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Protein

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

Gene

fabI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 and in the biotin biosynthesis.3 Publications

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.1 Publication

Enzyme regulationi

Inhibited by diazaborines, triclosan (5-chloro-2-2,4-dichlorophenoxyphenol), 1,4-disubstituted imidazoles, 1,4-benzodiazepine derivatives, naphthyridinone derivatives, luteolin and curcumin.9 Publications

Kineticsi

  1. KM=3.3 µM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius and pH 8)2 Publications
  2. KM=22 µM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5)2 Publications
  3. KM=24 µM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius and pH 8)2 Publications
  4. KM=2700 µM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5)2 Publications

    Pathwayi: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Pathwayi: biotin biosynthesis

    This protein is involved in the pathway biotin biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway biotin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei13NAD; via carbonyl oxygen8 Publications1
    Binding sitei40NAD8 Publications1
    Binding sitei92NAD; via carbonyl oxygen8 Publications1
    Binding sitei95Substrate; via amide nitrogen and carbonyl oxygen1
    Active sitei146Proton acceptorBy similarity1
    Active sitei156Proton acceptorBy similarity1
    Binding sitei163NAD8 Publications1
    Sitei201Involved in acyl-ACP binding1
    Sitei204Involved in acyl-ACP binding1
    Sitei205Involved in acyl-ACP binding1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi19 – 20NAD8 Publications2
    Nucleotide bindingi64 – 65NAD8 Publications2
    Nucleotide bindingi192 – 196NAD8 Publications5

    GO - Molecular functioni

    • enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • biotin biosynthetic process Source: UniProtKB
    • fatty acid elongation Source: UniProtKB
    • lipid biosynthetic process Source: EcoCyc
    • protein homotetramerization Source: UniProtKB
    • response to antibiotic Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    ECOL316407:JW1281-MONOMER.
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    BRENDAi1.3.1.9. 2026.
    SABIO-RKP0AEK4.
    UniPathwayiUPA00078.
    UPA00094.

    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
    Synonyms:envM
    Ordered Locus Names:b1288, JW1281
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11528. fabI.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi93G → S: Diazaborine resistance. 2 Publications1
    Mutagenesisi93G → V: Triclosan resistance. 2 Publications1
    Mutagenesisi146Y → F: Large impact on catalysis, with kcat and kcat/Km for DD-ACP decreasing by around 50-fold compared with wild-type. 1 Publication1
    Mutagenesisi156Y → F: No effect on substrate reduction. 1 Publication1
    Mutagenesisi159M → T: Triclosan resistance. 1 Publication1
    Mutagenesisi201K → A: No effect on substrate reduction. 1 Publication1
    Mutagenesisi201K → E: Little activity toward DD-CoA and DD-ACP. 1 Publication1
    Mutagenesisi203F → L: Triclosan resistance. 1 Publication1
    Mutagenesisi204R → A: No effect on substrate reduction. 1 Publication1
    Mutagenesisi204R → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. 1 Publication1
    Mutagenesisi205K → A: No effect on substrate reduction. 1 Publication1
    Mutagenesisi205K → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. Has a larger impact on substrate reduction. 1 Publication1
    Mutagenesisi241S → F: Produces temperature-sensitive phenotype. 1

    Chemistry databases

    ChEMBLiCHEMBL1857.
    DrugBankiDB08604. Triclosan.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved3 Publications
    ChainiPRO_00000548992 – 262Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST261

    Proteomic databases

    EPDiP0AEK4.
    PaxDbiP0AEK4.
    PRIDEiP0AEK4.

    2D gel databases

    SWISS-2DPAGEP0AEK4.

    Interactioni

    Subunit structurei

    Homotetramer.8 Publications

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260135. 284 interactors.
    DIPiDIP-31867N.
    IntActiP0AEK4. 12 interactors.
    MINTiMINT-1251203.
    STRINGi511145.b1288.

    Chemistry databases

    BindingDBiP0AEK4.

    Structurei

    Secondary structure

    1262
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni3 – 6Combined sources4
    Beta strandi8 – 11Combined sources4
    Beta strandi16 – 19Combined sources4
    Helixi20 – 30Combined sources11
    Beta strandi34 – 41Combined sources8
    Turni42 – 44Combined sources3
    Helixi45 – 54Combined sources10
    Beta strandi60 – 62Combined sources3
    Helixi68 – 79Combined sources12
    Beta strandi83 – 90Combined sources8
    Helixi97 – 100Combined sources4
    Beta strandi101 – 103Combined sources3
    Helixi104 – 107Combined sources4
    Helixi110 – 120Combined sources11
    Helixi122 – 131Combined sources10
    Helixi132 – 134Combined sources3
    Beta strandi135 – 145Combined sources11
    Helixi147 – 149Combined sources3
    Turni154 – 157Combined sources4
    Helixi158 – 177Combined sources20
    Turni178 – 181Combined sources4
    Beta strandi182 – 189Combined sources8
    Helixi197 – 199Combined sources3
    Beta strandi200 – 202Combined sources3
    Helixi203 – 213Combined sources11
    Helixi222 – 232Combined sources11
    Helixi235 – 237Combined sources3
    Beta strandi244 – 248Combined sources5
    Helixi251 – 253Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1C14X-ray2.00A/B1-262[»]
    1D8AX-ray2.20A/B2-262[»]
    1DFGX-ray2.50A/B2-262[»]
    1DFHX-ray2.20A/B2-262[»]
    1DFIX-ray2.09A/B/C/D2-262[»]
    1I2ZX-ray2.80A/B1-262[»]
    1I30X-ray2.40A/B1-262[»]
    1LX6X-ray2.40A/B1-262[»]
    1LXCX-ray2.40A/B1-262[»]
    1MFPX-ray2.33A/B1-262[»]
    1QG6X-ray1.90A/B/C/D2-262[»]
    1QSGX-ray1.75A/B/C/D/E/F/G/H1-262[»]
    2FHSX-ray2.70A/B1-262[»]
    3PJDX-ray2.50A/B1-262[»]
    3PJEX-ray2.50A/B1-262[»]
    3PJFX-ray1.90A/B1-262[»]
    4JQCX-ray2.80A/B1-262[»]
    4JX8X-ray3.20A/B1-262[»]
    5CFZX-ray1.97A/B1-262[»]
    5CG1X-ray2.07A/B1-262[»]
    5CG2X-ray2.11A/B1-262[»]
    ProteinModelPortaliP0AEK4.
    SMRiP0AEK4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CSJ. Bacteria.
    COG0623. LUCA.
    InParanoidiP0AEK4.
    KOiK00208.
    OMAiSACKREG.
    PhylomeDBiP0AEK4.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR016040. NAD(P)-bd_dom.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PTHR24322:SF317. PTHR24322:SF317. 2 hits.
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0AEK4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE
    60 70 80 90 100
    FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL
    110 120 130 140 150
    DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE
    160 170 180 190 200
    RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI
    210 220 230 240 250
    KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG
    260
    FSIAAMNELE LK
    Length:262
    Mass (Da):27,864
    Last modified:January 23, 2007 - v2
    Checksum:i436A89AF349D1866
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M97219 Unassigned DNA. Translation: AAA17755.1.
    X78733 Genomic DNA. Translation: CAA55381.1.
    U00096 Genomic DNA. Translation: AAC74370.1.
    AP009048 Genomic DNA. Translation: BAA14841.1.
    PIRiS48029.
    RefSeqiNP_415804.1. NC_000913.3.
    WP_000506490.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74370; AAC74370; b1288.
    BAA14841; BAA14841; BAA14841.
    GeneIDi945870.
    KEGGiecj:JW1281.
    eco:b1288.
    PATRICi32117844. VBIEscCol129921_1342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M97219 Unassigned DNA. Translation: AAA17755.1.
    X78733 Genomic DNA. Translation: CAA55381.1.
    U00096 Genomic DNA. Translation: AAC74370.1.
    AP009048 Genomic DNA. Translation: BAA14841.1.
    PIRiS48029.
    RefSeqiNP_415804.1. NC_000913.3.
    WP_000506490.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1C14X-ray2.00A/B1-262[»]
    1D8AX-ray2.20A/B2-262[»]
    1DFGX-ray2.50A/B2-262[»]
    1DFHX-ray2.20A/B2-262[»]
    1DFIX-ray2.09A/B/C/D2-262[»]
    1I2ZX-ray2.80A/B1-262[»]
    1I30X-ray2.40A/B1-262[»]
    1LX6X-ray2.40A/B1-262[»]
    1LXCX-ray2.40A/B1-262[»]
    1MFPX-ray2.33A/B1-262[»]
    1QG6X-ray1.90A/B/C/D2-262[»]
    1QSGX-ray1.75A/B/C/D/E/F/G/H1-262[»]
    2FHSX-ray2.70A/B1-262[»]
    3PJDX-ray2.50A/B1-262[»]
    3PJEX-ray2.50A/B1-262[»]
    3PJFX-ray1.90A/B1-262[»]
    4JQCX-ray2.80A/B1-262[»]
    4JX8X-ray3.20A/B1-262[»]
    5CFZX-ray1.97A/B1-262[»]
    5CG1X-ray2.07A/B1-262[»]
    5CG2X-ray2.11A/B1-262[»]
    ProteinModelPortaliP0AEK4.
    SMRiP0AEK4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260135. 284 interactors.
    DIPiDIP-31867N.
    IntActiP0AEK4. 12 interactors.
    MINTiMINT-1251203.
    STRINGi511145.b1288.

    Chemistry databases

    BindingDBiP0AEK4.
    ChEMBLiCHEMBL1857.
    DrugBankiDB08604. Triclosan.

    2D gel databases

    SWISS-2DPAGEP0AEK4.

    Proteomic databases

    EPDiP0AEK4.
    PaxDbiP0AEK4.
    PRIDEiP0AEK4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74370; AAC74370; b1288.
    BAA14841; BAA14841; BAA14841.
    GeneIDi945870.
    KEGGiecj:JW1281.
    eco:b1288.
    PATRICi32117844. VBIEscCol129921_1342.

    Organism-specific databases

    EchoBASEiEB1490.
    EcoGeneiEG11528. fabI.

    Phylogenomic databases

    eggNOGiENOG4105CSJ. Bacteria.
    COG0623. LUCA.
    InParanoidiP0AEK4.
    KOiK00208.
    OMAiSACKREG.
    PhylomeDBiP0AEK4.

    Enzyme and pathway databases

    UniPathwayiUPA00078.
    UPA00094.
    BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    ECOL316407:JW1281-MONOMER.
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
    BRENDAi1.3.1.9. 2026.
    SABIO-RKP0AEK4.

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4.
    PROiP0AEK4.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR016040. NAD(P)-bd_dom.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PTHR24322:SF317. PTHR24322:SF317. 2 hits.
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFABI_ECOLI
    AccessioniPrimary (citable) accession number: P0AEK4
    Secondary accession number(s): P29132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The antibiotic diazaborine interferes with the activity by binding to the protein and NAD.

    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.