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P24183 (FDNG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:fdnG
Ordered Locus Names:b1474, JW1470
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1015 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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). Ref.7

Catalytic activity

Formate + a quinone = CO2 + a quinol. Ref.7

Cofactor

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit. Ref.7

Binds 1 4Fe-4S cluster per subunit. Ref.7

Subunit structure

Trimer of heterotrimers, consisting of subunits alpha, beta and gamma. Ref.7

Subcellular location

Periplasm Ref.7.

Induction

By nitrate under anaerobic conditions. Ref.6

Post-translational modification

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.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fdhEP130244EBI-550115,EBI-550129

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333Tat-type signal Potential
Chain34 – 1015982Formate dehydrogenase, nitrate-inducible, major subunit
PRO_0000063222

Regions

Domain43 – 106644Fe-4S Mo/W bis-MGD-type

Sites

Metal binding501Iron-sulfur (4Fe-4S)
Metal binding531Iron-sulfur (4Fe-4S)
Metal binding571Iron-sulfur (4Fe-4S)
Metal binding921Iron-sulfur (4Fe-4S)
Metal binding1961Molybdenum

Amino acid modifications

Non-standard residue1961Selenocysteine

Experimental info

Sequence conflict961A → P Ref.1
Sequence conflict484 – 4918ANTPKATL → GEHAERRRW Ref.1
Sequence conflict9411S → A Ref.1

Secondary structure

......................................................................................................................................................................................... 1015
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24183 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: E4B9449D6B2407DA

FASTA1,015112,963
        10         20         30         40         50         60 
MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC TYCSVGCGLL 

        70         80         90        100        110        120 
MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD YVNSENRLRY PEYRAPGSDK 

       130        140        150        160        170        180 
WQRISWEEAF SRIAKLMKAD RDANFIEKNE QGVTVNRWLS TGMLCASGAS NETGMLTQKF 

       190        200        210        220        230        240 
ARSLGMLAVD NQARVUHGPT VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG 

       250        260        270        280        290        300 
FRWAMEAKNN NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE 

       310        320        330        340        350        360 
YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR DETLTHPRCV 

       370        380        390        400        410        420 
WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP DRTTTFLYAL GWTQHTVGAQ 

       430        440        450        460        470        480 
NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL STSLPGYLTL PSEKQVDLQS 

       490        500        510        520        530        540 
YLEANTPKAT LADQVNYWSN YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY 

       550        560        570        580        590        600 
FNMMDEGKVT GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN 

       610        620        630        640        650        660 
DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG EILAGIYHHL 

       670        680        690        700        710        720 
RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY ALEDLYDANG VLIAKKGQLL 

       730        740        750        760        770        780 
SSFAHLRDDG TTASSCWIYT GSWTEQGNQM ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN 

       790        800        810        820        830        840 
RASADINGKP WDPKRMLIQW NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK 

       850        860        870        880        890        900 
MAEGPFPEHY EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH 

       910        920        930        940        950        960 
FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV AVVTRRLKPL 

       970        980        990       1000       1010 
NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS QTPEYKAFLV NIEKA 

« Hide

References

« Hide 'large scale' references
[1]"Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine."
Berg B.L., Li J., Heider J., Stewart V.
J. Biol. Chem. 266:22380-22385(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SELENOCYSTEINE AT SEC-196.
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides."
Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G.
J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPORT VIA THE TAT-SYSTEM.
[6]"Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12."
Berg B.L., Stewart V.
Genetics 125:691-702(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12.
[7]"Molecular basis of proton motive force generation: structure of formate dehydrogenase-N."
Jormakka M., Tornroth S., Byrne B., Iwata S.
Science 295:1863-1868(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH BETA AND GAMMA SUBUNITS; [4FE-4S] CLUSTER AND MO-BIS-MGD, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ELECTRON TRANSFER CHAIN, SUBCELLULAR LOCATION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75029 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAD13438.1.
AP009048 Genomic DNA. Translation: BAA15123.1.
PIRJS0628. E64900.
RefSeqNP_415991.1. NC_000913.3.
YP_489739.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60A1-1015[»]
1KQGX-ray2.80A1-1015[»]
ProteinModelPortalP24183.
SMRP24183. Positions 34-1015.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9573N.
IntActP24183. 14 interactions.
MINTMINT-1236143.
STRING511145.b1474.

Protein family/group databases

TCDB5.A.3.2.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbP24183.
PRIDEP24183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD13438; AAD13438; b1474.
BAA15123; BAA15123; BAA15123.
GeneID12933906.
946035.
KEGGecj:Y75_p1450.
eco:b1474.
PATRIC32118240. VBIEscCol129921_1540.

Organism-specific databases

EchoBASEEB1209.
EcoGeneEG11227. fdnG.

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000163271.
KOK08348.
OMAIMQQEGL.
OrthoDBEOG6D8B5R.
PhylomeDBP24183.

Enzyme and pathway databases

BioCycEcoCyc:FDNG-MONOMER.
ECOL316407:JW1470-MONOMER.
MetaCyc:FDNG-MONOMER.

Gene expression databases

GenevestigatorP24183.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate_DH_asu_anaerob.
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]
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR01553. formate-DH-alph. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24183.
PROP24183.

Entry information

Entry nameFDNG_ECOLI
AccessionPrimary (citable) accession number: P24183
Secondary accession number(s): P78261
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 26, 2008
Last modified: June 11, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene