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Protein

Acyl-CoA dehydrogenase FadE26

Gene

fadE26

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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.
    UniPathwayiUPA01058.

    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
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 23Combined sources17
    Helixi26 – 32Combined sources7
    Helixi44 – 54Combined sources11
    Turni58 – 61Combined sources4
    Helixi64 – 66Combined sources3
    Helixi73 – 86Combined sources14
    Helixi92 – 96Combined sources5
    Helixi98 – 105Combined sources8
    Helixi108 – 119Combined sources12
    Beta strandi125 – 128Combined sources4
    Beta strandi134 – 136Combined sources3
    Helixi138 – 140Combined sources3
    Beta strandi144 – 148Combined sources5
    Beta strandi151 – 159Combined sources9
    Helixi164 – 166Combined sources3
    Beta strandi168 – 176Combined sources9
    Helixi178 – 180Combined sources3
    Helixi184 – 186Combined sources3
    Beta strandi189 – 195Combined sources7
    Beta strandi201 – 206Combined sources6
    Beta strandi208 – 211Combined sources4
    Beta strandi214 – 225Combined sources12
    Helixi226 – 228Combined sources3
    Beta strandi229 – 232Combined sources4
    Helixi237 – 240Combined sources4
    Turni241 – 244Combined sources4
    Helixi255 – 269Combined sources15
    Helixi279 – 281Combined sources3
    Helixi283 – 308Combined sources26
    Helixi320 – 345Combined sources26
    Helixi346 – 348Combined sources3
    Helixi360 – 362Combined sources3
    Helixi363 – 370Combined sources8
    Helixi372 – 376Combined sources5
    Beta strandi377 – 379Combined sources3
    Helixi381 – 393Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4X28X-ray1.99A/B1-400[»]
    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: November 22, 2017
    This is version 53 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

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families