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Q820V5

- FABI_ENTFA

UniProt

Q820V5 - FABI_ENTFA

Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene

fabI

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.By similarity

    Catalytic activityi

    An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

    Enzyme regulationi

    Inhibited by triclosan and its diphenyl ether analgues.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121NAD; via carbonyl oxygenBy similarity
    Binding sitei39 – 391NADBy similarity
    Binding sitei89 – 891NAD; via carbonyl oxygenBy similarity
    Binding sitei92 – 921Substrate; via amide nitrogen and carbonyl oxygenBy similarity
    Active sitei142 – 1421Proton acceptorBy similarity
    Active sitei152 – 1521Proton acceptorBy similarity
    Binding sitei159 – 1591NADBy similarity
    Sitei197 – 1971Involved in acyl-ACP bindingBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 192NADBy similarity
    Nucleotide bindingi61 – 622NADBy similarity
    Nucleotide bindingi188 – 1925NADBy similarity

    GO - Molecular functioni

    1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid elongation Source: UniProtKB
    2. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEFAE226185:GHI1-289-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
    Short name:
    ENR
    Alternative name(s):
    NADH-dependent enoyl-ACP reductase
    Gene namesi
    Name:fabI
    Ordered Locus Names:EF_0282
    OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
    Taxonomic identifieri226185 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
    ProteomesiUP000001415: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 250250Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000407977Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi226185.EF0282.

    Structurei

    3D structure databases

    ProteinModelPortaliQ820V5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0623.
    KOiK00208.
    OMAiCFATIKE.
    OrthoDBiEOG6HF644.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.

    Sequencei

    Sequence statusi: Complete.

    Q820V5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLQNKNVVV MGVANKKSIA WGCAKALKDQ GANVIYTYQN ERMKKQVVKL    50
    ADENDLLVEC DVASDASIQA AFETIKNEVG TIDGLVHAIA FAKKEELSGN 100
    VSDITRDGFL LAQDISSYSL LAVTHYAKPL LNPGSGIVTL TYLGSERAIP 150
    NYNMMGIAKA SLETAVKYLA FELAADKIRV NGISAGAIKT LAVTGVKDYD 200
    QLISISNERT PDKTGVTIEE VGNTCAFLVS DLASGVVGDI IYVDKGVHLT 250
    Length:250
    Mass (Da):26,767
    Last modified:June 1, 2003 - v1
    Checksum:iA0A4DA491D22F78E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016830 Genomic DNA. Translation: AAO80145.1.
    RefSeqiNP_814074.1. NC_004668.1.

    Genome annotation databases

    EnsemblBacteriaiAAO80145; AAO80145; EF_0282.
    GeneIDi1199200.
    KEGGiefa:EF0282.
    PATRICi21851013. VBIEntFae7065_0260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016830 Genomic DNA. Translation: AAO80145.1 .
    RefSeqi NP_814074.1. NC_004668.1.

    3D structure databases

    ProteinModelPortali Q820V5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226185.EF0282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO80145 ; AAO80145 ; EF_0282 .
    GeneIDi 1199200.
    KEGGi efa:EF0282.
    PATRICi 21851013. VBIEntFae7065_0260.

    Phylogenomic databases

    eggNOGi COG0623.
    KOi K00208.
    OMAi CFATIKE.
    OrthoDBi EOG6HF644.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci EFAE226185:GHI1-289-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    2. "Mechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureus."
      Xu H., Sullivan T.J., Sekiguchi J., Kirikae T., Ojima I., Stratton C.F., Mao W., Rock F.L., Alley M.R., Johnson F., Walker S.G., Tonge P.J.
      Biochemistry 47:4228-4236(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiFABI_ENTFA
    AccessioniPrimary (citable) accession number: Q820V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3