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Protein

Steroid 3-ketoacyl-CoA thiolase

Gene

fadA5

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

Functioni

Involved in the beta-oxidation of the cholesterol side chain (PubMed:19822655). It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection (PubMed:19822655). Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) and acetyl-CoA (PubMed:25482540). Also able to use acetoacetyl-CoA (AcAcCoA) as substrate (PubMed:19822655).2 Publications

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.2 Publications
3-oxo-4-pregnene-20-carboxyl-CoA + acetyl-CoA = CoA + 3,22-dioxochol-4-en-24-oyl-CoA.2 Publications

Kineticsi

Kcat is 0.725 sec(-1) for 3,22-dioxochol-4-en-24-oyl-CoA substrate (PubMed:25482540). Kcat is 0.076 sec(-1) for AcAcCoA substrate (PubMed:19822655). Kcat is 0.018 sec(-1) for CoA substrate (PubMed:19822655).2 Publications
  1. KM=3.1 µM for CoA1 Publication
  2. KM=15 µM for CoA1 Publication
  3. KM=11.8 µM for 3,22-dioxochol-4-en-24-oyl-CoA1 Publication
  4. KM=464 µM for AcAcCoA1 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
    Active sitei93Acyl-thioester intermediateCombined sources1 Publication1
    Binding sitei151Coenzyme ACombined sources1 Publication1
    Binding sitei246Coenzyme A; via carbonyl oxygenCombined sources1 Publication1
    Active sitei347Proton acceptorCombined sources1 Publication1
    Active sitei377Proton acceptor1 Publication1
    Binding sitei379Substrate; via amide nitrogenCombined sources1 Publication1

    GO - Molecular functioni

    • acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC
    • identical protein binding Source: IntAct

    GO - Biological processi

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism, Virulence

    Enzyme and pathway databases

    BioCyciMetaCyc:G185E-7823-MONOMER
    UniPathwayiUPA01058

    Chemistry databases

    SwissLipidsiSLP:000001007

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Steroid 3-ketoacyl-CoA thiolase1 Publication (EC:2.3.1.162 Publications)
    Alternative name(s):
    Acetyl-CoA acetyltransferase FadA51 Publication
    Beta-ketoacyl-CoA thiolase1 Publication
    Gene namesi
    Name:fadA5
    Ordered Locus Names:LH57_19345Imported, Rv3546
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome
    • UP000031768 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv3546

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene display an attenuated disease phenotype with reduced colony-forming units in comparison to the wild-type. This mutant is unable to metabolize cholesterol to androst-4-ene-3,17-dione (AD) and androsta-1,4-diene-3,17-dione (ADD).1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004385021 – 391Steroid 3-ketoacyl-CoA thiolaseAdd BLAST391

    Proteomic databases

    PaxDbiI6XHI4

    Expressioni

    Inductioni

    Induced by cholesterol and repressed by KstR.1 Publication

    Interactioni

    Subunit structurei

    Dimer of dimers.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-16132055,EBI-16132055

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    STRINGi83332.Rv3546

    Structurei

    Secondary structure

    1391
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 11Combined sources8
    Turni20 – 23Combined sources4
    Helixi26 – 42Combined sources17
    Beta strandi43 – 45Combined sources3
    Helixi49 – 51Combined sources3
    Beta strandi54 – 58Combined sources5
    Helixi64 – 66Combined sources3
    Turni67 – 69Combined sources3
    Helixi70 – 77Combined sources8
    Beta strandi85 – 91Combined sources7
    Helixi92 – 94Combined sources3
    Helixi95 – 108Combined sources14
    Beta strandi113 – 122Combined sources10
    Turni123 – 125Combined sources3
    Turni128 – 132Combined sources5
    Helixi136 – 139Combined sources4
    Helixi151 – 162Combined sources12
    Helixi166 – 185Combined sources20
    Turni186 – 192Combined sources7
    Beta strandi196 – 201Combined sources6
    Beta strandi207 – 214Combined sources8
    Helixi225 – 230Combined sources6
    Helixi242 – 244Combined sources3
    Beta strandi249 – 259Combined sources11
    Helixi260 – 265Combined sources6
    Beta strandi272 – 281Combined sources10
    Turni284 – 286Combined sources3
    Helixi291 – 302Combined sources12
    Helixi306 – 308Combined sources3
    Beta strandi310 – 314Combined sources5
    Helixi319 – 329Combined sources11
    Helixi333 – 335Combined sources3
    Helixi342 – 345Combined sources4
    Turni349 – 351Combined sources3
    Helixi352 – 367Combined sources16
    Beta strandi371 – 378Combined sources8
    Turni379 – 381Combined sources3
    Beta strandi382 – 390Combined sources9

    3D structure databases

    ProteinModelPortaliI6XHI4
    SMRiI6XHI4
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni221 – 223Coenzyme A bindingCombined sources1 Publication3

    Sequence similaritiesi

    Belongs to the thiolase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105F2C Bacteria
    ENOG410XVDF LUCA
    KOiK00626
    OMAiGMKMGDI
    PhylomeDBiI6XHI4

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 1 hit
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00737 THIOLASE_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

    I6XHI4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGYPVIVEAT RSPIGKRNGW LSGLHATELL GAVQKAVVDK AGIQSGLHAG
    60 70 80 90 100
    DVEQVIGGCV TQFGEQSNNI SRVAWLTAGL PEHVGATTVD CQCGSGQQAN
    110 120 130 140 150
    HLIAGLIAAG AIDVGIACGI EAMSRVGLGA NAGPDRSLIR AQSWDIDLPN
    160 170 180 190 200
    QFEAAERIAK RRGITREDVD VFGLESQRRA QRAWAEGRFD REISPIQAPV
    210 220 230 240 250
    LDEQNQPTGE RRLVFRDQGL RETTMAGLGE LKPVLEGGIH TAGTSSQISD
    260 270 280 290 300
    GAAAVLWMDE AVARAHGLTP RARIVAQALV GAEPYYHLDG PVQSTAKVLE
    310 320 330 340 350
    KAGMKIGDID IVEINEAFAS VVLSWARVHE PDMDRVNVNG GAIALGHPVG
    360 370 380 390
    CTGSRLITTA LHELERTDQS LALITMCAGG ALSTGTIIER I
    Length:391
    Mass (Da):41,329
    Last modified:October 3, 2012 - v1
    Checksum:iD0B4C64729B00D76
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA Translation: CCP46368.1
    CP009480 Genomic DNA Translation: AIR16336.1
    RefSeqiNP_218063.1, NC_000962.3
    WP_003419307.1, NZ_KK339374.1

    Genome annotation databases

    EnsemblBacteriaiAIR16336; AIR16336; LH57_19345
    CCP46368; CCP46368; Rv3546
    GeneIDi887360
    KEGGimtu:Rv3546
    mtv:RVBD_3546
    PATRICifig|83332.111.peg.3951

    Similar proteinsi

    Entry informationi

    Entry nameiFADA5_MYCTU
    AccessioniPrimary (citable) accession number: I6XHI4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 30, 2016
    Last sequence update: October 3, 2012
    Last modified: February 28, 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

    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

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