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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

scu

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei149 – 1491SubstrateBy similarity
    Active sitei162 – 1621Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 3126NADBy similarityAdd
    BLAST

    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
    • steroid metabolic process Source: FlyBase
    • tRNA processing Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_306893. Branched-chain amino acid catabolism.

    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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803 Componenti: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0021765. scu.

    Subcellular locationi

    • Mitochondrion By similarity

    • Note: Localizes to the lipid droplet fraction in early embryos.1 Publication

    GO - Cellular componenti

    • cytosol Source: FlyBase
    • lipid particle Source: FlyBase
    • microtubule associated complex Source: FlyBase
    • mitochondrion Source: UniProtKB
    Complete GO annotation...

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331L → Q: Lethal allele. 1 Publication
    Mutagenesisi120 – 1201F → I: Lethal allele. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2552553-hydroxyacyl-CoA dehydrogenase type-2PRO_0000054813Add
    BLAST

    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

    BgeeiO18404.
    GenevisibleiO18404. DM.

    Interactioni

    Subunit structurei

    Multimer.Curated

    Protein-protein interaction databases

    BioGridi59109. 74 interactions.
    DIPiDIP-17092N.
    IntActiO18404. 6 interactions.
    MINTiMINT-289527.
    STRINGi7227.FBpp0074285.

    Structurei

    3D structure databases

    ProteinModelPortaliO18404.
    SMRiO18404. Positions 2-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00760000118868.
    InParanoidiO18404.
    OMAiNMANIRC.
    OrthoDBiEOG7JT6X7.
    PhylomeDBiO18404.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    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 AET07646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341E → K in AAM51999 (PubMed:12537569).Curated

    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.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliO18404.
    SMRiO18404. Positions 2-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi59109. 74 interactions.
    DIPiDIP-17092N.
    IntActiO18404. 6 interactions.
    MINTiMINT-289527.
    STRINGi7227.FBpp0074285.

    Proteomic databases

    PaxDbiO18404.
    PRIDEiO18404.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiFBtr0074511; FBpp0074285; FBgn0021765.
    GeneIDi32789.

    Organism-specific databases

    CTDi32789.
    FlyBaseiFBgn0021765. scu.

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00760000118868.
    InParanoidiO18404.
    OMAiNMANIRC.
    OrthoDBiEOG7JT6X7.
    PhylomeDBiO18404.

    Enzyme and pathway databases

    ReactomeiREACT_306893. Branched-chain amino acid catabolism.

    Miscellaneous databases

    ChiTaRSiscu. fly.
    GenomeRNAii32789.
    NextBioi780387.
    PROiO18404.

    Gene expression databases

    BgeeiO18404.
    GenevisibleiO18404. DM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta peptide-binding protein."
      Torroja L., Ortuno-Sahagun D., Ferrus A., Haemmerle B., Barbas J.A.
      J. Cell Biol. 141:1009-1018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF LEU-33 AND PHE-120.
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    6. "Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD."
      Shafqat N., Marschall H.U., Filling C., Nordling E., Wu X.Q., Bjork L., Thyberg J., Martensson E., Salim S., Jornvall H., Oppermann U.
      Biochem. J. 376:49-60(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "The lipid-droplet proteome reveals that droplets are a protein-storage depot."
      Cermelli S., Guo Y., Gross S.P., Welte M.A.
      Curr. Biol. 16:1783-1795(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    8. "Proteomic identification of PKC-mediated expression of 20E-induced protein in Drosophila melanogaster."
      Sun Y., An S., Henrich V.C., Sun X., Song Q.
      J. Proteome Res. 6:4478-4488(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY 20-HYDROXYECDYSONE.

    Entry informationi

    Entry nameiHCD2_DROME
    AccessioniPrimary (citable) accession number: O18404
    Secondary accession number(s): G7H840, Q059C3, Q8MRC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 1, 1998
    Last modified: July 22, 2015
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.