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Protein

Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit

Gene

fdnH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S)
Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S)
Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)
Metal bindingi49 – 491Iron-sulfur 2 (4Fe-4S)
Metal bindingi100 – 1001Iron-sulfur 3 (4Fe-4S)
Metal bindingi103 – 1031Iron-sulfur 3 (4Fe-4S)
Metal bindingi108 – 1081Iron-sulfur 3 (4Fe-4S)
Metal bindingi112 – 1121Iron-sulfur 4 (4Fe-4S)
Metal bindingi133 – 1331Iron-sulfur 4 (4Fe-4S)
Metal bindingi136 – 1361Iron-sulfur 4 (4Fe-4S)
Metal bindingi139 – 1391Iron-sulfur 4 (4Fe-4S)
Metal bindingi143 – 1431Iron-sulfur 3 (4Fe-4S)
Metal bindingi160 – 1601Iron-sulfur 2 (4Fe-4S)
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S)
Metal bindingi175 – 1751Iron-sulfur 2 (4Fe-4S)
Metal bindingi179 – 1791Iron-sulfur 1 (4Fe-4S)

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier 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
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FDNH-MONOMER.
ECOL316407:JW1471-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 256256PeriplasmicAdd
BLAST
Transmembranei257 – 27923HelicalAdd
BLAST
Topological domaini280 – 29415CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • formate dehydrogenase complex Source: EcoCyc
  • integral component of external side of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Formate dehydrogenase, nitrate-inducible, iron-sulfur subunitPRO_0000159247Add
BLAST

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. 8 interactions.
DIPiDIP-35836N.
IntActiP0AAJ3. 18 interactions.
MINTiMINT-1286317.
STRINGi511145.b1475.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Beta strandi30 – 356Combined sources
Turni36 – 383Combined sources
Helixi44 – 5310Combined sources
Beta strandi63 – 664Combined sources
Beta strandi69 – 713Combined sources
Beta strandi79 – 857Combined sources
Beta strandi92 – 998Combined sources
Beta strandi103 – 1053Combined sources
Helixi107 – 1115Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi126 – 1283Combined sources
Helixi130 – 1323Combined sources
Helixi138 – 1425Combined sources
Turni152 – 1543Combined sources
Helixi164 – 1674Combined sources
Turni168 – 1703Combined sources
Helixi174 – 1785Combined sources
Beta strandi184 – 1885Combined sources
Helixi189 – 20517Combined sources
Beta strandi212 – 2143Combined sources
Helixi217 – 2193Combined sources
Beta strandi222 – 2287Combined sources
Turni229 – 2324Combined sources
Helixi234 – 2363Combined sources
Turni237 – 2393Combined sources
Helixi248 – 2547Combined sources
Helixi257 – 27923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60B1-294[»]
1KQGX-ray2.80B1-294[»]
ProteinModelPortaliP0AAJ3.
SMRiP0AAJ3. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAJ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 58294Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini91 – 123334Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 153304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 189324Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105QA4. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163382.
InParanoidiP0AAJ3.
KOiK08349.
OMAiQQDNCIG.
PhylomeDBiP0AAJ3.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR006470. Formate_DH_bsu_Proteobacteria.
IPR014603. Formate_DH_Fe-S_su.
IPR015246. Formate_DH_TM.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF12800. Fer4_4. 1 hit.
PF09163. Form-deh_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF036298. FDH_4Fe4S. 1 hit.
TIGRFAMsiTIGR01582. FDH-beta. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1022MH → ID (PubMed:1834669).Curated

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.
PATRICi32118242. VBIEscCol129921_1541.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60B1-294[»]
1KQGX-ray2.80B1-294[»]
ProteinModelPortaliP0AAJ3.
SMRiP0AAJ3. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262901. 8 interactions.
DIPiDIP-35836N.
IntActiP0AAJ3. 18 interactions.
MINTiMINT-1286317.
STRINGi511145.b1475.

Protein family/group databases

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

Proteomic databases

PaxDbiP0AAJ3.
PRIDEiP0AAJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13439; AAD13439; b1475.
BAA15124; BAA15124; BAA15124.
GeneIDi948794.
KEGGiecj:JW1471.
eco:b1475.
PATRICi32118242. VBIEscCol129921_1541.

Organism-specific databases

EchoBASEiEB1210.
EcoGeneiEG11228. fdnH.

Phylogenomic databases

eggNOGiENOG4105QA4. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163382.
InParanoidiP0AAJ3.
KOiK08349.
OMAiQQDNCIG.
PhylomeDBiP0AAJ3.

Enzyme and pathway databases

BioCyciEcoCyc:FDNH-MONOMER.
ECOL316407:JW1471-MONOMER.
MetaCyc:FDNH-MONOMER.
BRENDAi1.1.5.6. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AAJ3.
PROiP0AAJ3.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR006470. Formate_DH_bsu_Proteobacteria.
IPR014603. Formate_DH_Fe-S_su.
IPR015246. Formate_DH_TM.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF12800. Fer4_4. 1 hit.
PF09163. Form-deh_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF036298. FDH_4Fe4S. 1 hit.
TIGRFAMsiTIGR01582. FDH-beta. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFDNH_ECOLI
AccessioniPrimary (citable) accession number: P0AAJ3
Secondary accession number(s): P24184, P77166
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: September 7, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.