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Entry version 138 (16 Oct 2019)
Sequence version 3 (05 Jul 2004)
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Protein

Acyl-CoA dehydrogenase FadE28

Gene

fadE28

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). May play an important role for the initial macrophage invasion, possibly in response to the acidification of phagosome (PubMed:18486437). It contributes partly to the virulence by increasing the efficiency of beta-oxidation (PubMed:18486437, PubMed:22045806). Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene-20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2'-propanoyl-CoA)-3a-alpha-H-7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), hexahydroindanone and pregenenone (PubMed:22045806, PubMed:23560677, PubMed:26161441).4 Publications

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD1 PublicationNote: Binds 1 FAD per heterodimer.1 Publication

<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

Kcat is 78 min(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:23560677). Kcat is 5.1 min(-1) for indanone-CoA ester as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:23560677). Kcat is 1.3 sec(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:26161441). Kcat is 0.16 sec(-1) for 3-OCO-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:26161441).2 Publications
  1. KM=5.3 µM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius)2 Publications
  2. KM=6.5 µM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication
  3. KM=86 µM for indanone-CoA ester (at pH 8.5 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is above 8. No activity is observed under pH 6.1 Publication

    <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: cholesterol degradation

    This protein is involved in the pathway cholesterol degradation, which is part of Steroid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway cholesterol degradation and in Steroid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei227FAD; shared with dimeric partner1 Publication1
    Binding sitei238FAD1 Publication1
    Binding sitei295FADBy similarity1
    Binding sitei299FAD; via amide nitrogenBy similarity1

    <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 processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism, Virulence
    LigandFAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:G185E-7821-MONOMER
    MTBH37RV:G185E-7821-MONOMER

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

    More...
    UniPathwayi
    UPA01058

    <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:
    Acyl-CoA dehydrogenase FadE281 Publication (EC:1.3.99.-2 Publications)
    Short name:
    ACAD1 Publication
    Alternative name(s):
    3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase alpha subunit1 Publication
    3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase alpha subunit1 Publication
    <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:fadE28
    Ordered Locus Names:Rv3544c
    ORF Names:LH57_19335
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv3544c

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004385171 – 339Acyl-CoA dehydrogenase FadE28Add BLAST339

    Proteomic databases

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

    More...
    PaxDbi
    P71857

    <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

    Induced by cholesterol and repressed by KtsR (PubMed:17635188). Up-regulated in vitro by acid shock and ex vivo by macrophage challenge (PubMed:18486437).2 Publications

    <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

    Heterotetramer composed of FadE28 and FadE29.

    2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv3544c

    <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

    3D structure databases

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

    More...
    SMRi
    P71857

    Database of comparative protein structure models

    More...
    ModBasei
    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

    <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

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108RK3 Bacteria
    ENOG4111G6X LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000131661

    KEGG Orthology (KO)

    More...
    KOi
    K22821

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DITYPMH

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P71857

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.540.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036250 AcylCo_DH-like_C
    IPR009075 AcylCo_DH/oxidase_C
    IPR013786 AcylCoA_DH/ox_N
    IPR037069 AcylCoA_DH/ox_N_sf
    IPR009100 AcylCoA_DH/oxidase_NM_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00441 Acyl-CoA_dh_1, 1 hit
    PF02771 Acyl-CoA_dh_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47203 SSF47203, 1 hit
    SSF56645 SSF56645, 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>. 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_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.

    P71857-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDFDPTAEQQ AVADVVTSVL ERDISWEALV CGGVTALPVP ERLGGDGVGL
    60 70 80 90 100
    FEVGALLTEV GRHGAVTPAL ATLGLGVVPL LELASAEQQD RFLAGVAKGG
    110 120 130 140 150
    VLTAALNEPG AALPDRPATS FVGGRLSGTK VGVGYAEQAD WMLVTADNAV
    160 170 180 190 200
    VVVSPTADGV RMVRTPTSNG SDEYVMTMDG VAVADCDILA DVAAHRVNQL
    210 220 230 240 250
    ALAVMGAYAD GLVAGALRLT ADYVANRKQF GKPLSTFQTV AAQLAEVYIA
    260 270 280 290 300
    SRTIDLVAKS VIWRLAEDLD AGDDLGVLGY WVTSQAPPAM QICHHLHGGM
    310 320 330
    GMDVTYPMHR YYSTIKDLTR LLGGPSHRLE LLGARCSLT
    Length:339
    Mass (Da):35,469
    Last modified:July 5, 2004 - v3
    <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:iD84AC763D7ACFE5F
    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
    CP009480 Genomic DNA Translation: AIR16334.1
    AL123456 Genomic DNA Translation: CCP46366.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_218061.1, NC_000962.3
    WP_003419299.1, NZ_NVQJ01000014.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AIR16334; AIR16334; LH57_19335
    CCP46366; CCP46366; Rv3544c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    888091

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv3544c
    mtv:RVBD_3544c

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|83332.111.peg.3949

    <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
    CP009480 Genomic DNA Translation: AIR16334.1
    AL123456 Genomic DNA Translation: CCP46366.1
    RefSeqiNP_218061.1, NC_000962.3
    WP_003419299.1, NZ_NVQJ01000014.1

    3D structure databases

    SMRiP71857
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3544c

    Proteomic databases

    PaxDbiP71857

    Genome annotation databases

    EnsemblBacteriaiAIR16334; AIR16334; LH57_19335
    CCP46366; CCP46366; Rv3544c
    GeneIDi888091
    KEGGimtu:Rv3544c
    mtv:RVBD_3544c
    PATRICifig|83332.111.peg.3949

    Organism-specific databases

    TubercuListiRv3544c

    Phylogenomic databases

    eggNOGiENOG4108RK3 Bacteria
    ENOG4111G6X LUCA
    HOGENOMiHOG000131661
    KOiK22821
    OMAiDITYPMH
    PhylomeDBiP71857

    Enzyme and pathway databases

    UniPathwayiUPA01058
    BioCyciMetaCyc:G185E-7821-MONOMER
    MTBH37RV:G185E-7821-MONOMER

    Family and domain databases

    Gene3Di1.10.540.10, 1 hit
    InterProiView protein in InterPro
    IPR036250 AcylCo_DH-like_C
    IPR009075 AcylCo_DH/oxidase_C
    IPR013786 AcylCoA_DH/ox_N
    IPR037069 AcylCoA_DH/ox_N_sf
    IPR009100 AcylCoA_DH/oxidase_NM_dom
    PfamiView protein in Pfam
    PF00441 Acyl-CoA_dh_1, 1 hit
    PF02771 Acyl-CoA_dh_N, 1 hit
    SUPFAMiSSF47203 SSF47203, 1 hit
    SSF56645 SSF56645, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiCHSE1_MYCTU
    <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: P71857
    Secondary accession number(s): I6YCD6
    <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: November 30, 2016
    Last sequence update: July 5, 2004
    Last modified: October 16, 2019
    This is version 138 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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