Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P07658

- FDHF_ECOLI

UniProt

P07658 - FDHF_ECOLI

Protein

Formate dehydrogenase H

Gene

fdhF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.

    Catalytic activityi

    Formate + NAD+ = CO2 + NADH.
    Formate + acceptor = CO2 + reduced acceptor.

    Cofactori

    Binds 1 4Fe-4S cluster per subunit.
    Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.

    Enzyme regulationi

    Inhibited by aerobic conditions.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi8 – 81Iron-sulfur (4Fe-4S)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi10 – 101Iron-sulfur (4Fe-4S)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi11 – 111Iron-sulfur (4Fe-4S)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi15 – 151Iron-sulfur (4Fe-4S)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi42 – 421Iron-sulfur (4Fe-4S)2 PublicationsPROSITE-ProRule annotation
    Active sitei44 – 441Electron donor/acceptor
    Binding sitei44 – 441Molybdopterin guanine dinucleotide 22 Publications
    Active sitei140 – 1401Proton donor/acceptor
    Metal bindingi140 – 1401Molybdenum
    Sitei141 – 1411Important for catalytic activity
    Binding sitei297 – 2971Molybdopterin guanine dinucleotide 2; via amide nitrogen2 Publications
    Binding sitei301 – 3011Molybdopterin guanine dinucleotide 12 Publications
    Sitei333 – 3331Important for catalytic activity
    Binding sitei335 – 3351Molybdopterin guanine dinucleotide 12 Publications
    Binding sitei445 – 4451Molybdopterin guanine dinucleotide 12 Publications
    Binding sitei478 – 4781Molybdopterin guanine dinucleotide 12 Publications
    Binding sitei588 – 5881Molybdopterin guanine dinucleotide 1; via amide nitrogen2 Publications
    Binding sitei654 – 6541Molybdopterin guanine dinucleotide 12 Publications
    Binding sitei655 – 6551Molybdopterin guanine dinucleotide 22 Publications
    Binding sitei678 – 6781Molybdopterin guanine dinucleotide 12 Publications
    Binding sitei679 – 6791Molybdopterin guanine dinucleotide 22 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. formate oxidation Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:FORMATEDEHYDROGH-MONOMER.
    ECOL316407:JW4040-MONOMER.
    MetaCyc:FORMATEDEHYDROGH-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenase H (EC:1.1.99.33, EC:1.2.1.2)
    Alternative name(s):
    Formate dehydrogenase-H subunit alpha
    Short name:
    FDH-H
    Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide
    Gene namesi
    Name:fdhF
    Ordered Locus Names:b4079, JW4040
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10285. fdhF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc
    2. membrane Source: RefGenome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 715715Formate dehydrogenase HPRO_0000063221Add
    BLAST

    Expressioni

    Inductioni

    By formate. Repressed by oxygen, nitrate, nitrite, and other electron acceptors.

    Gene expression databases

    GenevestigatoriP07658.

    Interactioni

    Subunit structurei

    Consists of two separable enzymatic activities: a formate dehydrogenase component (FDH-H) and hydrogenase-3.2 Publications

    Protein-protein interaction databases

    DIPiDIP-9572N.
    IntActiP07658. 7 interactions.
    STRINGi511145.b4079.

    Structurei

    Secondary structure

    1
    715
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi9 – 113
    Beta strandi16 – 227
    Beta strandi25 – 317
    Turni35 – 395
    Helixi43 – 475
    Helixi50 – 534
    Beta strandi57 – 593
    Beta strandi69 – 724
    Helixi80 – 9819
    Helixi100 – 1023
    Beta strandi103 – 1064
    Helixi114 – 12613
    Helixi137 – 1404
    Beta strandi143 – 1453
    Helixi148 – 1525
    Helixi161 – 1666
    Beta strandi168 – 1747
    Helixi177 – 1804
    Helixi182 – 19312
    Beta strandi197 – 2015
    Helixi207 – 2104
    Beta strandi213 – 2164
    Helixi223 – 23614
    Helixi242 – 2487
    Helixi252 – 2609
    Helixi265 – 2673
    Helixi268 – 2714
    Helixi275 – 28713
    Beta strandi288 – 2969
    Helixi299 – 3013
    Beta strandi302 – 3043
    Helixi305 – 31814
    Beta strandi322 – 3243
    Beta strandi328 – 3325
    Helixi338 – 3436
    Helixi352 – 3543
    Helixi360 – 36910
    Helixi383 – 3853
    Helixi386 – 3916
    Beta strandi397 – 4026
    Helixi405 – 4084
    Beta strandi409 – 4113
    Helixi412 – 42110
    Beta strandi422 – 43110
    Helixi434 – 4374
    Beta strandi440 – 4456
    Helixi448 – 4503
    Beta strandi453 – 4564
    Beta strandi460 – 4656
    Beta strandi472 – 4743
    Helixi478 – 48811
    Helixi498 – 50811
    Turni510 – 5145
    Helixi517 – 5204
    Turni521 – 5233
    Beta strandi526 – 5283
    Beta strandi541 – 5433
    Beta strandi553 – 5564
    Beta strandi571 – 5733
    Beta strandi575 – 5795
    Beta strandi583 – 5853
    Helixi592 – 5943
    Helixi596 – 5994
    Beta strandi607 – 6115
    Helixi612 – 6187
    Beta strandi625 – 6295
    Beta strandi634 – 64512
    Beta strandi649 – 6524
    Beta strandi657 – 6593
    Helixi661 – 6633
    Turni671 – 6733
    Beta strandi681 – 6877
    Helixi691 – 71323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AA6X-ray2.30A1-715[»]
    1FDIX-ray2.90A1-715[»]
    1FDOX-ray2.80A1-715[»]
    2IV2X-ray2.27X1-715[»]
    ProteinModelPortaliP07658.
    SMRiP07658. Positions 1-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07658.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 56564Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1123MGD 1 binding
    Regioni173 – 1808MGD 2 binding
    Regioni201 – 2044MGD 2 binding
    Regioni221 – 2233MGD 2 binding
    Regioni402 – 4109MGD 1 binding
    Regioni428 – 4292MGD 1 binding
    Regioni579 – 5813MGD 1 binding
    Regioni581 – 5877MGD 2 binding
    Regioni661 – 6622MGD 1 binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0243.
    HOGENOMiHOG000031440.
    KOiK00123.
    OMAiMHIDAFV.
    OrthoDBiEOG6CVV7G.
    PhylomeDBiP07658.

    Family and domain databases

    InterProiIPR009010. Asp_de-COase-like_dom.
    IPR006478. Formate_DH_asu.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR006655. Mopterin_OxRdtase_prok_CS.
    IPR027467. MopterinOxRdtase_cofactor_BS.
    [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.
    TIGRFAMsiTIGR01591. Fdh-alpha. 1 hit.
    PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
    PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
    PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07658-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD    50
    FINDTQILTP RLKTPMIRRQ RGGKLEPVSW DEALNYVAER LSAIKEKYGP 100
    DAIQTTGSSR GTGNETNYVM QKFARAVIGT NNVDCCARVU HGPSVAGLHQ 150
    SVGNGAMSNA INEIDNTDLV FVFGYNPADS HPIVANHVIN AKRNGAKIIV 200
    CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY DKAFVASRTE 250
    GFEEYRKIVE GYTPESVEDI TGVSASEIRQ AARMYAQAKS AAILWGMGVT 300
    QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT 350
    YPGYQYVKDP ANREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI 400
    MGEDPLQTDA ELSAVRKAFE DLELVIVQDI FMTKTASAAD VILPSTSWGE 450
    HEGVFTAADR GFQRFFKAVE PKWDLKTDWQ IISEIATRMG YPMHYNNTQE 500
    IWDELRHLCP DFYGATYEKM GELGFIQWPC RDTSDADQGT SYLFKEKFDT 550
    PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA 600
    LADEPGYAQI NTEDAKRLGI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI 650
    YMTYQWWIGA CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID 700
    EYNKLKTRLR EAALA 715
    Length:715
    Mass (Da):79,374
    Last modified:February 26, 2008 - v2
    Checksum:iC7C86F6F704A142D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191L → V in AAA23754. (PubMed:2941757)Curated

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei140 – 1401Selenocysteine1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13563 Genomic DNA. Translation: AAA23754.2.
    U00006 Genomic DNA. Translation: AAC43173.2.
    U00096 Genomic DNA. Translation: AAD13462.1.
    AP009048 Genomic DNA. Translation: BAE78081.1.
    PIRiA24145. DEECFS.
    RefSeqiNP_418503.1. NC_000913.3.
    YP_492222.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAD13462; AAD13462; b4079.
    BAE78081; BAE78081; BAE78081.
    GeneIDi12933956.
    948584.
    KEGGiecj:Y75_p3966.
    eco:b4079.
    PATRICi32123709. VBIEscCol129921_4203.

    Keywords - Coding sequence diversityi

    Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13563 Genomic DNA. Translation: AAA23754.2 .
    U00006 Genomic DNA. Translation: AAC43173.2 .
    U00096 Genomic DNA. Translation: AAD13462.1 .
    AP009048 Genomic DNA. Translation: BAE78081.1 .
    PIRi A24145. DEECFS.
    RefSeqi NP_418503.1. NC_000913.3.
    YP_492222.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AA6 X-ray 2.30 A 1-715 [» ]
    1FDI X-ray 2.90 A 1-715 [» ]
    1FDO X-ray 2.80 A 1-715 [» ]
    2IV2 X-ray 2.27 X 1-715 [» ]
    ProteinModelPortali P07658.
    SMRi P07658. Positions 1-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9572N.
    IntActi P07658. 7 interactions.
    STRINGi 511145.b4079.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD13462 ; AAD13462 ; b4079 .
    BAE78081 ; BAE78081 ; BAE78081 .
    GeneIDi 12933956.
    948584.
    KEGGi ecj:Y75_p3966.
    eco:b4079.
    PATRICi 32123709. VBIEscCol129921_4203.

    Organism-specific databases

    EchoBASEi EB0281.
    EcoGenei EG10285. fdhF.

    Phylogenomic databases

    eggNOGi COG0243.
    HOGENOMi HOG000031440.
    KOi K00123.
    OMAi MHIDAFV.
    OrthoDBi EOG6CVV7G.
    PhylomeDBi P07658.

    Enzyme and pathway databases

    BioCyci EcoCyc:FORMATEDEHYDROGH-MONOMER.
    ECOL316407:JW4040-MONOMER.
    MetaCyc:FORMATEDEHYDROGH-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P07658.
    PROi P07658.

    Gene expression databases

    Genevestigatori P07658.

    Family and domain databases

    InterProi IPR009010. Asp_de-COase-like_dom.
    IPR006478. Formate_DH_asu.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR006655. Mopterin_OxRdtase_prok_CS.
    IPR027467. MopterinOxRdtase_cofactor_BS.
    [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 TIGR01591. Fdh-alpha. 1 hit.
    PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
    PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
    PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli."
      Zinoni F., Birkmann A., Stadtman T.C., Boeck A.
      Proc. Natl. Acad. Sci. U.S.A. 83:4650-4654(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component."
      Axley M.J., Grahame D.A., Stadtman T.C.
      J. Biol. Chem. 265:18213-18218(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12, CHARACTERIZATION.
    6. "Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis."
      Gladyshev V.N., Boyington J.C., Khangulov S.V., Grahame D.A., Stadtman T.C., Sun P.D.
      J. Biol. Chem. 271:8095-8100(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, CRYSTALLIZATION.
    7. "Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer."
      Khangulov S.V., Gladyshev V.N., Dismukes G.C., Stadtman T.C.
      Biochemistry 37:3518-3528(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR.
    8. "Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster."
      Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D.
      Science 275:1305-1308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S); MOLYBDENUM ION AND MOLYBDOPTERIN, SELENOCYSTEINE AT SEC-140, COFACTOR, CATALYTIC ACTIVITY.
    9. "Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism."
      Raaijmakers H.C., Romao M.J.
      J. Biol. Inorg. Chem. 11:849-854(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND MOLYBDOPTERIN, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiFDHF_ECOLI
    AccessioniPrimary (citable) accession number: P07658
    Secondary accession number(s): P78137, Q2M6M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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