HCD2_BOVIN
ID HCD2_BOVIN Reviewed; 261 AA.
AC O02691; Q2TBG6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
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=HADH2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=9061028; DOI=10.1016/s0167-4781(96)00171-6;
RA Furuta S., Kobayashi A., Miyazawa S., Hashimoto T.;
RT "Cloning and expression of cDNA for a newly identified isozyme of bovine
RT liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria.";
RL Biochim. Biophys. Acta 1350:317-324(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; AB002156; BAA19510.1; -; mRNA.
DR EMBL; BC110264; AAI10265.1; -; mRNA.
DR RefSeq; NP_776759.1; NM_174334.3.
DR AlphaFoldDB; O02691; -.
DR SMR; O02691; -.
DR IntAct; O02691; 1.
DR STRING; 9913.ENSBTAP00000023642; -.
DR PaxDb; O02691; -.
DR PeptideAtlas; O02691; -.
DR PRIDE; O02691; -.
DR Ensembl; ENSBTAT00000023642; ENSBTAP00000023642; ENSBTAG00000017779.
DR GeneID; 281809; -.
DR KEGG; bta:281809; -.
DR CTD; 3028; -.
DR VEuPathDB; HostDB:ENSBTAG00000017779; -.
DR VGNC; VGNC:29969; HSD17B10.
DR eggNOG; KOG1199; Eukaryota.
DR GeneTree; ENSGT00940000155170; -.
DR HOGENOM; CLU_010194_42_0_1; -.
DR InParanoid; O02691; -.
DR OMA; QGIRVCT; -.
DR OrthoDB; 1074094at2759; -.
DR TreeFam; TF354307; -.
DR BRENDA; 1.1.1.135; 908.
DR Reactome; R-BTA-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00221; -.
DR UniPathway; UPA00364; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000017779; Expressed in liver and 106 other tissues.
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; IEA:Ensembl.
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: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; IBA:GO_Central.
DR GO; GO:0106282; F:isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; ISS:UniProtKB.
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: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; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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 Acetylation; Direct protein sequencing; Fatty acid metabolism;
KW Lipid metabolism; Mitochondrion; Mitochondrion nucleoid; NAD;
KW Oxidoreductase; Reference proteome; 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_0000054809"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
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 64
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:0000250|UniProtKB:Q99714"
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"
SQ SEQUENCE 261 AA; 27140 MW; 8C7572B6A9A49780 CRC64;
MAAACRSVKG LVALITGGAS GLGLATAERL VGQGATAVLL DLPNSDGETQ AKKLGKSCAF
APADVTSEKD VQAALTLARE KFGRVDVAVN CAGIAVASKT YNLKKSQAHT LEDFQRVINV
NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL
PIARDLAPMG IRVMTIAPGL FGTPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQAI
IENSFLNGEV IRLDGAIRMQ P
