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Entry version 142 (23 Feb 2022)
Sequence version 2 (23 Jan 2007)
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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.

5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 (PubMed:10398587, PubMed:10493822, PubMed:11514139, PubMed:12109908, PubMed:12699381, PubMed:19959361, PubMed:8119879, PubMed:8953047, PubMed:9707111). The antibiotic diazaborine interferes with the activity by binding to the protein and NAD (PubMed:8119879).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)1 Publication
  2. KM=22 µM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5)1 Publication
  3. KM=24 µM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius and pH 8)1 Publication
  4. KM=2700 µM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.1 Publication
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.1 Publication
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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

<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

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

<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%5Fand%5Fbiotech%5Fsection">'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
CHEMBL2364678

Drug and drug target database

More...
DrugBanki
DB04030, 1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole
DB08265, 2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL
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
DB08605, 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL
DB02379, Beta-D-Glucose
DB01691, Indole Naphthyridinone
DB08604, Triclosan

DrugCentral

More...
DrugCentrali
P0AEK4

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000548992 – 262Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST261

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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
511145.b1288

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

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

More...
SMRi
P0AEK4

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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
COG0623, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AEK4

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AEK4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05372, ENR_SDR, 1 hit

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, PTHR43159, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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_STEB01000005.1

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
67417387
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_STEB01000005.1

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[»]
SMRiP0AEK4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260135, 290 interactors
DIPiDIP-31867N
IntActiP0AEK4, 12 interactors
STRINGi511145.b1288

Chemistry databases

BindingDBiP0AEK4
ChEMBLiCHEMBL1857
CHEMBL2364678
DrugBankiDB04030, 1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole
DB08265, 2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL
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
DB08605, 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL
DB02379, Beta-D-Glucose
DB01691, Indole Naphthyridinone
DB08604, Triclosan
DrugCentraliP0AEK4
SwissLipidsiSLP:000001775

2D gel databases

SWISS-2DPAGEiP0AEK4

Proteomic databases

jPOSTiP0AEK4
PaxDbiP0AEK4
PRIDEiP0AEK4

Genome annotation databases

EnsemblBacteriaiAAC74370; AAC74370; b1288
BAA14841; BAA14841; BAA14841
GeneIDi67417387
945870
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

Phylogenomic databases

eggNOGiCOG0623, Bacteria
InParanoidiP0AEK4
PhylomeDBiP0AEK4

Enzyme and pathway databases

UniPathwayiUPA00078
UPA00094
BioCyciEcoCyc: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

CDDicd05372, ENR_SDR, 1 hit
InterProiView protein in InterPro
IPR014358, Enoyl-ACP_Rdtase_NADH
IPR036291, NAD(P)-bd_dom_sf
IPR002347, SDR_fam
PANTHERiPTHR43159, PTHR43159, 1 hit
PIRSFiPIRSF000094, Enoyl-ACP_rdct, 1 hit
PRINTSiPR00081, GDHRDH
SUPFAMiSSF51735, SSF51735, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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%5Fand%5Fisoforms">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: February 23, 2022
This is version 142 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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