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Protein

Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit

Gene

fdnH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).1 Publication

Miscellaneous

The 4Fe-4S clusters from PubMed:11884747 are renumbered in standard order.

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 4 [4Fe-4S] clusters per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi39Iron-sulfur 1 (4Fe-4S)1
Metal bindingi42Iron-sulfur 1 (4Fe-4S)1
Metal bindingi45Iron-sulfur 1 (4Fe-4S)1
Metal bindingi49Iron-sulfur 2 (4Fe-4S)1
Metal bindingi100Iron-sulfur 3 (4Fe-4S)1
Metal bindingi103Iron-sulfur 3 (4Fe-4S)1
Metal bindingi108Iron-sulfur 3 (4Fe-4S)1
Metal bindingi112Iron-sulfur 4 (4Fe-4S)1
Metal bindingi133Iron-sulfur 4 (4Fe-4S)1
Metal bindingi136Iron-sulfur 4 (4Fe-4S)1
Metal bindingi139Iron-sulfur 4 (4Fe-4S)1
Metal bindingi143Iron-sulfur 3 (4Fe-4S)1
Metal bindingi160Iron-sulfur 2 (4Fe-4S)1
Metal bindingi163Iron-sulfur 2 (4Fe-4S)1
Metal bindingi175Iron-sulfur 2 (4Fe-4S)1
Metal bindingi179Iron-sulfur 1 (4Fe-4S)1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron transfer activity Source: EcoCyc
  • formate dehydrogenase (quinone) activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • formate oxidation Source: EcoCyc

Keywordsi

Biological processElectron transport, Transport
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FDNH-MONOMER
MetaCyc:FDNH-MONOMER
BRENDAi1.1.5.6 2026

Protein family/group databases

TCDBi5.A.3.2.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit
Alternative name(s):
Anaerobic formate dehydrogenase iron-sulfur subunit
Formate dehydrogenase-N subunit beta
Short name:
FDH-N subunit beta
Gene namesi
Name:fdnH
Ordered Locus Names:b1475, JW1471
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11228 fdnH

Subcellular locationi

  • Cell inner membrane 1 Publication; Single-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 256PeriplasmicAdd BLAST256
Transmembranei257 – 279HelicalAdd BLAST23
Topological domaini280 – 294CytoplasmicAdd BLAST15

GO - Cellular componenti

  • formate dehydrogenase complex Source: EcoCyc
  • integral component of external side of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB07918 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001592471 – 294Formate dehydrogenase, nitrate-inducible, iron-sulfur subunitAdd BLAST294

Proteomic databases

PaxDbiP0AAJ3
PRIDEiP0AAJ3

Expressioni

Inductioni

By nitrate under anaerobic conditions.1 Publication

Interactioni

Subunit structurei

Trimer of heterotrimers, consisting of subunits alpha, beta and gamma.1 Publication

Protein-protein interaction databases

BioGridi4262901, 24 interactors
DIPiDIP-35836N
IntActiP0AAJ3, 18 interactors
STRINGi316385.ECDH10B_1606

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Beta strandi30 – 35Combined sources6
Turni36 – 38Combined sources3
Helixi44 – 53Combined sources10
Beta strandi63 – 66Combined sources4
Beta strandi69 – 71Combined sources3
Beta strandi79 – 85Combined sources7
Beta strandi92 – 99Combined sources8
Beta strandi103 – 105Combined sources3
Helixi107 – 111Combined sources5
Beta strandi117 – 121Combined sources5
Beta strandi126 – 128Combined sources3
Helixi130 – 132Combined sources3
Helixi138 – 142Combined sources5
Turni152 – 154Combined sources3
Helixi164 – 167Combined sources4
Turni168 – 170Combined sources3
Helixi174 – 178Combined sources5
Beta strandi184 – 188Combined sources5
Helixi189 – 205Combined sources17
Beta strandi212 – 214Combined sources3
Helixi217 – 219Combined sources3
Beta strandi222 – 228Combined sources7
Turni229 – 232Combined sources4
Helixi234 – 236Combined sources3
Turni237 – 239Combined sources3
Helixi248 – 254Combined sources7
Helixi257 – 279Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60B1-294[»]
1KQGX-ray2.80B1-294[»]
ProteinModelPortaliP0AAJ3
SMRiP0AAJ3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAJ3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 584Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini91 – 1234Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST33
Domaini124 – 1534Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30
Domaini158 – 1894Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105QA4 Bacteria
COG0437 LUCA
HOGENOMiHOG000163382
InParanoidiP0AAJ3
KOiK08349
OMAiCVDRIQN
PhylomeDBiP0AAJ3

Family and domain databases

CDDicd10558 FDH-N, 1 hit
Gene3Di1.20.5.480, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR006470 Formate_DH_bsu_Proteobacteria
IPR038384 Formate_DH_C_sf
IPR014603 Formate_DH_Fe-S_su
IPR015246 Formate_DH_TM
PfamiView protein in Pfam
PF13247 Fer4_11, 1 hit
PF12800 Fer4_4, 1 hit
PF09163 Form-deh_trans, 1 hit
PIRSFiPIRSF036298 FDH_4Fe4S, 1 hit
TIGRFAMsiTIGR01582 FDH-beta, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 1 hit
PS51379 4FE4S_FER_2, 4 hits

Sequencei

Sequence statusi: Complete.

P0AAJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMETQDIIK RSATNSITPP SQVRDYKAEV AKLIDVSTCI GCKACQVACS
60 70 80 90 100
EWNDIRDEVG HCVGVYDNPA DLSAKSWTVM RFSETEQNGK LEWLIRKDGC
110 120 130 140 150
MHCEDPGCLK ACPSAGAIIQ YANGIVDFQS ENCIGCGYCI AGCPFNIPRL
160 170 180 190 200
NKEDNRVYKC TLCVDRVSVG QEPACVKTCP TGAIHFGTKK EMLELAEQRV
210 220 230 240 250
AKLKARGYEH AGVYNPEGVG GTHVMYVLHH ADQPELYHGL PKDPKIDTSV
260 270 280 290
SLWKGALKPL AAAGFIATFA GLIFHYIGIG PNKEVDDDEE DHHE
Length:294
Mass (Da):32,239
Last modified:October 11, 2005 - v1
Checksum:i44F361F4AC0AEF36
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101 – 102MH → ID (PubMed:1834669).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75029 Genomic DNA No translation available.
U00096 Genomic DNA Translation: AAD13439.1
AP009048 Genomic DNA Translation: BAA15124.1
PIRiF64900 JS0629
RefSeqiNP_415992.1, NC_000913.3
WP_001240582.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAD13439; AAD13439; b1475
BAA15124; BAA15124; BAA15124
GeneIDi948794
KEGGiecj:JW1471
eco:b1475
PATRICifig|1411691.4.peg.792

Similar proteinsi

Entry informationi

Entry nameiFDNH_ECOLI
AccessioniPrimary (citable) accession number: P0AAJ3
Secondary accession number(s): P24184, P77166
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: March 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health