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Protein

3-ketosteroid-9-alpha-monooxygenase oxygenase subunit

Gene

kshA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the opening of ring B of 1,4-androstadiene-3,17,-dione (ADD) and 4-androstene-3,17-dione (ADD) with concomitant aromatization of ring A. The ring B is subsequently hydroxylated to yield a catechol and then subject to meta-cleavage.1 Publication

Catalytic activityi

Androsta-1,4-diene-3,17-dione + NADH + O2 = 9-alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterPROSITE-ProRule annotation1 PublicationNote: Binds 1 [2Fe-2S] cluster per subunit.PROSITE-ProRule annotation1 Publication
  • Fe cation1 PublicationNote: Binds 1 Fe cation.1 Publication

Kineticsi

  1. KM=24 µM for AD (at pH 7 and at 25 degrees Celsius)1 Publication
  2. KM=110 µM for ADD (at pH 7 and at 25 degrees Celsius)1 Publication

    Pathwayi: steroid biosynthesis

    This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi67 – 671Iron-sulfur
    Metal bindingi69 – 691Iron-sulfur (2Fe-2S); via pros nitrogen
    Metal bindingi86 – 861Iron-sulfur
    Metal bindingi89 – 891Iron-sulfur (2Fe-2S); via pros nitrogen
    Metal bindingi181 – 1811Iron
    Metal bindingi186 – 1861Iron
    Metal bindingi304 – 3041Iron

    GO - Molecular functioni

    • 2 iron, 2 sulfur cluster binding Source: UniProtKB
    • 3-ketosteroid 9-alpha-monooxygenase activity Source: UniProtKB-EC
    • ferrous iron binding Source: UniProtKB
    • iron ion binding Source: MTBBASE
    • ketosteroid monooxygenase activity Source: MTBBASE
    • steroid 9-alpha-monooxygenase activity Source: UniProtKB

    GO - Biological processi

    • cholesterol catabolic process Source: MTBBASE
    • pathogenesis Source: MTBBASE
    • protein homotrimerization Source: MTBBASE
    • response to cholesterol Source: MTBBASE
    • steroid biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16885.
    MTBRV:RV3526-MONOMER.
    BRENDAi1.14.13.142. 3445.
    UniPathwayiUPA00062.

    Chemistry

    SwissLipidsiSLP:000001163.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketosteroid-9-alpha-monooxygenase oxygenase subunit (EC:1.14.13.142)
    Alternative name(s):
    3-ketosteroid-9-alpha-hydroxylase oxygenase subunit
    Rieske-type oxygenase
    Short name:
    RO
    Gene namesi
    Name:kshA
    Ordered Locus Names:Rv3526
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv3526.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3863863-ketosteroid-9-alpha-monooxygenase oxygenase subunitPRO_0000404098Add
    BLAST

    Proteomic databases

    PaxDbiP71875.
    PRIDEiP71875.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv3526.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 318Combined sources
    Helixi32 – 354Combined sources
    Beta strandi37 – 393Combined sources
    Beta strandi41 – 455Combined sources
    Beta strandi48 – 547Combined sources
    Beta strandi60 – 667Combined sources
    Turni68 – 703Combined sources
    Helixi74 – 763Combined sources
    Beta strandi77 – 804Combined sources
    Beta strandi83 – 853Combined sources
    Turni87 – 893Combined sources
    Beta strandi92 – 943Combined sources
    Beta strandi97 – 1015Combined sources
    Beta strandi119 – 1224Combined sources
    Beta strandi125 – 1306Combined sources
    Helixi139 – 1413Combined sources
    Helixi147 – 1504Combined sources
    Beta strandi158 – 16710Combined sources
    Helixi169 – 1779Combined sources
    Helixi181 – 1844Combined sources
    Beta strandi188 – 19811Combined sources
    Beta strandi201 – 21010Combined sources
    Beta strandi214 – 2163Combined sources
    Beta strandi219 – 2213Combined sources
    Beta strandi224 – 24623Combined sources
    Beta strandi249 – 26315Combined sources
    Beta strandi266 – 27611Combined sources
    Beta strandi279 – 2813Combined sources
    Helixi287 – 30822Combined sources
    Helixi321 – 3233Combined sources
    Helixi326 – 3349Combined sources
    Helixi335 – 3373Combined sources
    Helixi340 – 3423Combined sources
    Helixi345 – 3484Combined sources
    Beta strandi351 – 3544Combined sources
    Helixi358 – 37215Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZYLX-ray2.30A1-386[»]
    4QCKX-ray2.46A1-386[»]
    ProteinModelPortaliP71875.
    SMRiP71875. Positions 14-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP71875.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 128103RieskePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Rieske domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CIJ. Bacteria.
    COG4638. LUCA.
    HOGENOMiHOG000052102.
    InParanoidiP71875.
    KOiK15982.
    OMAiAVYQMRR.
    OrthoDBiEOG6R5C3M.
    PhylomeDBiP71875.

    Family and domain databases

    Gene3Di2.102.10.10. 1 hit.
    InterProiIPR017941. Rieske_2Fe-2S.
    [Graphical view]
    PfamiPF00355. Rieske. 1 hit.
    [Graphical view]
    SUPFAMiSSF50022. SSF50022. 1 hit.
    PROSITEiPS51296. RIESKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P71875-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTDTSGVGV REIDAGALPT RYARGWHCLG VAKDYLEGKP HGVEAFGTKL
    60 70 80 90 100
    VVFADSHGDL KVLDGYCRHM GGDLSEGTVK GDEVACPFHD WRWGGDGRCK
    110 120 130 140 150
    LVPYARRTPR MARTRSWTTD VRSGLLFVWH DHEGNPPDPA VRIPEIPEAA
    160 170 180 190 200
    SDEWTDWRWN RILIEGSNCR DIIDNVTDMA HFFYIHFGLP TYFKNVFEGH
    210 220 230 240 250
    IASQYLHNVG RPDVDDLGTS YGEAHLDSEA SYFGPSFMIN WLHNRYGNYK
    260 270 280 290 300
    SESILINCHY PVTQNSFVLQ WGVIVEKPKG MSEEMTDKLS RVFTEGVSKG
    310 320 330 340 350
    FLQDVEIWKH KTRIDNPLLV EEDGAVYQLR RWYEQFYVDV ADIKPEMVER
    360 370 380
    FEIEVDTKRA NEFWNAEVEK NLKSREVSDD VPAEQH
    Length:386
    Mass (Da):44,268
    Last modified:July 1, 1997 - v2
    Checksum:i510F89D334D230B4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46348.1.
    PIRiG70674.
    RefSeqiNP_218043.1. NC_000962.3.
    WP_003419211.1. NZ_KK339374.1.

    Genome annotation databases

    EnsemblBacteriaiCCP46348; CCP46348; Rv3526.
    GeneIDi888268.
    KEGGimtu:Rv3526.
    PATRICi18156454. VBIMycTub87468_3937.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46348.1.
    PIRiG70674.
    RefSeqiNP_218043.1. NC_000962.3.
    WP_003419211.1. NZ_KK339374.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZYLX-ray2.30A1-386[»]
    4QCKX-ray2.46A1-386[»]
    ProteinModelPortaliP71875.
    SMRiP71875. Positions 14-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3526.

    Chemistry

    SwissLipidsiSLP:000001163.

    Proteomic databases

    PaxDbiP71875.
    PRIDEiP71875.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP46348; CCP46348; Rv3526.
    GeneIDi888268.
    KEGGimtu:Rv3526.
    PATRICi18156454. VBIMycTub87468_3937.

    Organism-specific databases

    TubercuListiRv3526.

    Phylogenomic databases

    eggNOGiENOG4105CIJ. Bacteria.
    COG4638. LUCA.
    HOGENOMiHOG000052102.
    InParanoidiP71875.
    KOiK15982.
    OMAiAVYQMRR.
    OrthoDBiEOG6R5C3M.
    PhylomeDBiP71875.

    Enzyme and pathway databases

    UniPathwayiUPA00062.
    BioCyciMetaCyc:MONOMER-16885.
    MTBRV:RV3526-MONOMER.
    BRENDAi1.14.13.142. 3445.

    Miscellaneous databases

    EvolutionaryTraceiP71875.

    Family and domain databases

    Gene3Di2.102.10.10. 1 hit.
    InterProiIPR017941. Rieske_2Fe-2S.
    [Graphical view]
    PfamiPF00355. Rieske. 1 hit.
    [Graphical view]
    SUPFAMiSSF50022. SSF50022. 1 hit.
    PROSITEiPS51296. RIESKE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25618 / H37Rv.
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.
    3. "Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis."
      Capyk J.K., D'Angelo I., Strynadka N.C., Eltis L.D.
      J. Biol. Chem. 284:9937-9946(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION AS A 3-KETOSTEROID-9-ALPHA-HYDROXYLASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR.
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiKSHA_MYCTU
    AccessioniPrimary (citable) accession number: P71875
    Secondary accession number(s): L0TCS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: July 1, 1997
    Last modified: December 9, 2015
    This is version 104 of the entry and version 2 of the sequence. [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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.