Skip Header

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

UniProtKB - P21177 (FADB_ECOLI)

Entry version 186 (02 Jun 2021)
Sequence version 2 (01 Aug 1992)
Previous versions | rss
Add a publicationFeedback
Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

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

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.

UniRule annotation5 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 '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=53 µM for crotonyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  2. KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  3. KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
  4. KM=5.8 µM for 3-cis-tetradecenoyl-CoA (for Delta3-cis-Delta2-trans-enoyl-CoA isomerase activity)3 Publications
  5. KM=69 µM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications
  6. KM=2.0 µM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications

    <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 beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei119Important for catalytic activityUniRule annotation1
    Sitei139Important for catalytic activityUniRule annotation1
    <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 sitei296SubstrateUniRule annotation1
    Binding sitei324NAD; via amide nitrogenUniRule annotationCurated1
    Binding sitei343NADUniRule annotation1
    Binding sitei407NADUniRule annotation1
    Binding sitei429NADUniRule annotation1
    <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 sitei450For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation2 Publications1
    Binding sitei453NADUniRule annotation1
    Binding sitei500SubstrateUniRule annotation1
    Binding sitei660SubstrateUniRule annotation1

    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 bindingi400 – 402NADUniRule annotation3

    <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

    • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
    • 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB
    • dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
    • enoyl-CoA hydratase activity Source: UniProtKB
    • long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: GO_Central
    • NAD+ binding Source: InterPro
    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
    Biological processFatty acid metabolism, Lipid degradation, Lipid metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:FADB-MONOMER
    MetaCyc:FADB-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P21177

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

    More...    UniPathwayi    		UPA00659

    <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:
    Fatty acid oxidation complex subunit alphaUniRule annotation
    Including the following 2 domains:
    Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
    3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
    <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:fadBUniRule annotation
    Synonyms:oldB
    Ordered Locus Names:b3846, JW3822
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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>Mutagenesisi116G → F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected. 1 Publication1
    Mutagenesisi322G → A: 10-fold increase in KM for NADH. 1 Publication1
    Mutagenesisi450H → A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity. 1 Publication1

    <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 '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_00001092681 – 729Fatty acid oxidation complex subunit alphaAdd BLAST729

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P21177

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

    More...    PaxDbi    		P21177

    PRoteomics IDEntifications database

    More...    PRIDEi    		P21177

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Repressed by FadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to FadR resulting in its release from the DNA and thus derepression of the transcription.

    <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

    Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).

    UniRule annotation1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4263448, 158 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...    ComplexPortali    		CPX-3964, fadBA fatty acid oxidation complex, aerobic conditions

    Database of interacting proteins

    More...    DIPi    		DIP-9560N

    Protein interaction database and analysis system

    More...    IntActi    		P21177, 7 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3846

    <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

    1729
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Small Angle Scattering Biological Data Bank

    More...    SASBDBi    		P21177

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

    More...    SMRi    		P21177

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST189
    Regioni311 – 7293-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST419
    Regioni708 – 729DisorderedSequence analysisAdd BLAST22

    <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

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
    In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1024, Bacteria
    COG1250, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_009834_16_3_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P21177

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P21177

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_01621, FadB, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR006180, 3-OHacyl-CoA_DH_CS
    IPR006176, 3-OHacyl-CoA_DH_NAD-bd
    IPR006108, 3HC_DH_C
    IPR008927, 6-PGluconate_DH-like_C_sf
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR018376, Enoyl-CoA_hyd/isom_CS
    IPR001753, Enoyl-CoA_hydra/iso
    IPR012799, FadB
    IPR036291, NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00725, 3HCDH, 2 hits
    PF02737, 3HCDH_N, 1 hit
    PF00378, ECH_1, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF48179, SSF48179, 2 hits
    SSF51735, SSF51735, 1 hit
    SSF52096, SSF52096, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR02437, FadB, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00067, 3HCDH, 1 hit
    PS00166, ENOYL_COA_HYDRATASE, 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.

    P21177-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS 
            60         70         80         90        100
    DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED 
           110        120        130        140        150
    LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG 
           160        170        180        190        200
    SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV 
           210        220        230        240        250
    LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA 
           260        270        280        290        300
    PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 
           310        320        330        340        350
    GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT 
           360        370        380        390        400
    LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV 
           410        420        430        440        450
    VENPKVKKAV LAETEQKVRQ DTVLASNTST IPISELANAL ERPENFCGMH 
           460        470        480        490        500
    FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN 
           510        520        530        540        550
    RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH 
           560        570        580        590        600
    HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 
           610        620        630        640        650
    KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT 
           660        670        680        690        700
    PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP 
           710        720 
    EGLRNKARHN EPYYPPVEPA RPVGDLKTA
    Length:729
    Mass (Da):79,594
    Last modified:August 1, 1992 - 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:i6F1055E402F6B129
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti518A → R in AAA23750 (PubMed:1699931).Curated1
    Sequence conflicti664F → L in CAB40809 (PubMed:2204034).Curated1
    Sequence conflicti666P → A in CAB40809 (PubMed:2204034).Curated1

    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
    		M59368 Genomic DNA Translation: AAA23750.1
    X52837 Genomic DNA Translation: CAB40809.1
    M74164 Genomic DNA Translation: AAA62777.1
    M87049 Genomic DNA Translation: AAA67643.1
    U00096 Genomic DNA Translation: AAC76849.1
    AP009048 Genomic DNA Translation: BAE77457.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A39592

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418288.1, NC_000913.3
    WP_000965936.1, NZ_SSZK01000046.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76849; AAC76849; b3846
    BAE77457; BAE77457; BAE77457

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948336

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW3822
    eco:b3846

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|511145.12.peg.3960

    <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
    		M59368 Genomic DNA Translation: AAA23750.1
    X52837 Genomic DNA Translation: CAB40809.1
    M74164 Genomic DNA Translation: AAA62777.1
    M87049 Genomic DNA Translation: AAA67643.1
    U00096 Genomic DNA Translation: AAC76849.1
    AP009048 Genomic DNA Translation: BAE77457.1
    PIRiA39592
    RefSeqiNP_418288.1, NC_000913.3
    WP_000965936.1, NZ_SSZK01000046.1

    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
    6TNMX-ray2.95A1-729[»]
    SASBDBiP21177
    SMRiP21177
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263448, 158 interactors
    ComplexPortaliCPX-3964, fadBA fatty acid oxidation complex, aerobic conditions
    DIPiDIP-9560N
    IntActiP21177, 7 interactors
    STRINGi511145.b3846

    Proteomic databases

    jPOSTiP21177
    PaxDbiP21177
    PRIDEiP21177

    Genome annotation databases

    EnsemblBacteriaiAAC76849; AAC76849; b3846
    BAE77457; BAE77457; BAE77457
    GeneIDi948336
    KEGGiecj:JW3822
    eco:b3846
    PATRICifig|511145.12.peg.3960

    Organism-specific databases

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

    More...    EchoBASEi    		EB0275

    Phylogenomic databases

    eggNOGiCOG1024, Bacteria
    COG1250, Bacteria
    HOGENOMiCLU_009834_16_3_6
    InParanoidiP21177
    PhylomeDBiP21177

    Enzyme and pathway databases

    UniPathwayiUPA00659
    BioCyciEcoCyc:FADB-MONOMER
    MetaCyc:FADB-MONOMER
    SABIO-RKiP21177

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P21177

    Family and domain databases

    HAMAPiMF_01621, FadB, 1 hit
    InterProiView protein in InterPro
    IPR006180, 3-OHacyl-CoA_DH_CS
    IPR006176, 3-OHacyl-CoA_DH_NAD-bd
    IPR006108, 3HC_DH_C
    IPR008927, 6-PGluconate_DH-like_C_sf
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR018376, Enoyl-CoA_hyd/isom_CS
    IPR001753, Enoyl-CoA_hydra/iso
    IPR012799, FadB
    IPR036291, NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF00725, 3HCDH, 2 hits
    PF02737, 3HCDH_N, 1 hit
    PF00378, ECH_1, 1 hit
    SUPFAMiSSF48179, SSF48179, 2 hits
    SSF51735, SSF51735, 1 hit
    SSF52096, SSF52096, 1 hit
    TIGRFAMsiTIGR02437, FadB, 1 hit
    PROSITEiView protein in PROSITE
    PS00067, 3HCDH, 1 hit
    PS00166, ENOYL_COA_HYDRATASE, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiFADB_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: P21177
    Secondary accession number(s): Q2M8E9
    <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: May 1, 1991
    Last sequence update: August 1, 1992
    Last modified: June 2, 2021
    This is version 186 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again