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P24183

- FDNG_ECOLI

UniProt

P24183 - FDNG_ECOLI

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
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    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

    Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.1 Publication
    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
    6. protein binding Source: IntAct

    GO - Biological processi

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

    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-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC     50
    TYCSVGCGLL MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD 100
    YVNSENRLRY PEYRAPGSDK WQRISWEEAF SRIAKLMKAD RDANFIEKNE 150
    QGVTVNRWLS TGMLCASGAS NETGMLTQKF ARSLGMLAVD NQARVUHGPT 200
    VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG FRWAMEAKNN 250
    NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE 300
    YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR 350
    DETLTHPRCV WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP 400
    DRTTTFLYAL GWTQHTVGAQ NIRTMAMIQL LLGNMGMAGG GVNALRGHSN 450
    IQGLTDLGLL STSLPGYLTL PSEKQVDLQS YLEANTPKAT LADQVNYWSN 500
    YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY FNMMDEGKVT 550
    GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN 600
    DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG 650
    EILAGIYHHL RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY 700
    ALEDLYDANG VLIAKKGQLL SSFAHLRDDG TTASSCWIYT GSWTEQGNQM 750
    ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN RASADINGKP WDPKRMLIQW 800
    NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK MAEGPFPEHY 850
    EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH 900
    FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV 950
    AVVTRRLKPL NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS 1000
    QTPEYKAFLV NIEKA 1015
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 148 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