Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

    Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141NAD; via carbonyl oxygen1 Publication
    Binding sitei95 – 951NAD; via carbonyl oxygen1 Publication
    Binding sitei98 – 981Substrate; via amide nitrogen and carbonyl oxygenBy similarity
    Active sitei148 – 1481Proton acceptorBy similarity
    Active sitei158 – 1581Proton acceptor
    Binding sitei165 – 1651NAD1 Publication
    Sitei206 – 2061Involved in acyl-ACP bindingBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 212NAD1 Publication
    Nucleotide bindingi67 – 682NAD1 Publication
    Nucleotide bindingi194 – 1985NAD1 Publication

    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
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU11720. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 258258Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054895Add
    BLAST

    Proteomic databases

    PaxDbiP54616.

    Expressioni

    Inductioni

    By cold shock.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135Combined sources
    Helixi21 – 3111Combined sources
    Beta strandi35 – 428Combined sources
    Helixi43 – 453Combined sources
    Helixi46 – 549Combined sources
    Beta strandi56 – 583Combined sources
    Beta strandi62 – 654Combined sources
    Beta strandi69 – 713Combined sources
    Helixi72 – 8514Combined sources
    Beta strandi90 – 934Combined sources
    Helixi100 – 1034Combined sources
    Helixi107 – 1093Combined sources
    Helixi112 – 12211Combined sources
    Helixi124 – 13310Combined sources
    Helixi134 – 1363Combined sources
    Beta strandi141 – 1477Combined sources
    Helixi149 – 1513Combined sources
    Turni156 – 1583Combined sources
    Helixi159 – 17921Combined sources
    Helixi180 – 1823Combined sources
    Beta strandi184 – 1918Combined sources
    Helixi197 – 1993Combined sources
    Beta strandi202 – 2043Combined sources
    Helixi205 – 21511Combined sources
    Helixi224 – 23512Combined sources
    Helixi237 – 2393Combined sources
    Beta strandi246 – 2505Combined sources
    Helixi253 – 2553Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OIFX-ray2.60A/B/C/D1-258[»]
    3OIGX-ray1.25A1-258[»]
    ProteinModelPortaliP54616.
    SMRiP54616. Positions 1-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54616.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0623.
    InParanoidiP54616.
    KOiK00208.
    OMAiGILDMIH.
    OrthoDBiEOG6HF644.
    PhylomeDBiP54616.

    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.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201S → Q AA sequence (PubMed:8755892).Curated

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OIFX-ray2.60A/B/C/D1-258[»]
    3OIGX-ray1.25A1-258[»]
    ProteinModelPortaliP54616.
    SMRiP54616. Positions 1-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiP54616.
    ChEMBLiCHEMBL1075044.

    Proteomic databases

    PaxDbiP54616.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU11720. [Micado]

    Phylogenomic databases

    eggNOGiCOG0623.
    InParanoidiP54616.
    KOiK00208.
    OMAiGILDMIH.
    OrthoDBiEOG6HF644.
    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.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
    PRINTSiPR00081. GDHRDH.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Cold shock stress-induced proteins in Bacillus subtilis."
      Graumann P., Schroeder K., Schmid R., Marahiel M.A.
      J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21, INDUCTION.
      Strain: 168 / JH642.
    3. "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
      Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
      Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-15.
      Strain: 168 / IS58.
    4. "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis."
      Heath R.J., Su N., Murphy C.K., Rock C.O.
      J. Biol. Chem. 275:40128-40133(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ENOYL-ACP REDUCTASE AND IN FATTY ACID BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    5. "Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis."
      Kim K.H., Ha B.H., Kim S.J., Hong S.K., Hwang K.Y., Kim E.E.
      J. Mol. Biol. 406:403-415(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.

    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: June 24, 2015
    This is version 118 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

    External Data

    Dasty 3

    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 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.