=1834669 [NCBI, ExPASy, EBI, Israel, Japan] Berg B.L., Li J., Heider J., Stewart V.; "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine."; J. Biol. Chem. 266:22380-22385(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan] Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."; DNA Res. 3:363-377(1996).
[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]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). DOI=10.1126/science.1068186; PubMed=11884747 [NCBI, ExPASy, EBI, Israel, Japan] Jormakka M., Tornroth S., Byrne B., Iwata S.; "Molecular basis of proton motive force generation: structure of formate dehydrogenase-N."; Science 295:1863-1868(2002).

Comments

FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit forms the active site.
CATALYTIC ACTIVITY: Formate + NAD⁺ = CO₂ + NADH.
COFACTOR: Binds 1 molybdenum ion per subunit.
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, beta and gamma.
SUBCELLULAR LOCATION: Periplasm.
INDUCTION: By nitrate under anaerobic conditions.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
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

M75029; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
U00096; AAD13438.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15123.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E64900; JS0628.

RefSeq

AP_002097.1; -.
NP_415991.1; -.

3D structure databases

PDB

1KQF; X-ray; 1.60 A; A=1-1015.	[ExPASy / RCSB / EBI]
1KQG; X-ray; 2.80 A; A=1-1015.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KQF; -.
1KQG; -.

ModBase

P24183.

Protein-protein interaction databases

DIP

DIP:9573N; -.

IntAct

P24183; -.

Enzyme and pathway databases

BioCyc

EcoCyc:FDNG-MON; -.
MetaCyc:FDNG-MON; -.

Organism-specific databases

EchoBASE

EB1209; -.

EcoGene

EG11227; fdnG.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008863;	Molecular function: formate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045333;	Biological process: cellular respiration (inferred from electronic annotation from InterPro).
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.
IPR006443; Formate_DH_asu_anaerob.
IPR006656; Mopterin_OxRdtase.
IPR006963; Mopterin_OxRdtase_Fe4S4.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR006311; Tat.
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

TIGR01553; formate-DH-alph; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; 1.
PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
PS00932; MOLYBDOPTERIN_PROK_3; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P24183.

Genome annotation databases

GeneID

946035; -.

GenomeReviews

U00096_GR; b1474.
AP009048_GR; JW1470.

KEGG

ecj:JW1470; -.
eco:b1474; -.

Phylogenomic databases

HOGENOM

P24183; -.

Other

LinkHub

P24183; -.

Genome annotation databases

CMR

P24183; b1474.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`	`Tat-type signal (Potential).`
`CHAIN`	`34 1015`	`982`	`Formate dehydrogenase, nitrate-inducible, major subunit.`	`PRO_0000063222`
`METAL`	`50 50`		`Iron-sulfur (4Fe-4S).`
`METAL`	`53 53`		`Iron-sulfur (4Fe-4S).`
`METAL`	`57 57`		`Iron-sulfur (4Fe-4S).`
`METAL`	`92 92`		`Iron-sulfur (4Fe-4S).`
`METAL`	`196 196`		`Molybdenum.`
`NON_STD`	`196 196`		`Selenocysteine.`
`CONFLICT`	`96 96`		`A -> P (in Ref. 1).`
`CONFLICT`	`484 491`		`ANTPKATL -> GEHAERRRW (in Ref. 1).`
`CONFLICT`	`941 941`		`S -> A (in Ref. 1).`
`TURN`	`39 42`	`4`
`STRAND`	`43 49`	`7`
`STRAND`	`51 53`	`3`
`TURN`	`54 55`	`2`
`STRAND`	`58 65`	`8`
`TURN`	`69 70`	`2`
`STRAND`	`74 80`	`7`
`TURN`	`85 89`	`5`
`HELIX`	`93 96`	`4`
`TURN`	`97 98`	`2`
`HELIX`	`99 102`	`4`
`TURN`	`103 103`	`1`
`TURN`	`105 106`	`2`
`STRAND`	`112 114`	`3`
`TURN`	`116 117`	`2`
`HELIX`	`126 144`	`19`
`STRAND`	`146 148`	`3`
`TURN`	`150 151`	`2`
`STRAND`	`154 158`	`5`
`STRAND`	`160 164`	`5`
`TURN`	`167 168`	`2`
`HELIX`	`171 183`	`13`
`TURN`	`184 185`	`2`
`HELIX`	`192 195`	`4`
`TURN`	`196 197`	`2`
`HELIX`	`198 208`	`11`
`TURN`	`217 217`	`1`
`HELIX`	`218 222`	`5`
`STRAND`	`224 230`	`7`
`HELIX`	`233 236`	`4`
`TURN`	`238 241`	`4`
`HELIX`	`242 250`	`9`
`STRAND`	`254 258`	`5`
`HELIX`	`264 267`	`4`
`TURN`	`268 268`	`1`
`STRAND`	`270 273`	`4`
`TURN`	`277 278`	`2`
`HELIX`	`280 293`	`14`
`TURN`	`294 295`	`2`
`HELIX`	`299 305`	`7`
`TURN`	`308 309`	`2`
`STRAND`	`310 312`	`3`
`TURN`	`314 315`	`2`
`TURN`	`320 321`	`2`
`TURN`	`324 325`	`2`
`TURN`	`328 331`	`4`
`TURN`	`336 337`	`2`
`STRAND`	`338 340`	`3`
`TURN`	`344 345`	`2`
`STRAND`	`346 348`	`3`
`TURN`	`352 353`	`2`
`TURN`	`357 358`	`2`
`HELIX`	`360 368`	`9`
`TURN`	`369 370`	`2`
`HELIX`	`373 380`	`8`
`HELIX`	`384 398`	`15`
`TURN`	`400 401`	`2`
`STRAND`	`404 409`	`6`
`HELIX`	`410 413`	`4`
`TURN`	`416 417`	`2`
`HELIX`	`418 431`	`14`
`TURN`	`432 433`	`2`
`TURN`	`435 436`	`2`
`TURN`	`438 439`	`2`
`STRAND`	`441 444`	`4`
`TURN`	`449 450`	`2`
`HELIX`	`451 456`	`6`
`TURN`	`457 458`	`2`
`TURN`	`461 462`	`2`
`HELIX`	`465 467`	`3`
`TURN`	`473 474`	`2`
`HELIX`	`478 485`	`8`
`STRAND`	`490 493`	`4`
`HELIX`	`497 516`	`20`
`HELIX`	`519 527`	`9`
`STRAND`	`531 533`	`3`
`HELIX`	`537 545`	`9`
`TURN`	`546 547`	`2`
`STRAND`	`551 556`	`6`
`HELIX`	`559 562`	`4`
`STRAND`	`563 565`	`3`
`HELIX`	`566 573`	`8`
`TURN`	`574 575`	`2`
`STRAND`	`577 585`	`9`
`TURN`	`588 593`	`6`
`HELIX`	`597 600`	`4`
`HELIX`	`604 606`	`3`
`STRAND`	`610 616`	`7`
`HELIX`	`619 621`	`3`
`STRAND`	`624 627`	`4`
`TURN`	`629 630`	`2`
`STRAND`	`632 636`	`5`
`TURN`	`644 645`	`2`
`HELIX`	`649 667`	`19`
`HELIX`	`672 677`	`6`
`TURN`	`685 686`	`2`
`HELIX`	`690 698`	`9`
`STRAND`	`700 703`	`4`
`TURN`	`708 709`	`2`
`STRAND`	`712 714`	`3`
`TURN`	`716 717`	`2`
`HELIX`	`723 725`	`3`
`STRAND`	`728 733`	`6`
`HELIX`	`737 739`	`3`
`TURN`	`740 741`	`2`
`STRAND`	`742 744`	`3`
`TURN`	`745 746`	`2`
`HELIX`	`749 751`	`3`
`TURN`	`758 759`	`2`
`STRAND`	`760 762`	`3`
`TURN`	`765 766`	`2`
`TURN`	`771 774`	`4`
`TURN`	`778 779`	`2`
`HELIX`	`780 783`	`4`
`TURN`	`786 787`	`2`
`STRAND`	`790 792`	`3`
`TURN`	`793 794`	`2`
`STRAND`	`798 800`	`3`
`STRAND`	`802 809`	`8`
`TURN`