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Protein

Acyl-CoA dehydrogenase FadE26

Gene

fadE26

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA (PubMed:26348625, PubMed:26161441). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) (PubMed:26161441). It dehydrogenates only (25S)-OCS-CoA diastereomer (Probable).2 Publications

Catalytic activityi

(25S)-3-oxo-cholest-4-en-26-oyl-CoA + acceptor = 3-oxo-cholest-4,24-dien-26-oyl-CoA + reduced acceptor.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per heterodimer.1 Publication

Activity regulationi

Uncompetitively inhibited by high concentration of 3-OCS-CoA.1 Publication

Kineticsi

Kcat is 2.7 sec(-1) for 3-OCS-CoA as substrate (at pH 8.5 and 25 degrees Celsius). Kcat is 1.5 sec(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius). Kcat is 0.48 sec(-1) for 3-OCO-CoA as substrate (at pH 8.5 and 25 degrees Celsius). Kcat is 0.042 sec(-1) for octanoyl-CoA as substrate (at pH 8.5 and 25 degrees Celsius).1 Publication
  1. KM=2.6 µM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication
  2. KM=3.3 µM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication
  3. KM=3.4 µM for 3-OCS-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication
  4. KM=4.1 µM for octanoyl-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication

    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
    Binding sitei136FADCombined sources1 Publication1
    Binding sitei162FADCombined sources1 Publication1
    Active sitei247Proton acceptor1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi127 – 130FADCombined sources1 Publication4
    Nucleotide bindingi380 – 382FADCombined sources1 Publication3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism, Virulence
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:G185E-7781-MONOMER
    UniPathwayi
    UPA01058

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA dehydrogenase FadE261 Publication (EC:1.3.99.-1 Publication)
    Short name:
    ACAD1 Publication
    Alternative name(s):
    3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit1 Publication
    Gene namesi
    Name:fadE26
    Ordered Locus Names:Rv3504
    ORF Names:LH57_19105Imported
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome
    • UP000031768 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv3504

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi247E → A: Loss of dehydrogenase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004385201 – 400Acyl-CoA dehydrogenase FadE26Add BLAST400

    Proteomic databases

    PaxDbiI6YCA3

    Expressioni

    Inductioni

    Induced by cholesterol and repressed by KstR.1 Publication

    Interactioni

    Subunit structurei

    Heterotetramer (dimer of heterodimers) composed of FadE26 and FadE27.1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv3504

    Structurei

    Secondary structure

    1400
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliI6YCA3
    SMRiI6YCA3
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105X7H Bacteria
    ENOG410XPQC LUCA
    OMAiRDIIAMT
    PhylomeDBiI6YCA3

    Family and domain databases

    Gene3Di1.10.540.10, 1 hit
    InterProiView protein in InterPro
    IPR006091 Acyl-CoA_Oxase/DH_cen-dom
    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
    PF02770 Acyl-CoA_dh_M, 1 hit
    PF02771 Acyl-CoA_dh_N, 1 hit
    SUPFAMiSSF47203 SSF47203, 1 hit
    SSF56645 SSF56645, 1 hit

    Sequencei

    Sequence statusi: Complete.

    I6YCA3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRISYTPQQE ELRRELRSYF ATLMTPERRE ALSSVQGEYG VGNVYRETIA
    60 70 80 90 100
    QMGRDGWLAL GWPKEYGGQG RSAMDQLIFT DEAAIAGAPV PFLTINSVAP
    110 120 130 140 150
    TIMAYGTDEQ KRFFLPRIAA GDLHFSIGYS EPGAGTDLAN LRTTAVRDGD
    160 170 180 190 200
    DYVVNGQKMW TSLIQYADYV WLAVRTNPES SGAKKHRGIS VLIVPTTAEG
    210 220 230 240 250
    FSWTPVHTMA GPDTSATYYS DVRVPVANRV GEENAGWKLV TNQLNHERVA
    260 270 280 290 300
    LVSPAPIFGC LREVREWAQN TKDAGGTRLI DSEWVQLNLA RVHAKAEVLK
    310 320 330 340 350
    LINWELASSQ SGPKDAGPSP ADASAAKVFG TELATEAYRL LMEVLGTAAT
    360 370 380 390 400
    LRQNSPGALL RGRVERMHRA CLILTFGGGT NEVQRDIIGM VALGLPRANR
    Length:400
    Mass (Da):43,785
    Last modified:October 3, 2012 - v1
    Checksum:i2B25B8A76861F271
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP009480 Genomic DNA Translation: AIR16298.1
    AL123456 Genomic DNA Translation: CCP46326.1
    RefSeqiNP_218021.1, NC_000962.3
    WP_003418997.1, NZ_KK339370.1

    Genome annotation databases

    EnsemblBacteriaiAIR16298; AIR16298; LH57_19105
    CCP46326; CCP46326; Rv3504
    GeneIDi887722
    KEGGimtu:Rv3504
    mtv:RVBD_3504
    PATRICifig|83332.111.peg.3902

    Similar proteinsi

    Entry informationi

    Entry nameiCHSE4_MYCTU
    AccessioniPrimary (citable) accession number: I6YCA3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 30, 2016
    Last sequence update: October 3, 2012
    Last modified: September 12, 2018
    This is version 54 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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