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Protein

Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL

Gene

fabL

Organism
Bacillus subtilis (strain 168)
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). It confers resistance to triclosan.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by triclosan.1 Publication

Kineticsi

  1. KM=16 µM for NADPH1 Publication

    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei89NAD1 Publication1
    Binding sitei141SubstrateBy similarity1
    Active sitei151Proton acceptor1
    Active sitei158Proton acceptor1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi10 – 17NADPBy similarity8
    Nucleotide bindingi13 – 16NAD1 Publication4
    Nucleotide bindingi36 – 38NAD1 Publication3
    Nucleotide bindingi62 – 63NAD1 Publication2
    Nucleotide bindingi187 – 189NAD1 Publication3

    GO - Molecular functioni

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

    GO - Biological processi

    • fatty acid elongation Source: UniProtKB
    • protein homotetramerization Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU08650-MONOMER.
    MetaCyc:BSU08650-MONOMER.
    BRENDAi1.3.1.10. 658.
    1.3.1.104. 658.
    1.3.1.39. 658.
    SABIO-RKP71079.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL (EC:1.3.1.104)
    Short name:
    ENR
    Alternative name(s):
    Enoyl-acyl carrier protein reductase III
    NADPH-dependent enoyl-ACP reductase
    Gene namesi
    Name:fabL
    Synonyms:yfhR, ygaA
    Ordered Locus Names:BSU08650
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene exhibit a 250-fold decrease in the triclosan MIC.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003770061 – 250Enoyl-[acyl-carrier-protein] reductase [NADPH] FabLAdd BLAST250

    Proteomic databases

    PaxDbiP71079.
    PRIDEiP71079.

    Expressioni

    Inductioni

    Expressed during exponential growth.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP71079. 1 interactor.
    MINTiMINT-8366743.
    STRINGi224308.Bsubs1_010100004793.

    Structurei

    Secondary structure

    1250
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Helixi15 – 26Combined sources12
    Beta strandi30 – 37Combined sources8
    Helixi39 – 50Combined sources12
    Turni51 – 53Combined sources3
    Beta strandi56 – 60Combined sources5
    Helixi66 – 80Combined sources15
    Beta strandi85 – 88Combined sources4
    Helixi98 – 100Combined sources3
    Helixi103 – 113Combined sources11
    Helixi115 – 129Combined sources15
    Turni130 – 132Combined sources3
    Beta strandi134 – 141Combined sources8
    Helixi142 – 144Combined sources3
    Helixi152 – 171Combined sources20
    Helixi173 – 175Combined sources3
    Beta strandi177 – 184Combined sources8
    Helixi190 – 194Combined sources5
    Helixi198 – 208Combined sources11
    Helixi217 – 227Combined sources11
    Turni231 – 234Combined sources4
    Beta strandi239 – 243Combined sources5
    Helixi246 – 248Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OICX-ray2.20A/D1-250[»]
    3OIDX-ray1.80A/B/C/D1-250[»]
    ProteinModelPortaliP71079.
    SMRiP71079.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP71079.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CAN. Bacteria.
    ENOG410XQEM. LUCA.
    InParanoidiP71079.
    KOiK10780.
    OMAiHSGQPFM.
    PhylomeDBiP71079.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P71079-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEQNKCALVT GSSRGVGKAA AIRLAENGYN IVINYARSKK AALETAEEIE
    60 70 80 90 100
    KLGVKVLVVK ANVGQPAKIK EMFQQIDETF GRLDVFVNNA ASGVLRPVME
    110 120 130 140 150
    LEETHWDWTM NINAKALLFC AQEAAKLMEK NGGGHIVSIS SLGSIRYLEN
    160 170 180 190 200
    YTTVGVSKAA LEALTRYLAV ELSPKQIIVN AVSGGAIDTD ALKHFPNRED
    210 220 230 240 250
    LLEDARQNTP AGRMVEIKDM VDTVEFLVSS KADMIRGQTI IVDGGRSLLV
    Length:250
    Mass (Da):27,178
    Last modified:February 1, 1997 - v1
    Checksum:i4314962C70E19C49
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85082 Genomic DNA. Translation: BAA24484.1.
    Z82044 Genomic DNA. Translation: CAB04808.1.
    AL009126 Genomic DNA. Translation: CAB12693.1.
    PIRiB69802.
    RefSeqiNP_388745.1. NC_000964.3.
    WP_003223262.1. NZ_JNCM01000032.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12693; CAB12693; BSU08650.
    GeneIDi939223.
    KEGGibsu:BSU08650.
    PATRICi18973382. VBIBacSub10457_0905.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85082 Genomic DNA. Translation: BAA24484.1.
    Z82044 Genomic DNA. Translation: CAB04808.1.
    AL009126 Genomic DNA. Translation: CAB12693.1.
    PIRiB69802.
    RefSeqiNP_388745.1. NC_000964.3.
    WP_003223262.1. NZ_JNCM01000032.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OICX-ray2.20A/D1-250[»]
    3OIDX-ray1.80A/B/C/D1-250[»]
    ProteinModelPortaliP71079.
    SMRiP71079.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP71079. 1 interactor.
    MINTiMINT-8366743.
    STRINGi224308.Bsubs1_010100004793.

    Proteomic databases

    PaxDbiP71079.
    PRIDEiP71079.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12693; CAB12693; BSU08650.
    GeneIDi939223.
    KEGGibsu:BSU08650.
    PATRICi18973382. VBIBacSub10457_0905.

    Phylogenomic databases

    eggNOGiENOG4105CAN. Bacteria.
    ENOG410XQEM. LUCA.
    InParanoidiP71079.
    KOiK10780.
    OMAiHSGQPFM.
    PhylomeDBiP71079.

    Enzyme and pathway databases

    UniPathwayiUPA00094.
    BioCyciBSUB:BSU08650-MONOMER.
    MetaCyc:BSU08650-MONOMER.
    BRENDAi1.3.1.10. 658.
    1.3.1.104. 658.
    1.3.1.39. 658.
    SABIO-RKP71079.

    Miscellaneous databases

    EvolutionaryTraceiP71079.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFABL_BACSU
    AccessioniPrimary (citable) accession number: P71079
    Secondary accession number(s): Q796Z2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: February 1, 1997
    Last modified: November 2, 2016
    This is version 121 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    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.