HCD2_RAT
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 03-AUG-2022, entry version 156.
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-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: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-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: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 iPTMnet; O70351; -.
DR PhosphoSitePlus; O70351; -.
DR jPOST; O70351; -.
DR PaxDb; O70351; -.
DR PRIDE; O70351; -.
DR GeneID; 63864; -.
DR KEGG; rno:63864; -.
DR CTD; 3028; -.
DR RGD; 69231; Hsd17b10.
DR eggNOG; KOG1199; Eukaryota.
DR InParanoid; O70351; -.
DR OrthoDB; 1074094at2759; -.
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; IDA:RGD.
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 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 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 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
