ID   HCD2_RAT                Reviewed;         261 AA.
AC   O70351; Q9QYD4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
DE            EC=1.1.1.35 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=17-beta-estradiol 17-dehydrogenase;
DE            EC=1.1.1.62 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=2-methyl-3-hydroxybutyryl-CoA dehydrogenase;
DE            Short=MHBD;
DE   AltName: Full=3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+));
DE            EC=1.1.1.239 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
DE            EC=1.1.1.178 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
DE   AltName: Full=3alpha(or 20beta)-hydroxysteroid dehydrogenase;
DE            EC=1.1.1.53 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=7-alpha-hydroxysteroid dehydrogenase;
DE            EC=1.1.1.159 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein;
DE   AltName: Full=Mitochondrial ribonuclease P protein 2;
DE            Short=Mitochondrial RNase P protein 2;
DE   AltName: Full=Short chain dehydrogenase/reductase family 5C member 1;
DE   AltName: Full=Short-chain type dehydrogenase/reductase XH98G2;
DE   AltName: Full=Type II HADH;
GN   Name=Hsd17b10; Synonyms=Erab, Hadh2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Gunn-Moore F.J., Tavare J.M.;
RT   "Rattus norvegicus amyloid beta-peptide binding protein (ERAB) mRNA.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Yang S.-Y., He X.-Y.;
RT   "Molecular cloning and characterization of the cDNA of rat brain short
RT   chain L-3-hydroxyacyl-CoA dehydrogenase.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 117-130 AND 193-212, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
RC   TISSUE=Brain;
RX   PubMed=11023795; DOI=10.1006/jmbi.2000.4139;
RA   Powell A.J., Read J.A., Banfield M.J., Gunn-Moore F., Yan S.D.,
RA   Lustbader J., Stern A.R., Stern D.M., Brady R.L.;
RT   "Recognition of structurally diverse substrates by type II 3-hydroxyacyl-
RT   CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase
RT   (ABAD).";
RL   J. Mol. Biol. 303:311-327(2000).
CC   -!- FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty
CC       acid, branched-chain amino acid and steroid metabolism. Acts as (S)-3-
CC       hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-
CC       oxidation, a major degradation pathway of fatty acids. Catalyzes the
CC       third step in the beta-oxidation cycle, namely the reversible
CC       conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially
CC       accepts straight medium- and short-chain acyl-CoA substrates with
CC       highest efficiency for (3S)-hydroxybutanoyl-CoA. Acts as 3-hydroxy-2-
CC       methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic
CC       pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into
CC       2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway.
CC       Has hydroxysteroid dehydrogenase activity toward steroid hormones and
CC       bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and
CC       21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes
CC       allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is
CC       known to be critical for the activation of gamma-aminobutyric acid
CC       receptors (GABAARs) chloride channel. Has phospholipase C-like activity
CC       toward cardiolipin and its oxidized species. Likely oxidizes the 2'-
CC       hydroxyl in the head group of cardiolipin to form a ketone intermediate
CC       that undergoes nucleophilic attack by water and fragments into
CC       diacylglycerol, dihydroxyacetone and orthophosphate. Has higher
CC       affinity for cardiolipin with oxidized fatty acids and may degrade
CC       these species during the oxidative stress response to protect cells
CC       from apoptosis. By interacting with intracellular amyloid-beta, it may
CC       contribute to the neuronal dysfunction associated with Alzheimer
CC       disease (AD). Essential for structural and functional integrity of
CC       mitochondria. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- FUNCTION: In addition to mitochondrial dehydrogenase activity,
CC       moonlights as a component of mitochondrial ribonuclease P, a complex
CC       that cleaves tRNA molecules in their 5'-ends. Together with
CC       TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P,
CC       named MRPP1-MRPP2 subcomplex, which displays functions that are
CC       independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex
CC       catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at
CC       position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2
CC       acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts
CC       as a tRNA maturation platform: following 5'-end cleavage by the
CC       mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex
CC       enhances the efficiency of 3'-processing catalyzed by ELAC2, retains
CC       the tRNA product after ELAC2 processing and presents the nascent tRNA
CC       to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme.
CC       Associates with mitochondrial DNA complexes at the nucleoids to
CC       initiate RNA processing and ribosome assembly.
CC       {ECO:0000250|UniProtKB:Q99714}.
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3-
CC         oxobutanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:13281,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57312, ChEBI:CHEBI:57335,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.178;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13282;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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;
CC         EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-
CC         cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.159;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31197;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC         + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31161;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-
CC         pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78594;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-
CC         pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-
CC         ene-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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH;
CC         Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
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:0000250|UniProtKB:Q99714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025;
CC         Evidence={ECO:0000250|UniProtKB:Q99714};
CC   -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SUBUNIT: Homotetramer. Component of mitochondrial ribonuclease P, a
CC       complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3.
CC       Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the
CC       mitochondrial ribonuclease P complex. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}.
CC       Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF049878; AAC05747.1; -; mRNA.
DR   EMBL; AF069770; AAF14853.1; -; mRNA.
DR   RefSeq; NP_113870.1; NM_031682.1.
DR   PDB; 1E3S; X-ray; 2.00 A; A/B/C/D=2-261.
DR   PDB; 1E3W; X-ray; 2.00 A; A/B/C/D=2-261.
DR   PDB; 1E6W; X-ray; 1.70 A; A/B/C/D=2-261.
DR   PDBsum; 1E3S; -.
DR   PDBsum; 1E3W; -.
DR   PDBsum; 1E6W; -.
DR   AlphaFoldDB; O70351; -.
DR   SMR; O70351; -.
DR   BioGRID; 248908; 4.
DR   IntAct; O70351; 2.
DR   MINT; O70351; -.
DR   STRING; 10116.ENSRNOP00000043608; -.
DR   GlyGen; O70351; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O70351; -.
DR   PhosphoSitePlus; O70351; -.
DR   SwissPalm; O70351; -.
DR   jPOST; O70351; -.
DR   PaxDb; 10116-ENSRNOP00000043608; -.
DR   GeneID; 63864; -.
DR   KEGG; rno:63864; -.
DR   AGR; RGD:69231; -.
DR   CTD; 3028; -.
DR   RGD; 69231; Hsd17b10.
DR   eggNOG; KOG1199; Eukaryota.
DR   InParanoid; O70351; -.
DR   OrthoDB; 149879at2759; -.
DR   PhylomeDB; O70351; -.
DR   Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR   SABIO-RK; O70351; -.
DR   UniPathway; UPA00221; -.
DR   UniPathway; UPA00364; -.
DR   UniPathway; UPA00659; -.
DR   EvolutionaryTrace; O70351; -.
DR   PRO; PR:O70351; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043527; C:tRNA methyltransferase complex; ISO:RGD.
DR   GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IDA:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; IDA:RGD.
DR   GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106281; F:chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase [NAD(P)] activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0106282; F:isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR   GO; GO:0005496; F:steroid binding; IDA:RGD.
DR   GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0106283; F:ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0008209; P:androgen metabolic process; ISS:UniProtKB.
DR   GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0062173; P:brexanolone metabolic process; ISS:UniProtKB.
DR   GO; GO:0008207; P:C21-steroid hormone metabolic process; ISS:UniProtKB.
DR   GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006550; P:isoleucine catabolic process; ISS:UniProtKB.
DR   GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; ISS:UniProtKB.
DR   GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR   GO; GO:0070901; P:mitochondrial tRNA methylation; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR   CDD; cd05371; HSD10-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43658:SF8; 3-HYDROXYACYL-COA DEHYDROGENASE TYPE-2; 1.
DR   PANTHER; PTHR43658; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Fatty acid metabolism; Lipid metabolism; Mitochondrion;
KW   Mitochondrion nucleoid; NAD; Oxidoreductase; Reference proteome;
KW   Steroid metabolism; tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   CHAIN           2..261
FT                   /note="3-hydroxyacyl-CoA dehydrogenase type-2"
FT                   /id="PRO_0000054812"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:11023795"
FT   BINDING         20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11023795"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99714"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         53
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   MOD_RES         212
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O08756"
FT   CONFLICT        5
FT                   /note="V -> C (in Ref. 2; AAF14853)"
FT                   /evidence="ECO:0000305"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           47..54
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           68..82
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           123..137
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           157..160
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           166..186
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   TURN            204..206
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   HELIX           230..242
FT                   /evidence="ECO:0007829|PDB:1E6W"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:1E6W"
SQ   SEQUENCE   261 AA;  27246 MW;  117FD723B11EA227 CRC64;
     MAAAVRSVKG LVAVITGGAS GLGLSTAKRL VGQGATAVLL DVPNSEGETE AKKLGGNCIF
     APANVTSEKE VQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHEKKNQVHT LEDFQRVINV
     NLIGTFNVIR LVAGVMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL
     PIARDLAPIG IRVVTIAPGL FATPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQMV
     IENPFLNGEV IRLDGAIRMQ P
//