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Protein

Formate dehydrogenase, nitrate-inducible, major subunit

Gene

fdnG

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 alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).1 Publication

Catalytic activityi

Formate + a quinone = CO2 + a quinol.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mo-bis(molybdopterin guanine dinucleotide)1 PublicationNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.1 Publication
  • [4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Iron-sulfur (4Fe-4S)1
Metal bindingi53Iron-sulfur (4Fe-4S)1
Metal bindingi57Iron-sulfur (4Fe-4S)1
Metal bindingi92Iron-sulfur (4Fe-4S)1
Metal bindingi196Molybdenum1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: EcoCyc
  • formate dehydrogenase (cytochrome-c-553) activity Source: InterPro
  • formate dehydrogenase (NAD+) activity Source: InterPro
  • formate dehydrogenase (quinone) activity Source: EcoCyc
  • molybdenum ion binding Source: EcoCyc
  • molybdopterin cofactor binding Source: InterPro
  • selenium binding Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • formate oxidation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciEcoCyc:FDNG-MONOMER.
ECOL316407:JW1470-MONOMER.
MetaCyc:FDNG-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, major subunit (EC:1.1.5.6)
Alternative name(s):
Anaerobic formate dehydrogenase major subunit
Formate dehydrogenase-N subunit alpha
Short name:
FDH-N subunit alpha
Gene namesi
Name:fdnG
Ordered Locus Names:b1474, JW1470
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11227. fdnG.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

  • formate dehydrogenase complex Source: EcoCyc
  • membrane Source: UniProtKB
  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Tat-type signalPROSITE-ProRule annotationAdd BLAST33
ChainiPRO_000006322234 – 1015Formate dehydrogenase, nitrate-inducible, major subunitAdd BLAST982

Post-translational modificationi

Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Proteomic databases

PaxDbiP24183.
PRIDEiP24183.

Expressioni

Inductioni

By nitrate under anaerobic conditions.1 Publication

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
fdhEP130244EBI-550115,EBI-550129

Protein-protein interaction databases

BioGridi4262900. 4 interactors.
DIPiDIP-9573N.
IntActiP24183. 14 interactors.
MINTiMINT-1236143.
STRINGi511145.b1474.

Structurei

Secondary structure

11015
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni39 – 42Combined sources4
Beta strandi43 – 49Combined sources7
Beta strandi51 – 53Combined sources3
Beta strandi58 – 65Combined sources8
Beta strandi74 – 80Combined sources7
Turni85 – 89Combined sources5
Helixi93 – 96Combined sources4
Helixi99 – 102Combined sources4
Beta strandi112 – 114Combined sources3
Helixi126 – 144Combined sources19
Beta strandi146 – 148Combined sources3
Beta strandi154 – 158Combined sources5
Beta strandi160 – 164Combined sources5
Helixi171 – 183Combined sources13
Beta strandi189 – 191Combined sources3
Helixi192 – 195Combined sources4
Helixi198 – 208Combined sources11
Helixi218 – 222Combined sources5
Beta strandi224 – 230Combined sources7
Helixi233 – 236Combined sources4
Turni238 – 241Combined sources4
Helixi242 – 250Combined sources9
Beta strandi254 – 258Combined sources5
Helixi264 – 267Combined sources4
Beta strandi270 – 273Combined sources4
Helixi280 – 293Combined sources14
Helixi299 – 305Combined sources7
Beta strandi310 – 312Combined sources3
Turni328 – 331Combined sources4
Beta strandi338 – 340Combined sources3
Beta strandi346 – 348Combined sources3
Helixi360 – 368Combined sources9
Helixi373 – 380Combined sources8
Helixi384 – 395Combined sources12
Helixi396 – 398Combined sources3
Beta strandi404 – 409Combined sources6
Helixi410 – 413Combined sources4
Helixi418 – 431Combined sources14
Beta strandi441 – 444Combined sources4
Helixi451 – 456Combined sources6
Helixi465 – 467Combined sources3
Helixi478 – 485Combined sources8
Beta strandi490 – 493Combined sources4
Helixi497 – 500Combined sources4
Helixi501 – 513Combined sources13
Helixi514 – 516Combined sources3
Helixi519 – 527Combined sources9
Beta strandi531 – 533Combined sources3
Helixi537 – 545Combined sources9
Beta strandi551 – 556Combined sources6
Helixi559 – 562Combined sources4
Beta strandi563 – 565Combined sources3
Helixi566 – 573Combined sources8
Beta strandi577 – 585Combined sources9
Turni588 – 593Combined sources6
Helixi597 – 600Combined sources4
Helixi604 – 606Combined sources3
Beta strandi610 – 616Combined sources7
Helixi619 – 621Combined sources3
Beta strandi624 – 627Combined sources4
Beta strandi632 – 636Combined sources5
Helixi649 – 667Combined sources19
Helixi672 – 677Combined sources6
Helixi690 – 698Combined sources9
Beta strandi700 – 703Combined sources4
Beta strandi712 – 714Combined sources3
Helixi723 – 725Combined sources3
Beta strandi728 – 733Combined sources6
Helixi737 – 739Combined sources3
Beta strandi742 – 744Combined sources3
Helixi749 – 751Combined sources3
Beta strandi760 – 762Combined sources3
Beta strandi767 – 770Combined sources4
Turni771 – 774Combined sources4
Helixi780 – 783Combined sources4
Beta strandi790 – 792Combined sources3
Helixi793 – 795Combined sources3
Beta strandi798 – 800Combined sources3
Beta strandi802 – 809Combined sources8
Beta strandi831 – 833Combined sources3
Beta strandi856 – 859Combined sources4
Helixi876 – 879Combined sources4
Turni885 – 887Combined sources3
Beta strandi890 – 895Combined sources6
Turni902 – 904Combined sources3
Helixi905 – 907Combined sources3
Helixi909 – 914Combined sources6
Beta strandi919 – 922Combined sources4
Helixi924 – 930Combined sources7
Beta strandi937 – 941Combined sources5
Beta strandi946 – 953Combined sources8
Beta strandi960 – 962Combined sources3
Beta strandi965 – 967Combined sources3
Beta strandi969 – 973Combined sources5
Beta strandi978 – 982Combined sources5
Helixi988 – 990Combined sources3
Turni998 – 1000Combined sources3
Beta strandi1007 – 1014Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60A1-1015[»]
1KQGX-ray2.80A1-1015[»]
ProteinModelPortaliP24183.
SMRiP24183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24183.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 1064Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST64

Sequence similaritiesi

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QIW. Bacteria.
COG0243. LUCA.
HOGENOMiHOG000163271.
InParanoidiP24183.
KOiK08348.
OMAiPLHWGFE.
PhylomeDBiP24183.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate-DH-alph_fdnG.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01553. formate-DH-alph. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24183-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC
60 70 80 90 100
TYCSVGCGLL MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD
110 120 130 140 150
YVNSENRLRY PEYRAPGSDK WQRISWEEAF SRIAKLMKAD RDANFIEKNE
160 170 180 190 200
QGVTVNRWLS TGMLCASGAS NETGMLTQKF ARSLGMLAVD NQARVUHGPT
210 220 230 240 250
VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG FRWAMEAKNN
260 270 280 290 300
NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE
310 320 330 340 350
YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR
360 370 380 390 400
DETLTHPRCV WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP
410 420 430 440 450
DRTTTFLYAL GWTQHTVGAQ NIRTMAMIQL LLGNMGMAGG GVNALRGHSN
460 470 480 490 500
IQGLTDLGLL STSLPGYLTL PSEKQVDLQS YLEANTPKAT LADQVNYWSN
510 520 530 540 550
YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY FNMMDEGKVT
560 570 580 590 600
GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN
610 620 630 640 650
DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG
660 670 680 690 700
EILAGIYHHL RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY
710 720 730 740 750
ALEDLYDANG VLIAKKGQLL SSFAHLRDDG TTASSCWIYT GSWTEQGNQM
760 770 780 790 800
ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN RASADINGKP WDPKRMLIQW
810 820 830 840 850
NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK MAEGPFPEHY
860 870 880 890 900
EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH
910 920 930 940 950
FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV
960 970 980 990 1000
AVVTRRLKPL NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS
1010
QTPEYKAFLV NIEKA
Length:1,015
Mass (Da):112,963
Last modified:February 26, 2008 - v3
Checksum:iE4B9449D6B2407DA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96A → P (PubMed:1834669).Curated1
Sequence conflicti484 – 491ANTPKATL → GEHAERRRW (PubMed:1834669).Curated8
Sequence conflicti941S → A (PubMed:1834669).Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei196Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75029 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAD13438.1.
AP009048 Genomic DNA. Translation: BAA15123.1.
PIRiE64900. JS0628.
RefSeqiNP_415991.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAD13438; AAD13438; b1474.
BAA15123; BAA15123; BAA15123.
GeneIDi946035.
KEGGiecj:JW1470.
eco:b1474.
PATRICi32118240. VBIEscCol129921_1540.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75029 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAD13438.1.
AP009048 Genomic DNA. Translation: BAA15123.1.
PIRiE64900. JS0628.
RefSeqiNP_415991.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60A1-1015[»]
1KQGX-ray2.80A1-1015[»]
ProteinModelPortaliP24183.
SMRiP24183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262900. 4 interactors.
DIPiDIP-9573N.
IntActiP24183. 14 interactors.
MINTiMINT-1236143.
STRINGi511145.b1474.

Protein family/group databases

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

Proteomic databases

PaxDbiP24183.
PRIDEiP24183.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD13438; AAD13438; b1474.
BAA15123; BAA15123; BAA15123.
GeneIDi946035.
KEGGiecj:JW1470.
eco:b1474.
PATRICi32118240. VBIEscCol129921_1540.

Organism-specific databases

EchoBASEiEB1209.
EcoGeneiEG11227. fdnG.

Phylogenomic databases

eggNOGiENOG4107QIW. Bacteria.
COG0243. LUCA.
HOGENOMiHOG000163271.
InParanoidiP24183.
KOiK08348.
OMAiPLHWGFE.
PhylomeDBiP24183.

Enzyme and pathway databases

BioCyciEcoCyc:FDNG-MONOMER.
ECOL316407:JW1470-MONOMER.
MetaCyc:FDNG-MONOMER.
BRENDAi1.1.5.6. 2026.

Miscellaneous databases

EvolutionaryTraceiP24183.
PROiP24183.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate-DH-alph_fdnG.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01553. formate-DH-alph. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFDNG_ECOLI
AccessioniPrimary (citable) accession number: P24183
Secondary accession number(s): P78261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 165 of the entry and version 3 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.