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Protein

Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit

Gene

fdnI

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. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).1 Publication

Cofactori

heme1 PublicationNote: Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18Iron (heme B 1 axial ligand); via tele nitrogen1
Metal bindingi57Iron (heme B 2 axial ligand); via tele nitrogen1
Metal bindingi155Iron (heme B 2 axial ligand); via tele nitrogen1
Metal bindingi169Iron (heme B 1 axial ligand); via tele nitrogen1
Binding sitei169Menaquinone; via pros nitrogen1

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • formate dehydrogenase (NAD+) activity Source: InterPro
  • formate dehydrogenase (quinone) activity Source: EcoCyc
  • heme binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • formate oxidation Source: EcoCyc
  • respiratory electron transport chain Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FDNI-MONOMER.
ECOL316407:JW1472-MONOMER.
MetaCyc:FDNI-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, cytochrome b556(Fdn) subunit
Alternative name(s):
Anaerobic formate dehydrogenase cytochrome b556 subunit
Formate dehydrogenase-N subunit gamma
Short name:
FDH-N subunit gamma
Gene namesi
Name:fdnI
Ordered Locus Names:b1476, JW1472
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11229. fdnI.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11Cytoplasmic1 PublicationAdd BLAST11
Transmembranei12 – 36HelicalAdd BLAST25
Topological domaini37 – 52Periplasmic1 PublicationAdd BLAST16
Transmembranei53 – 74HelicalAdd BLAST22
Topological domaini75 – 110Cytoplasmic1 PublicationAdd BLAST36
Transmembranei111 – 134HelicalAdd BLAST24
Topological domaini135 – 150Periplasmic1 PublicationAdd BLAST16
Transmembranei151 – 175HelicalAdd BLAST25
Topological domaini176 – 217Cytoplasmic1 PublicationAdd BLAST42

GO - Cellular componenti

  • formate dehydrogenase complex Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000872101 – 217Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunitAdd BLAST217

Proteomic databases

PaxDbiP0AEK7.
PRIDEiP0AEK7.

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

BioGridi4262903. 6 interactors.
IntActiP0AEK7. 1 interactor.
STRINGi511145.b1476.

Structurei

Secondary structure

1217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi12 – 36Combined sources25
Helixi41 – 45Combined sources5
Helixi50 – 75Combined sources26
Helixi76 – 78Combined sources3
Helixi83 – 85Combined sources3
Helixi86 – 90Combined sources5
Helixi92 – 96Combined sources5
Helixi100 – 103Combined sources4
Helixi111 – 133Combined sources23
Turni136 – 139Combined sources4
Helixi140 – 142Combined sources3
Helixi145 – 175Combined sources31
Helixi179 – 184Combined sources6
Beta strandi187 – 189Combined sources3
Helixi190 – 196Combined sources7
Helixi198 – 215Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60C1-217[»]
1KQGX-ray2.80C1-217[»]
ProteinModelPortaliP0AEK7.
SMRiP0AEK7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEK7.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108MG3. Bacteria.
COG2864. LUCA.
HOGENOMiHOG000163500.
InParanoidiP0AEK7.
KOiK08350.
OMAiKQDIPWL.
PhylomeDBiP0AEK7.

Family and domain databases

InterProiIPR011577. Cyt_b561_bac/Ni-Hgenase.
IPR016174. Di-haem_cyt_TM.
IPR006471. Formate_DH_gsu.
[Graphical view]
PfamiPF01292. Ni_hydr_CYTB. 1 hit.
[Graphical view]
SUPFAMiSSF81342. SSF81342. 1 hit.
TIGRFAMsiTIGR01583. formate-DH-gamm. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AEK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSKMIVRT KFIDRACHWT VVICFFLVAL SGISFFFPTL QWLTQTFGTP
60 70 80 90 100
QMGRILHPFF GIAIFVALMF MFVRFVHHNI PDKKDIPWLL NIVEVLKGNE
110 120 130 140 150
HKVADVGKYN AGQKMMFWSI MSMIFVLLVT GVIIWRPYFA QYFPMQVVRY
160 170 180 190 200
SLLIHAAAGI ILIHAILIHM YMAFWVKGSI KGMIEGKVSR RWAKKHHPRW
210
YREIEKAEAK KESEEGI
Length:217
Mass (Da):25,368
Last modified:December 20, 2005 - v1
Checksum:iB10073F14343515E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160 – 217IILIH…SEEGI → YHPDPRHPDPYVYGILGERI D (PubMed:1834669).CuratedAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75029 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAD13440.1.
AP009048 Genomic DNA. Translation: BAA15125.1.
PIRiG64900. JS0630.
RefSeqiNP_415993.1. NC_000913.3.
WP_000045648.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAD13440; AAD13440; b1476.
BAA15125; BAA15125; BAA15125.
GeneIDi946038.
KEGGiecj:JW1472.
eco:b1476.
PATRICi32118244. VBIEscCol129921_1542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75029 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAD13440.1.
AP009048 Genomic DNA. Translation: BAA15125.1.
PIRiG64900. JS0630.
RefSeqiNP_415993.1. NC_000913.3.
WP_000045648.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60C1-217[»]
1KQGX-ray2.80C1-217[»]
ProteinModelPortaliP0AEK7.
SMRiP0AEK7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262903. 6 interactors.
IntActiP0AEK7. 1 interactor.
STRINGi511145.b1476.

Protein family/group databases

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

Proteomic databases

PaxDbiP0AEK7.
PRIDEiP0AEK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13440; AAD13440; b1476.
BAA15125; BAA15125; BAA15125.
GeneIDi946038.
KEGGiecj:JW1472.
eco:b1476.
PATRICi32118244. VBIEscCol129921_1542.

Organism-specific databases

EchoBASEiEB1211.
EcoGeneiEG11229. fdnI.

Phylogenomic databases

eggNOGiENOG4108MG3. Bacteria.
COG2864. LUCA.
HOGENOMiHOG000163500.
InParanoidiP0AEK7.
KOiK08350.
OMAiKQDIPWL.
PhylomeDBiP0AEK7.

Enzyme and pathway databases

BioCyciEcoCyc:FDNI-MONOMER.
ECOL316407:JW1472-MONOMER.
MetaCyc:FDNI-MONOMER.
BRENDAi1.1.5.6. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AEK7.
PROiP0AEK7.

Family and domain databases

InterProiIPR011577. Cyt_b561_bac/Ni-Hgenase.
IPR016174. Di-haem_cyt_TM.
IPR006471. Formate_DH_gsu.
[Graphical view]
PfamiPF01292. Ni_hydr_CYTB. 1 hit.
[Graphical view]
SUPFAMiSSF81342. SSF81342. 1 hit.
TIGRFAMsiTIGR01583. formate-DH-gamm. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFDNI_ECOLI
AccessioniPrimary (citable) accession number: P0AEK7
Secondary accession number(s): P24185, P77513
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.