Reviewed, UniProtKB/Swiss-Prot P24183 (FDNG_ECOLI)

Names and origin

Protein names

Recommended name:
    Formate dehydrogenase, nitrate-inducible, major subunit
    EC=1.2.1.2
Alternative name(s):
    Formate dehydrogenase-N subunit alpha
      Short name=FDH-N subunit alpha
    Anaerobic formate dehydrogenase major subunit

Gene names

Name:	fdnG
Ordered Locus Names:	b1474, JW1470

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	1015 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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(+) = CO(2) + NADH.
Cofactor	Binds 1 molybdenum ion per subunit. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit. Binds 1 4Fe-4S cluster per subunit.
Subunit structure	Trimer of heterotrimers, consisting of subunits alpha, beta and gamma.
Subcellular location	Periplasm.
Induction	By nitrate under anaerobic conditions.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
Cellular component	Periplasm
Coding sequence diversity	Selenocysteine
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum NAD Selenium
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular respiration Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro formate dehydrogenase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: InterPro selenium binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Tat-type signal Potential

Chain

34 – 1015

982

Formate dehydrogenase, nitrate-inducible, major subunit

PRO_0000063222

Sites

Metal binding

50

1

Iron-sulfur (4Fe-4S)

Metal binding

53

1

Iron-sulfur (4Fe-4S)

Metal binding

57

1

Iron-sulfur (4Fe-4S)

Metal binding

92

1

Iron-sulfur (4Fe-4S)

Metal binding

196

1

Molybdenum

Amino acid modifications

Non-standard residue

196

1

Selenocysteine

Experimental info

Sequence conflict

96

1

A → P Ref.1

Sequence conflict

484 – 491

8

ANTPKATL → GEHAERRRW Ref.1

Sequence conflict

941

1

S → A Ref.1

Secondary structure

1

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1015

Helix Strand Turn

Details...

Turn

39 – 42

4

Beta strand

43 – 49

7

Beta strand

51 – 53

3

Turn

54 – 55

2

Beta strand

58 – 65

8

Turn

69 – 70

2

Beta strand

74 – 80

7

Turn

85 – 89

5

Helix

93 – 96

4

Turn

97 – 98

2

Helix

99 – 102

4

Turn

103

1

Turn

105 – 106

2

Beta strand

112 – 114

3

Turn

116 – 117

2

Helix

126 – 144

19

Beta strand

146 – 148

3

Turn

150 – 151

2

Beta strand

154 – 158

5

Beta 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

1

Helix

218 – 222

5

Beta strand

224 – 230

7

Helix

233 – 236

4

Turn

238 – 241

4

Helix

242 – 250

9

Beta strand

254 – 258

5

Helix

264 – 267

4

Turn

268

1

Beta strand

270 – 273

4

Turn

277 – 278

2

Helix

280 – 293

14

Turn

294 – 295

2

Helix

299 – 305

7

Turn

308 – 309

2

Beta strand

310 – 312

3

Turn

314 – 315

2

Turn

320 – 321

2

Turn

324 – 325

2

Turn

328 – 331

4

Turn

336 – 337

2