SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O18404

- HCD2_DROME

UniProt

O18404 - HCD2_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
3-hydroxyacyl-CoA dehydrogenase type-2
Gene
scu, CG7113
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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)
  3. KM=37.3 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)
  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)
  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)
  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)
  7. KM=3 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)
  8. KM=32.5 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)
  9. KM=64.4 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)
  10. KM=124 µM for NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491Substrate By similarity
Active sitei162 – 1621Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 3126NAD By similarity
Add
BLAST

GO - Molecular functioni

  1. 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
  2. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
  3. 7-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: FlyBase
  4. acetoacetyl-CoA reductase activity Source: FlyBase
  5. estradiol 17-beta-dehydrogenase activity Source: FlyBase
  6. steroid dehydrogenase activity Source: FlyBase
  7. testosterone dehydrogenase (NAD+) activity Source: FlyBase
  8. testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

GO - Biological processi

  1. acyl-CoA metabolic process Source: FlyBase
  2. androgen metabolic process Source: FlyBase
  3. ecdysone metabolic process Source: FlyBase
  4. estrogen metabolic process Source: FlyBase
  5. fatty acid metabolic process Source: FlyBase
  6. steroid metabolic process Source: FlyBase
  7. 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_216692. 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: 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

  1. cytosol Source: FlyBase
  2. lipid particle Source: FlyBase
  3. microtubule associated complex Source: FlyBase
  4. 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-2
PRO_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.

Interactioni

Subunit structurei

Multimer Reviewed prediction.

Protein-protein interaction databases

BioGridi59109. 74 interactions.
DIPiDIP-17092N.
IntActiO18404. 2 interactions.
MINTiMINT-289527.

Structurei

3D structure databases

ProteinModelPortaliO18404.
SMRiO18404. Positions 2-255.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00710000106273.
InParanoidiO18404.
KOiK08683.
OMAiLMGANEP.
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

MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD    50
KVVFVPVDVT SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN 100
VAHRLEDFQR VININTVGTF NVIRLSAGLM GANEPNQDGQ RGVIVNTASV 150
AAFDGQIGQA AYSASKAAVV GMTLPIARDL STQGIRICTI APGLFNTPML 200
AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL NGEVIRIDGA 250
LRMMP 255
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341E → K in AAM51999. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_078672.4.
UniGeneiDm.7957.

Genome annotation databases

EnsemblMetazoaiFBtr0074511; FBpp0074285; FBgn0021765.
GeneIDi32789.
KEGGidme:Dmel_CG7113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqi NP_523396.1. NM_078672.4.
UniGenei Dm.7957.

3D structure databases

ProteinModelPortali O18404.
SMRi O18404. Positions 2-255.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 59109. 74 interactions.
DIPi DIP-17092N.
IntActi O18404. 2 interactions.
MINTi MINT-289527.

Proteomic databases

PaxDbi O18404.
PRIDEi O18404.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074511 ; FBpp0074285 ; FBgn0021765 .
GeneIDi 32789.
KEGGi dme:Dmel_CG7113.

Organism-specific databases

CTDi 32789.
FlyBasei FBgn0021765. scu.

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00710000106273.
InParanoidi O18404.
KOi K08683.
OMAi LMGANEP.
OrthoDBi EOG7JT6X7.
PhylomeDBi O18404.

Enzyme and pathway databases

Reactomei REACT_216692. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSi scu. drosophila.
GenomeRNAii 32789.
NextBioi 780387.
PROi O18404.

Gene expression databases

Bgeei O18404.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 123 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