HCD2_DROME
ID HCD2_DROME Reviewed; 255 AA.
AC O18404; G7H840; Q059C3; Q8MRC1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2 {ECO:0000303|PubMed:9585418};
DE EC=1.1.1.35 {ECO:0000269|PubMed:12917011};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 10;
DE Short=17-beta-HSD 10 {ECO:0000303|PubMed:12917011};
DE EC=1.1.1.51 {ECO:0000269|PubMed:12917011};
DE EC=1.1.1.62 {ECO:0000269|PubMed:12917011};
DE AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
DE AltName: Full=Hydroxysteroid dehydrogenase {ECO:0000305|PubMed:12917011};
DE EC=1.1.1.- {ECO:0000269|PubMed:12917011};
DE EC=1.1.1.53 {ECO:0000269|PubMed:12917011};
DE AltName: Full=Mitochondrial ribonuclease P protein 2;
DE Short=Mitochondrial RNase P protein 2;
DE AltName: Full=Scully protein {ECO:0000303|PubMed:9585418};
DE AltName: Full=Type II HADH;
GN Name=scu; ORFNames=CG7113;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-33 AND PHE-120.
RC STRAIN=Canton-S;
RX PubMed=9585418; DOI=10.1083/jcb.141.4.1009;
RA Torroja L., Ortuno-Sahagun D., Ferrus A., Haemmerle B., Barbas J.A.;
RT "Scully, an essential gene of Drosophila, is homologous to mammalian
RT mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta
RT peptide-binding protein.";
RL J. Cell Biol. 141:1009-1018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12917011; DOI=10.1042/bj20030877;
RA Shafqat N., Marschall H.U., Filling C., Nordling E., Wu X.Q., Bjork L.,
RA Thyberg J., Martensson E., Salim S., Jornvall H., Oppermann U.;
RT "Expanded substrate screenings of human and Drosophila type 10 17beta-
RT hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile
RT acid and steroid hormone metabolism: characterization of multifunctional
RT 3alpha/7alpha/7beta/17beta/20beta/21-HSD.";
RL Biochem. J. 376:49-60(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16979555; DOI=10.1016/j.cub.2006.07.062;
RA Cermelli S., Guo Y., Gross S.P., Welte M.A.;
RT "The lipid-droplet proteome reveals that droplets are a protein-storage
RT depot.";
RL Curr. Biol. 16:1783-1795(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY 20-HYDROXYECDYSONE.
RX PubMed=17924685; DOI=10.1021/pr0705183;
RA Sun Y., An S., Henrich V.C., Sun X., Song Q.;
RT "Proteomic identification of PKC-mediated expression of 20E-induced protein
RT in Drosophila melanogaster.";
RL J. Proteome Res. 6:4478-4488(2007).
CC -!- FUNCTION: Versatile enzyme presenting two types of activity; L-3-
CC hydroxyacyl-CoA dehydrogenase ((3S)-3-hydroxyacyl-CoA dehydrogenase)
CC activity and hydroxysteroid dehydrogenase (HSD) activity with a wide
CC substrate spectrum. As a (3S)-3-hydroxyacyl-CoA dehydrogenase, it
CC functions in the third step of the fatty acid beta-oxidation pathway, a
CC major metabolic process in which fatty acids are oxidized to provide a
CC significant source of energy, while also generating acyl-CoA
CC metabolites used by many metabolic routes (PubMed:12917011) (Probable).
CC As a HSD, it functions in the degradation pathways of glucocorticoids
CC and sex steroids and epimerization of bile acids; catalyzes the beta-
CC oxidation at position 17 of androgens and estrogens, has 3-alpha-
CC hydroxysteroid dehydrogenase activity with androsterone, and carries
CC out oxidative conversions of 7-beta-hydroxylated bile acids like
CC ursodeoxycholate or isoursodeoxycholate (also known as 3-beta,7-beta-
CC dihydroxy-5-beta-cholan-24-oate or 7-beta-hydroxyisolithocholate,
CC respectively). Also exhibits 20-beta-OH and 21-OH dehydrogenase
CC activities with C21 steroids (PubMed:12917011). Required for cell
CC survival during embryonic development. May play a role in germline
CC formation (PubMed:9585418, PubMed:12917011).
CC {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:9585418,
CC ECO:0000305|PubMed:9585418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.51;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + ursodeoxycholate = 7-oxolithocholate + H(+) + NADH;
CC Xref=Rhea:RHEA:42028, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta,7beta-dihydroxy-5beta-cholan-24-oate + NAD(+) = 3beta-
CC hydroxy-7-oxo-5beta-cholan-24-oate + H(+) + NADH;
CC Xref=Rhea:RHEA:42024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78602, ChEBI:CHEBI:78603;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-dehydrocorticosterone + NAD(+) = H(+) + NADH + pregn-4-ene-
CC 3,11,20,21-tetraone; Xref=Rhea:RHEA:42020, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600,
CC ChEBI:CHEBI:78601; Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cortisone + NAD(+) = 17alpha-hydroxypregn-4-en-3,11,20-trione-
CC 21-al + H(+) + NADH; Xref=Rhea:RHEA:42016, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16962, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78596; Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-ene-
CC 3,20,21-trione + H(+) + NADH; Xref=Rhea:RHEA:42012,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78595;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-pregnane-
CC 3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28952, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78594; Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:12917011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993;
CC Evidence={ECO:0000269|PubMed:12917011};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH
CC 6.4 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=101 uM for (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA)
CC (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12917011};
CC KM=37.3 uM for androsterone (in the presence of 1 mM NAD, at pH 9.3
CC and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=12.3 uM for 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-
CC dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and
CC 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=11.1 uM for 17-beta-estradiol (in the presence of 1 mM NAD, at pH
CC 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=9 uM for 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM
CC NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=3 uM for 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as
CC isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence
CC of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12917011};
CC KM=32.5 uM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0
CC and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=64.4 uM for NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at
CC pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC KM=124 uM for NAD (in the presence of aldosterone, at pH 9.3 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12917011};
CC pH dependence:
CC Optimum pH is 9.3 for the dehydrogenase reaction, and 6.4 for the
CC reductase reaction. {ECO:0000269|PubMed:12917011};
CC -!- SUBUNIT: Multimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=Localizes to
CC the lipid droplet fraction in early embryos (PubMed:16979555). Co-
CC localization with mitochondrial markers for human, but not for the
CC Drosophila form (PubMed:12917011). {ECO:0000269|PubMed:12917011,
CC ECO:0000269|PubMed:16979555}.
CC -!- TISSUE SPECIFICITY: Found in many tissues including CNS, imaginal disks
CC and salivary glands. Highest expression in both embryonic gonadal
CC primordia and mature ovaries and testes. {ECO:0000269|PubMed:9585418}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development. In
CC adults, expression is higher in females than in males.
CC {ECO:0000269|PubMed:9585418}.
CC -!- INDUCTION: By 20-hydroxyecdysone. {ECO:0000269|PubMed:17924685}.
CC -!- DISRUPTION PHENOTYPE: Embryonic and pupal lethal. Male mutants show
CC small testes and degenerating spermatocytes with a large accumulation
CC of small fat-containing vesicles in the cytoplasm and almost no
CC mitochondria. Null mutant photoreceptors fail to differentiate
CC normally, are unable to form proper rhabdomeres and present smaller
CC mitochondria with fewer, but swollen crestae, than wild-type cells.
CC {ECO:0000269|PubMed:9585418}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AET07646.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y15102; CAA75377.1; -; mRNA.
DR EMBL; AE014298; AAF48797.1; -; Genomic_DNA.
DR EMBL; AY121672; AAM51999.1; -; mRNA.
DR EMBL; BT029045; ABJ16978.1; -; mRNA.
DR EMBL; BT132763; AET07646.1; ALT_INIT; mRNA.
DR RefSeq; NP_523396.1; NM_078672.5.
DR AlphaFoldDB; O18404; -.
DR SMR; O18404; -.
DR BioGRID; 59109; 78.
DR DIP; DIP-17092N; -.
DR IntAct; O18404; 6.
DR STRING; 7227.FBpp0074285; -.
DR SwissLipids; SLP:000000795; -.
DR PaxDb; O18404; -.
DR PRIDE; O18404; -.
DR DNASU; 32789; -.
DR EnsemblMetazoa; FBtr0074511; FBpp0074285; FBgn0021765.
DR GeneID; 32789; -.
DR KEGG; dme:Dmel_CG7113; -.
DR CTD; 32789; -.
DR FlyBase; FBgn0021765; scu.
DR VEuPathDB; VectorBase:FBgn0021765; -.
DR eggNOG; KOG1199; Eukaryota.
DR GeneTree; ENSGT00940000155170; -.
DR HOGENOM; CLU_010194_42_0_1; -.
DR InParanoid; O18404; -.
DR OMA; QGIRVCT; -.
DR PhylomeDB; O18404; -.
DR Reactome; R-DME-70895; Branched-chain amino acid catabolism.
DR SignaLink; O18404; -.
DR BioGRID-ORCS; 32789; 0 hits in 1 CRISPR screen.
DR ChiTaRS; scu; fly.
DR GenomeRNAi; 32789; -.
DR PRO; PR:O18404; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0021765; Expressed in seminal fluid secreting gland and 19 other tissues.
DR ExpressionAtlas; O18404; baseline and differential.
DR Genevisible; O18404; DM.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047022; F:7-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:FlyBase.
DR GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IDA:FlyBase.
DR GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:FlyBase.
DR GO; GO:0106282; F:isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IDA:FlyBase.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:FlyBase.
DR GO; GO:0106283; F:ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:FlyBase.
DR GO; GO:0008209; P:androgen metabolic process; IDA:FlyBase.
DR GO; GO:0008205; P:ecdysone metabolic process; IDA:FlyBase.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:FlyBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:FlyBase.
DR GO; GO:0090646; P:mitochondrial tRNA processing; IMP:FlyBase.
DR GO; GO:0008202; P:steroid metabolic process; IDA:FlyBase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..255
FT /note="3-hydroxyacyl-CoA dehydrogenase type-2"
FT /id="PRO_0000054813"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT MUTAGEN 33
FT /note="L->Q: Lethal allele."
FT /evidence="ECO:0000269|PubMed:9585418"
FT MUTAGEN 120
FT /note="F->I: Lethal allele."
FT /evidence="ECO:0000269|PubMed:9585418"
FT CONFLICT 134
FT /note="E -> K (in Ref. 4; AAM51999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 26905 MW; F58690643FA0FD03 CRC64;
MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD KVVFVPVDVT
SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN VAHRLEDFQR VININTVGTF
NVIRLSAGLM GANEPNQDGQ RGVIVNTASV AAFDGQIGQA AYSASKAAVV GMTLPIARDL
STQGIRICTI APGLFNTPML AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL
NGEVIRIDGA LRMMP
