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P54616

- FABI_BACSU

UniProt

P54616 - FABI_BACSU

Protein

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

Gene

fabI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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.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

    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

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

    GO - Biological processi

    1. cellular response to cold Source: UniProtKB
    2. fatty acid elongation Source: UniProtKB
    3. protein homotetramerization Source: UniProtKB

    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.
    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: 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.BSU11720.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00208.
    OMAiTGEIHHV.
    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

    MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH    50
    ELAGTLDRND SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK 100
    EELVGEYLNT NRDGFLLAHN ISSYSLTAVV KAARPMMTEG GSIVTLTYLG 150
    GELVMPNYNV MGVAKASLDA SVKYLAADLG KENIRVNSIS AGPIRTLSAK 200
    GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR GITGENLHVD 250
    SGFHITAR 258
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13029.2.
    PIRiG69845.
    RefSeqiNP_389054.2. NC_000964.3.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13029.2 .
    PIRi G69845.
    RefSeqi NP_389054.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OIF X-ray 2.60 A/B/C/D 1-258 [» ]
    3OIG X-ray 1.25 A 1-258 [» ]
    ProteinModelPortali P54616.
    SMRi P54616. Positions 1-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P54616. 1 interaction.
    MINTi MINT-8366040.
    STRINGi 224308.BSU11720.

    Chemistry

    ChEMBLi CHEMBL1075044.

    Proteomic databases

    PaxDbi P54616.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13029 ; CAB13029 ; BSU11720 .
    GeneIDi 939379.
    KEGGi bsu:BSU11720.
    PATRICi 18974061. VBIBacSub10457_1224.

    Organism-specific databases

    GenoListi BSU11720. [Micado ]

    Phylogenomic databases

    eggNOGi COG0623.
    KOi K00208.
    OMAi TGEIHHV.
    OrthoDBi EOG6HF644.
    PhylomeDBi P54616.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci BSUB:BSU11720-MONOMER.
    SABIO-RK P54616.

    Miscellaneous databases

    EvolutionaryTracei P54616.

    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. "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: October 1, 2014
    This is version 112 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