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P24183

- FDNG_ECOLI

UniProt

P24183 - FDNG_ECOLI

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Protein

Formate dehydrogenase, nitrate-inducible, major subunit

Gene

fdnG

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Iron-sulfur (4Fe-4S)
Metal bindingi53 – 531Iron-sulfur (4Fe-4S)
Metal bindingi57 – 571Iron-sulfur (4Fe-4S)
Metal bindingi92 – 921Iron-sulfur (4Fe-4S)
Metal bindingi196 – 1961Molybdenum

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: EcoCyc
  3. formate dehydrogenase (NAD+) activity Source: EcoCyc
  4. formate dehydrogenase (quinone) activity Source: UniProtKB-EC
  5. molybdenum ion binding Source: EcoCyc

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. cellular respiration 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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11227. fdnG.

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. formate dehydrogenase complex Source: EcoCyc
  3. membrane Source: UniProtKB
  4. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Tat-type signalPROSITE-ProRule annotationAdd
BLAST
Chaini34 – 1015982Formate dehydrogenase, nitrate-inducible, major subunitPRO_0000063222Add
BLAST

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

Gene expression databases

GenevestigatoriP24183.

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

DIPiDIP-9573N.
IntActiP24183. 14 interactions.
MINTiMINT-1236143.
STRINGi511145.b1474.

Structurei

Secondary structure

1
1015
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni39 – 424Combined sources
Beta strandi43 – 497Combined sources
Beta strandi51 – 533Combined sources
Beta strandi58 – 658Combined sources
Beta strandi74 – 807Combined sources
Turni85 – 895Combined sources
Helixi93 – 964Combined sources
Helixi99 – 1024Combined sources
Beta strandi112 – 1143Combined sources
Helixi126 – 14419Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi160 – 1645Combined sources
Helixi171 – 18313Combined sources
Beta strandi189 – 1913Combined sources
Helixi192 – 1954Combined sources
Helixi198 – 20811Combined sources
Helixi218 – 2225Combined sources
Beta strandi224 – 2307Combined sources
Helixi233 – 2364Combined sources
Turni238 – 2414Combined sources
Helixi242 – 2509Combined sources
Beta strandi254 – 2585Combined sources
Helixi264 – 2674Combined sources
Beta strandi270 – 2734Combined sources
Helixi280 – 29314Combined sources
Helixi299 – 3057Combined sources
Beta strandi310 – 3123Combined sources
Turni328 – 3314Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi346 – 3483Combined sources
Helixi360 – 3689Combined sources
Helixi373 – 3808Combined sources
Helixi384 – 39512Combined sources
Helixi396 – 3983Combined sources
Beta strandi404 – 4096Combined sources
Helixi410 – 4134Combined sources
Helixi418 – 43114Combined sources
Beta strandi441 – 4444Combined sources
Helixi451 – 4566Combined sources
Helixi465 – 4673Combined sources
Helixi478 – 4858Combined sources
Beta strandi490 – 4934Combined sources
Helixi497 – 5004Combined sources
Helixi501 – 51313Combined sources
Helixi514 – 5163Combined sources
Helixi519 – 5279Combined sources
Beta strandi531 – 5333Combined sources
Helixi537 – 5459Combined sources
Beta strandi551 – 5566Combined sources
Helixi559 – 5624Combined sources
Beta strandi563 – 5653Combined sources
Helixi566 – 5738Combined sources
Beta strandi577 – 5859Combined sources
Turni588 – 5936Combined sources
Helixi597 – 6004Combined sources
Helixi604 – 6063Combined sources
Beta strandi610 – 6167Combined sources
Helixi619 – 6213Combined sources
Beta strandi624 – 6274Combined sources
Beta strandi632 – 6365Combined sources
Helixi649 – 66719Combined sources
Helixi672 – 6776Combined sources
Helixi690 – 6989Combined sources
Beta strandi700 – 7034Combined sources
Beta strandi712 – 7143Combined sources
Helixi723 – 7253Combined sources
Beta strandi728 – 7336Combined sources
Helixi737 – 7393Combined sources
Beta strandi742 – 7443Combined sources
Helixi749 – 7513Combined sources
Beta strandi760 – 7623Combined sources
Beta strandi767 – 7704Combined sources
Turni771 – 7744Combined sources
Helixi780 – 7834Combined sources
Beta strandi790 – 7923Combined sources
Helixi793 – 7953Combined sources
Beta strandi798 – 8003Combined sources
Beta strandi802 – 8098Combined sources
Beta strandi831 – 8333Combined sources
Beta strandi856 – 8594Combined sources
Helixi876 – 8794Combined sources
Turni885 – 8873Combined sources
Beta strandi890 – 8956Combined sources
Turni902 – 9043Combined sources
Helixi905 – 9073Combined sources
Helixi909 – 9146Combined sources
Beta strandi919 – 9224Combined sources
Helixi924 – 9307Combined sources
Beta strandi937 – 9415Combined sources
Beta strandi946 – 9538Combined sources
Beta strandi960 – 9623Combined sources
Beta strandi965 – 9673Combined sources
Beta strandi969 – 9735Combined sources
Beta strandi978 – 9825Combined sources
Helixi988 – 9903Combined sources
Turni998 – 10003Combined sources
Beta strandi1007 – 10148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQFX-ray1.60A1-1015[»]
1KQGX-ray2.80A1-1015[»]
ProteinModelPortaliP24183.
SMRiP24183. Positions 34-1015.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24183.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 106644Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000163271.
InParanoidiP24183.
KOiK08348.
OMAiIMQQEGL.
OrthoDBiEOG6D8B5R.
PhylomeDBiP24183.

Family and domain databases

InterProiIPR009010. 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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961A → P(PubMed:1834669)Curated
Sequence conflicti484 – 4918ANTPKATL → GEHAERRRW(PubMed:1834669)Curated
Sequence conflicti941 – 9411S → A(PubMed:1834669)Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei196 – 1961Selenocysteine

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.
YP_489739.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAD13438; AAD13438; b1474.
BAA15123; BAA15123; BAA15123.
GeneIDi12933906.
946035.
KEGGiecj:Y75_p1450.
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 .
PIRi E64900. JS0628.
RefSeqi NP_415991.1. NC_000913.3.
YP_489739.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KQF X-ray 1.60 A 1-1015 [» ]
1KQG X-ray 2.80 A 1-1015 [» ]
ProteinModelPortali P24183.
SMRi P24183. Positions 34-1015.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9573N.
IntActi P24183. 14 interactions.
MINTi MINT-1236143.
STRINGi 511145.b1474.

Protein family/group databases

TCDBi 5.A.3.2.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbi P24183.
PRIDEi P24183.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD13438 ; AAD13438 ; b1474 .
BAA15123 ; BAA15123 ; BAA15123 .
GeneIDi 12933906.
946035.
KEGGi ecj:Y75_p1450.
eco:b1474.
PATRICi 32118240. VBIEscCol129921_1540.

Organism-specific databases

EchoBASEi EB1209.
EcoGenei EG11227. fdnG.

Phylogenomic databases

eggNOGi COG0243.
HOGENOMi HOG000163271.
InParanoidi P24183.
KOi K08348.
OMAi IMQQEGL.
OrthoDBi EOG6D8B5R.
PhylomeDBi P24183.

Enzyme and pathway databases

BioCyci EcoCyc:FDNG-MONOMER.
ECOL316407:JW1470-MONOMER.
MetaCyc:FDNG-MONOMER.

Miscellaneous databases

EvolutionaryTracei P24183.
PROi P24183.

Gene expression databases

Genevestigatori P24183.

Family and domain databases

InterProi IPR009010. 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 ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01553. formate-DH-alph. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

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 26, 2014
This is version 150 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

External Data

Dasty 3