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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei13NAD; via carbonyl oxygen8 Publications1
    Binding sitei40NAD8 Publications1
    Binding sitei92NAD; via carbonyl oxygen8 Publications1
    Binding sitei95Substrate; via amide nitrogen and carbonyl oxygen1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei146Proton acceptorBy similarity1
    Active sitei156Proton acceptorBy similarity1
    Binding sitei163NAD8 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei201Involved in acyl-ACP binding1
    Sitei204Involved in acyl-ACP binding1
    Sitei205Involved in acyl-ACP binding1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi19 – 20NAD8 Publications2
    Nucleotide bindingi64 – 65NAD8 Publications2
    Nucleotide bindingi192 – 196NAD8 Publications5

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    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

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processAntibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.3.1.9 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0AEK4

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00078

    UPA00094

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001775

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:fabI
    Synonyms:envM
    Ordered Locus Names:b1288, JW1281
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG11528 fabI

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1857

    Drug and drug target database

    More...
    DrugBanki
    DB01865 3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide
    DB03534 3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide
    DB03030 4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole
    DB02379 Beta-D-Glucose
    DB01691 Indole Naphthyridinone
    DB08604 Triclosan

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved3 Publications
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000548992 – 262Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST261

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0AEK4

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0AEK4

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AEK4

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0AEK4

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.8 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    rraBP0AF902EBI-370029,EBI-544031

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260135, 290 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-31867N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AEK4, 12 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_1405

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P0AEK4

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1262
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0AEK4

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0AEK4

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AEK4

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CSJ Bacteria
    COG0623 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AEK4

    KEGG Orthology (KO)

    More...
    KOi
    K00208

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AEK4

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR014358 Enoyl-ACP_Rdtase_NADH
    IPR036291 NAD(P)-bd_dom_sf
    IPR002347 SDR_fam

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43159:SF2 PTHR43159:SF2, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000094 Enoyl-ACP_rdct, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00081 GDHRDH

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i436A89AF349D1866
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S48029

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415804.1, NC_000913.3
    WP_000506490.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74370; AAC74370; b1288
    BAA14841; BAA14841; BAA14841

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945870

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1281
    eco:b1288

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.991

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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, 290 interactors
    DIPiDIP-31867N
    IntActiP0AEK4, 12 interactors
    STRINGi316385.ECDH10B_1405

    Chemistry databases

    BindingDBiP0AEK4
    ChEMBLiCHEMBL1857
    DrugBankiDB01865 3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide
    DB03534 3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide
    DB03030 4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole
    DB02379 Beta-D-Glucose
    DB01691 Indole Naphthyridinone
    DB08604 Triclosan
    SwissLipidsiSLP:000001775

    2D gel databases

    SWISS-2DPAGEiP0AEK4

    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
    PATRICifig|1411691.4.peg.991

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

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    EchoBASEi
    EB1490
    EcoGeneiEG11528 fabI

    Phylogenomic databases

    eggNOGiENOG4105CSJ Bacteria
    COG0623 LUCA
    InParanoidiP0AEK4
    KOiK00208
    PhylomeDBiP0AEK4

    Enzyme and pathway databases

    UniPathwayi
    UPA00078

    UPA00094

    BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER
    MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER
    BRENDAi1.3.1.9 2026
    SABIO-RKiP0AEK4

    Miscellaneous databases

    EvolutionaryTraceiP0AEK4

    Protein Ontology

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    PROi
    PR:P0AEK4

    Family and domain databases

    InterProiView protein in InterPro
    IPR014358 Enoyl-ACP_Rdtase_NADH
    IPR036291 NAD(P)-bd_dom_sf
    IPR002347 SDR_fam
    PANTHERiPTHR43159:SF2 PTHR43159:SF2, 1 hit
    PIRSFiPIRSF000094 Enoyl-ACP_rdct, 1 hit
    PRINTSiPR00081 GDHRDH
    SUPFAMiSSF51735 SSF51735, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFABI_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AEK4
    Secondary accession number(s): P29132
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 123 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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