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Protein

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

Gene

fabI

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). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by triclosan and acrylamide.2 Publications

Kineticsi

  1. KM=7 µM for NADH1 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 sitei14NAD; via carbonyl oxygen1 Publication1
    Binding sitei95NAD; via carbonyl oxygen1 Publication1
    Binding sitei98Substrate; via amide nitrogen and carbonyl oxygenBy similarity1
    Active sitei148Proton acceptorBy similarity1
    Active sitei158Proton acceptor1
    Binding sitei165NAD1 Publication1
    Sitei206Involved in acyl-ACP bindingBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi20 – 21NAD1 Publication2
    Nucleotide bindingi67 – 68NAD1 Publication2
    Nucleotide bindingi194 – 198NAD1 Publication5

    GO - Molecular functioni

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

    GO - Biological processi

    • cellular response to cold Source: UniProtKB
    • 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, Stress response

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU11720-MONOMER.
    BRENDAi1.3.1.9. 658.
    SABIO-RKP54616.
    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):
    Cold shock-induced protein 15
    Short name:
    CSI15
    NADH-dependent enoyl-ACP reductase
    Vegetative protein 241
    Short name:
    VEG241
    Gene namesi
    Name:fabI
    Synonyms:yjbW
    Ordered Locus Names:BSU11720
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1075044.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000548951 – 258Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST258

    Proteomic databases

    PaxDbiP54616.

    Expressioni

    Inductioni

    By cold shock.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP54616. 1 interactor.
    MINTiMINT-8366040.
    STRINGi224308.Bsubs1_010100006476.

    Chemistry databases

    BindingDBiP54616.

    Structurei

    Secondary structure

    1258
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi9 – 13Combined sources5
    Helixi21 – 31Combined sources11
    Beta strandi35 – 42Combined sources8
    Helixi43 – 45Combined sources3
    Helixi46 – 54Combined sources9
    Beta strandi56 – 58Combined sources3
    Beta strandi62 – 65Combined sources4
    Beta strandi69 – 71Combined sources3
    Helixi72 – 85Combined sources14
    Beta strandi90 – 93Combined sources4
    Helixi100 – 103Combined sources4
    Helixi107 – 109Combined sources3
    Helixi112 – 122Combined sources11
    Helixi124 – 133Combined sources10
    Helixi134 – 136Combined sources3
    Beta strandi141 – 147Combined sources7
    Helixi149 – 151Combined sources3
    Turni156 – 158Combined sources3
    Helixi159 – 179Combined sources21
    Helixi180 – 182Combined sources3
    Beta strandi184 – 191Combined sources8
    Helixi197 – 199Combined sources3
    Beta strandi202 – 204Combined sources3
    Helixi205 – 215Combined sources11
    Helixi224 – 235Combined sources12
    Helixi237 – 239Combined sources3
    Beta strandi246 – 250Combined sources5
    Helixi253 – 255Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OIFX-ray2.60A/B/C/D1-258[»]
    3OIGX-ray1.25A1-258[»]
    ProteinModelPortaliP54616.
    SMRiP54616.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54616.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CSJ. Bacteria.
    COG0623. LUCA.
    InParanoidiP54616.
    KOiK00208.
    OMAiAGYCING.
    PhylomeDBiP54616.

    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.

    P54616-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH
    60 70 80 90 100
    ELAGTLDRND SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK
    110 120 130 140 150
    EELVGEYLNT NRDGFLLAHN ISSYSLTAVV KAARPMMTEG GSIVTLTYLG
    160 170 180 190 200
    GELVMPNYNV MGVAKASLDA SVKYLAADLG KENIRVNSIS AGPIRTLSAK
    210 220 230 240 250
    GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR GITGENLHVD

    SGFHITAR
    Length:258
    Mass (Da):27,874
    Last modified:May 30, 2000 - v2
    Checksum:i097667168B3F0470
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti20S → Q AA sequence (PubMed:8755892).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13029.2.
    PIRiG69845.
    RefSeqiNP_389054.2. NC_000964.3.
    WP_003232896.1. NZ_JNCM01000035.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13029; CAB13029; BSU11720.
    GeneIDi939379.
    KEGGibsu:BSU11720.
    PATRICi18974061. VBIBacSub10457_1224.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13029.2.
    PIRiG69845.
    RefSeqiNP_389054.2. NC_000964.3.
    WP_003232896.1. NZ_JNCM01000035.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3OIFX-ray2.60A/B/C/D1-258[»]
    3OIGX-ray1.25A1-258[»]
    ProteinModelPortaliP54616.
    SMRiP54616.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP54616. 1 interactor.
    MINTiMINT-8366040.
    STRINGi224308.Bsubs1_010100006476.

    Chemistry databases

    BindingDBiP54616.
    ChEMBLiCHEMBL1075044.

    Proteomic databases

    PaxDbiP54616.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB13029; CAB13029; BSU11720.
    GeneIDi939379.
    KEGGibsu:BSU11720.
    PATRICi18974061. VBIBacSub10457_1224.

    Phylogenomic databases

    eggNOGiENOG4105CSJ. Bacteria.
    COG0623. LUCA.
    InParanoidiP54616.
    KOiK00208.
    OMAiAGYCING.
    PhylomeDBiP54616.

    Enzyme and pathway databases

    UniPathwayiUPA00094.
    BioCyciBSUB:BSU11720-MONOMER.
    BRENDAi1.3.1.9. 658.
    SABIO-RKP54616.

    Miscellaneous databases

    EvolutionaryTraceiP54616.

    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_BACSU
    AccessioniPrimary (citable) accession number: P54616
    Secondary accession number(s): O31621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: November 2, 2016
    This is version 127 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. 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.