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P42593

- FADH_ECOLI

UniProt

P42593 - FADH_ECOLI

Protein

2,4-dienoyl-CoA reductase [NADPH]

Gene

fadH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-2- enoyl-CoA.

    Catalytic activityi

    Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi335 – 3351Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi338 – 3381Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi342 – 3421Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi354 – 3541Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 2,4-dienoyl-CoA reductase (NADPH) activity Source: EcoCyc
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. FMN binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:DIENOYLCOAREDUCT-MONOMER.
    ECOL316407:JW3052-MONOMER.
    MetaCyc:DIENOYLCOAREDUCT-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,4-dienoyl-CoA reductase [NADPH] (EC:1.3.1.34)
    Alternative name(s):
    2,4-dienoyl coenzyme A reductase
    Gene namesi
    Name:fadH
    Synonyms:ygjL
    Ordered Locus Names:b3081, JW3052
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12723. fadH.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 6726712,4-dienoyl-CoA reductase [NADPH]PRO_0000194482Add
    BLAST

    Proteomic databases

    PRIDEiP42593.

    Expressioni

    Gene expression databases

    GenevestigatoriP42593.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-9562N.
    IntActiP42593. 10 interactions.
    STRINGi511145.b3081.

    Structurei

    Secondary structure

    1
    672
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74
    Beta strandi16 – 238
    Helixi36 – 4914
    Beta strandi53 – 6412
    Helixi78 – 803
    Helixi81 – 9313
    Beta strandi98 – 1025
    Helixi106 – 1083
    Beta strandi109 – 1113
    Beta strandi115 – 1195
    Helixi134 – 15320
    Beta strandi157 – 1637
    Helixi168 – 1736
    Turni175 – 1773
    Beta strandi185 – 1873
    Helixi188 – 20619
    Beta strandi208 – 21912
    Helixi228 – 24114
    Beta strandi244 – 2507
    Beta strandi259 – 2613
    Turni266 – 2694
    Helixi270 – 2767
    Beta strandi284 – 2863
    Helixi293 – 3019
    Beta strandi306 – 3116
    Helixi313 – 3164
    Helixi320 – 3256
    Helixi329 – 3313
    Turni340 – 3423
    Helixi343 – 3475
    Turni358 – 3614
    Turni363 – 3653
    Beta strandi376 – 3805
    Helixi384 – 39411
    Turni395 – 3973
    Beta strandi399 – 40911
    Helixi413 – 4164
    Helixi425 – 43915
    Beta strandi442 – 4465
    Beta strandi451 – 4544
    Beta strandi457 – 4626
    Beta strandi466 – 4683
    Turni475 – 4773
    Beta strandi481 – 4833
    Helixi484 – 4885
    Beta strandi496 – 5016
    Helixi504 – 51411
    Helixi521 – 5233
    Helixi525 – 5317
    Helixi541 – 5433
    Beta strandi555 – 5617
    Turni568 – 5714
    Turni574 – 5763
    Helixi577 – 58610
    Beta strandi590 – 5923
    Beta strandi596 – 6016
    Beta strandi604 – 6096
    Beta strandi612 – 6165
    Beta strandi619 – 6235
    Beta strandi627 – 6293
    Helixi634 – 6385
    Turni639 – 6413
    Beta strandi644 – 6463
    Helixi648 – 6503
    Helixi658 – 67114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PS9X-ray2.20A2-672[»]
    ProteinModelPortaliP42593.
    SMRiP42593. Positions 2-672.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42593.

    Family & Domainsi

    Domaini

    The N-terminus may contain the FAD-binding domain whereas the NADPH-binding domain may be located in the C-terminus.

    Phylogenomic databases

    eggNOGiCOG1902.
    HOGENOMiHOG000237760.
    KOiK00219.
    OMAiIAEFCNE.
    OrthoDBiEOG6VF2ZQ.
    PhylomeDBiP42593.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR001155. OxRdtase_FMN_N.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    [Graphical view]
    PfamiPF00724. Oxidored_FMN. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.

    Sequencei

    Sequence statusi: Complete.

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

    P42593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYPSLFAPL DLGFTTLKNR VLMGSMHTGL EEYPDGAERL AAFYAERARH    50
    GVALIVSGGI APDLTGVGME GGAMLNDASQ IPHHRTITEA VHQEGGKIAL 100
    QILHTGRYSY QPHLVAPSAL QAPINRFVPH ELSHEEILQL IDNFARCAQL 150
    AREAGYDGVE VMGSEGYLIN EFLTLRTNQR SDQWGGDYRN RMRFAVEVVR 200
    AVRERVGNDF IIIYRLSMLD LVEDGGTFAE TVELAQAIEA AGATIINTGI 250
    GWHEARIPTI ATPVPRGAFS WVTRKLKGHV SLPLVTTNRI NDPQVADDIL 300
    SRGDADMVSM ARPFLADAEL LSKAQSGRAD EINTCIGCNQ ACLDQIFVGK 350
    VTSCLVNPRA CHETKMPILP AVQKKNLAVV GAGPAGLAFA INAAARGHQV 400
    TLFDAHSEIG GQFNIAKQIP GKEEFYETLR YYRRMIEVTG VTLKLNHTVT 450
    ADQLQAFDET ILASGIVPRT PPIDGIDHPK VLSYLDVLRD KAPVGNKVAI 500
    IGCGGIGFDT AMYLSQPGES TSQNIAGFCN EWGIDSSLQQ AGGLSPQGMQ 550
    IPRSPRQIVM LQRKASKPGQ GLGKTTGWIH RTTLLSRGVK MIPGVSYQKI 600
    DDDGLHVVIN GETQVLAVDN VVICAGQEPN RALAQPLIDS GKTVHLIGGC 650
    DVAMELDARR AIAQGTRLAL EI 672
    Length:672
    Mass (Da):72,678
    Last modified:January 23, 2007 - v3
    Checksum:iB26C7CAAACE760C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93405 Genomic DNA. Translation: AAB82738.1.
    U18997 Genomic DNA. Translation: AAA57882.1.
    U00096 Genomic DNA. Translation: AAC76116.1.
    AP009048 Genomic DNA. Translation: BAE77131.1.
    PIRiF65096.
    RefSeqiNP_417552.1. NC_000913.3.
    YP_491272.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76116; AAC76116; b3081.
    BAE77131; BAE77131; BAE77131.
    GeneIDi12932990.
    947594.
    KEGGiecj:Y75_p3006.
    eco:b3081.
    PATRICi32121580. VBIEscCol129921_3176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93405 Genomic DNA. Translation: AAB82738.1 .
    U18997 Genomic DNA. Translation: AAA57882.1 .
    U00096 Genomic DNA. Translation: AAC76116.1 .
    AP009048 Genomic DNA. Translation: BAE77131.1 .
    PIRi F65096.
    RefSeqi NP_417552.1. NC_000913.3.
    YP_491272.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PS9 X-ray 2.20 A 2-672 [» ]
    ProteinModelPortali P42593.
    SMRi P42593. Positions 2-672.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9562N.
    IntActi P42593. 10 interactions.
    STRINGi 511145.b3081.

    Proteomic databases

    PRIDEi P42593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76116 ; AAC76116 ; b3081 .
    BAE77131 ; BAE77131 ; BAE77131 .
    GeneIDi 12932990.
    947594.
    KEGGi ecj:Y75_p3006.
    eco:b3081.
    PATRICi 32121580. VBIEscCol129921_3176.

    Organism-specific databases

    EchoBASEi EB2582.
    EcoGenei EG12723. fadH.

    Phylogenomic databases

    eggNOGi COG1902.
    HOGENOMi HOG000237760.
    KOi K00219.
    OMAi IAEFCNE.
    OrthoDBi EOG6VF2ZQ.
    PhylomeDBi P42593.

    Enzyme and pathway databases

    BioCyci EcoCyc:DIENOYLCOAREDUCT-MONOMER.
    ECOL316407:JW3052-MONOMER.
    MetaCyc:DIENOYLCOAREDUCT-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P42593.
    PROi P42593.

    Gene expression databases

    Genevestigatori P42593.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR001155. OxRdtase_FMN_N.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    [Graphical view ]
    Pfami PF00724. Oxidored_FMN. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli."
      He X.-Y., Yang S.-Y., Schulz H.
      Eur. J. Biochem. 248:516-520(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.

    Entry informationi

    Entry nameiFADH_ECOLI
    AccessioniPrimary (citable) accession number: P42593
    Secondary accession number(s): Q2M9C5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 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, 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

    External Data

    Dasty 3