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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

scu

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May function in mitochondrial tRNA maturation. Catalyzes the beta-oxidation at position 17 of androgens and estrogens, and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-beta-hydroxylated bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. Required for cell survival during embryonic development. May play a role in germline formation.2 Publications

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.1 Publication
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.1 Publication
Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.1 Publication

Kineticsi

  1. KM=33.7 µM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)1 Publication
  2. KM=101 µM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  3. KM=37.3 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  4. KM=12.3 µM for 5-alpha-dihydrotestosterone (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)1 Publication
  5. KM=11.1 µM for 17-beta-estradiol (in the presence of 0.2 mM NADH, at pH 9.3 and 25 degrees Celsius)1 Publication
  6. KM=9 µM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  7. KM=3 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  8. KM=32.5 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)1 Publication
  9. KM=64.4 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)1 Publication
  10. KM=124 µM for NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.3 for the dehydrogenase reaction, and 6.4 for the reductase reaction.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei149SubstrateBy similarity1
    Active sitei162Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi6 – 31NADBy similarityAdd BLAST26

    GO - Molecular functioni

    • 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
    • 7-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: FlyBase
    • acetoacetyl-CoA reductase activity Source: FlyBase
    • estradiol 17-beta-dehydrogenase activity Source: FlyBase
    • steroid dehydrogenase activity Source: FlyBase
    • testosterone dehydrogenase (NAD+) activity Source: FlyBase
    • testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

    GO - Biological processi

    • acyl-CoA metabolic process Source: FlyBase
    • androgen metabolic process Source: FlyBase
    • ecdysone metabolic process Source: FlyBase
    • estrogen metabolic process Source: FlyBase
    • fatty acid metabolic process Source: FlyBase
    • mitochondrial tRNA processing Source: FlyBase
    • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    • steroid metabolic process Source: FlyBase

    Keywordsi

    Molecular functionOxidoreductase
    Biological processtRNA processing
    LigandNAD

    Enzyme and pathway databases

    ReactomeiR-DME-70895 Branched-chain amino acid catabolism

    Chemistry databases

    SwissLipidsiSLP:000000795

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.35)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.51)
    Short name:
    17-beta-HSD 10
    3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.178)
    3-hydroxyacyl-CoA dehydrogenase type II
    Mitochondrial ribonuclease P protein 2
    Short name:
    Mitochondrial RNase P protein 2
    Scully protein
    Type II HADH
    Gene namesi
    Name:scu
    ORF Names:CG7113
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    Proteomesi
    • UP000000803 Componenti: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0021765 scu

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic and pupal lethal. Male mutants show small testes and degenerating spermatocytes with a large accumulation of small fat-containing vesicles in the cytoplasm and almost no mitochondria. Null mutant photoreceptors fail to differentiate normally, are unable to form proper rhabdomeres and present smaller mitochondria with fewer, but swollen crestae, than wild-type cells.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi33L → Q: Lethal allele. 1 Publication1
    Mutagenesisi120F → I: Lethal allele. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000548131 – 2553-hydroxyacyl-CoA dehydrogenase type-2Add BLAST255

    Proteomic databases

    PaxDbiO18404
    PRIDEiO18404

    Expressioni

    Tissue specificityi

    Found in many tissues including CNS, imaginal disks and salivary glands. Highest expression in both embryonic gonadal primordia and mature ovaries and testes.1 Publication

    Developmental stagei

    Expressed throughout embryonic development. In adults, expression is higher in females than in males.1 Publication

    Inductioni

    By 20-hydroxyecdysone.1 Publication

    Gene expression databases

    BgeeiFBgn0021765
    ExpressionAtlasiO18404 differential
    GenevisibleiO18404 DM

    Interactioni

    Subunit structurei

    Multimer.Curated

    Protein-protein interaction databases

    BioGridi59109, 78 interactors
    DIPiDIP-17092N
    IntActiO18404, 12 interactors
    STRINGi7227.FBpp0074285

    Structurei

    3D structure databases

    ProteinModelPortaliO18404
    SMRiO18404
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1199 Eukaryota
    ENOG410XNNW LUCA
    GeneTreeiENSGT00910000144076
    InParanoidiO18404
    KOiK08683
    OMAiLMGLVNC
    OrthoDBiEOG091G0G9O
    PhylomeDBiO18404

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR020904 Sc_DH/Rdtase_CS
    IPR002347 SDR_fam
    PfamiView protein in Pfam
    PF00106 adh_short, 1 hit
    PRINTSiPR00081 GDHRDH
    PR00080 SDRFAMILY
    SUPFAMiSSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00061 ADH_SHORT, 1 hit

    Sequencei

    Sequence statusi: Complete.

    O18404-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD
    60 70 80 90 100
    KVVFVPVDVT SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN
    110 120 130 140 150
    VAHRLEDFQR VININTVGTF NVIRLSAGLM GANEPNQDGQ RGVIVNTASV
    160 170 180 190 200
    AAFDGQIGQA AYSASKAAVV GMTLPIARDL STQGIRICTI APGLFNTPML
    210 220 230 240 250
    AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL NGEVIRIDGA

    LRMMP
    Length:255
    Mass (Da):26,905
    Last modified:January 1, 1998 - v1
    Checksum:iF58690643FA0FD03
    GO

    Sequence cautioni

    The sequence AET07646 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti134E → K in AAM51999 (PubMed:12537569).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y15102 mRNA Translation: CAA75377.1
    AE014298 Genomic DNA Translation: AAF48797.1
    AY121672 mRNA Translation: AAM51999.1
    BT029045 mRNA Translation: ABJ16978.1
    BT132763 mRNA Translation: AET07646.1 Different initiation.
    RefSeqiNP_523396.1, NM_078672.5
    UniGeneiDm.7957

    Genome annotation databases

    EnsemblMetazoaiFBtr0074511; FBpp0074285; FBgn0021765
    GeneIDi32789
    KEGGidme:Dmel_CG7113

    Similar proteinsi

    Entry informationi

    Entry nameiHCD2_DROME
    AccessioniPrimary (citable) accession number: O18404
    Secondary accession number(s): G7H840, Q059C3, Q8MRC1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 1, 1998
    Last modified: March 28, 2018
    This is version 153 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

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