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HCD2_HUMAN
ID   HCD2_HUMAN              Reviewed;         261 AA.
AC   Q99714; Q5H927; Q6IBS9; Q8TCV9; Q96HD5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 223.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
DE            EC=1.1.1.35 {ECO:0000269|PubMed:10600649, ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:9553139};
DE   AltName: Full=17-beta-estradiol 17-dehydrogenase;
DE            EC=1.1.1.62 {ECO:0000269|PubMed:10600649, ECO:0000269|PubMed:12917011};
DE   AltName: Full=2-methyl-3-hydroxybutyryl-CoA dehydrogenase {ECO:0000303|PubMed:16148061};
DE            Short=MHBD {ECO:0000303|PubMed:16148061};
DE   AltName: Full=3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+));
DE            EC=1.1.1.239 {ECO:0000269|PubMed:12917011};
DE   AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
DE            EC=1.1.1.178 {ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:19706438, ECO:0000269|PubMed:20077426};
DE   AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
DE   AltName: Full=3alpha(or 20beta)-hydroxysteroid dehydrogenase;
DE            EC=1.1.1.53 {ECO:0000269|PubMed:12917011};
DE   AltName: Full=7-alpha-hydroxysteroid dehydrogenase;
DE            EC=1.1.1.159 {ECO:0000269|PubMed:12917011};
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, MRPP2, SCHAD, SDR5C1, XH98G2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9338779; DOI=10.1038/39522;
RA   Yan S.D., Fu J., Soto C., Chen X., Zhu H., Al-Mohanna F., Collinson K.,
RA   Zhu A., Stern E., Saido T., Tohyama M., Ogawa S., Roher A., Stern D.;
RT   "An intracellular protein that binds amyloid-beta peptide and mediates
RT   neurotoxicity in Alzheimer's disease.";
RL   Nature 389:689-695(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Zhuchenko O.P., Wehnert M., Bailey J., Sun Z.S., Lee C.C.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9671743; DOI=10.1073/pnas.95.15.8709;
RA   Miller A.P., Willard H.F.;
RT   "Chromosomal basis of X chromosome inactivation: identification of a
RT   multigene domain in Xp11.21-p11.22 that escapes X inactivation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8709-8714(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RC   TISSUE=Brain;
RX   PubMed=9553139; DOI=10.1074/jbc.273.17.10741;
RA   He X.Y., Schulz H., Yang S.Y.;
RT   "A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an
RT   amyloid beta-peptide-binding protein involved in Alzheimer's disease.";
RL   J. Biol. Chem. 273:10741-10746(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 51-246.
RA   Deininger M.H., Meyermann R., Schluesener H.J.;
RT   "Expression, release and induction of endoplasmic reticulum-associated
RT   amyloid beta-binding protein in brain disease.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=10600649; DOI=10.1042/bj3450139;
RA   He X.Y., Yang Y.Z., Schulz H., Yang S.Y.;
RT   "Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase
RT   activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA
RT   dehydrogenase.";
RL   Biochem. J. 345:139-143(2000).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND PATHWAY.
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   [12]
RP   INVOLVEMENT IN HSD10MD.
RX   PubMed=17236142; DOI=10.1086/511527;
RA   Lenski C., Kooy R.F., Reyniers E., Loessner D., Wanders R.J.A.,
RA   Winnepenninckx B., Hellebrand H., Engert S., Schwartz C.E., Meindl A.,
RA   Ramser J.;
RT   "The reduced expression of the HADH2 protein causes X-linked mental
RT   retardation, choreoathetosis, and abnormal behavior.";
RL   Am. J. Hum. Genet. 80:372-377(2007).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH KIAA0391
RP   AND TRMT10C, AND SUBCELLULAR LOCATION.
RX   PubMed=18984158; DOI=10.1016/j.cell.2008.09.013;
RA   Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C., Rossmanith W.;
RT   "RNase P without RNA: identification and functional reconstitution of the
RT   human mitochondrial tRNA processing enzyme.";
RL   Cell 135:462-474(2008).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   FUNCTION, INTERACTION WITH TRMT10C, AND MUTAGENESIS OF SER-20 AND LYS-172.
RX   PubMed=23042678; DOI=10.1093/nar/gks910;
RA   Vilardo E., Nachbagauer C., Buzet A., Taschner A., Holzmann J.,
RA   Rossmanith W.;
RT   "A subcomplex of human mitochondrial RNase P is a bifunctional
RT   methyltransferase--extensive moonlighting in mitochondrial tRNA
RT   biogenesis.";
RL   Nucleic Acids Res. 40:11583-11593(2012).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=24703694; DOI=10.1016/j.cmet.2014.03.013;
RA   Bogenhagen D.F., Martin D.W., Koller A.;
RT   "Initial steps in RNA processing and ribosome assembly occur at
RT   mitochondrial DNA nucleoids.";
RL   Cell Metab. 19:618-629(2014).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS
RP   HSD10MD GLY-86; CYS-130 AND HIS-165.
RX   PubMed=26338420; DOI=10.1101/gad.268482.115;
RA   Boynton T.O., Shimkets L.J.;
RT   "Myxococcus CsgA, Drosophila Sniffer, and human HSD10 are cardiolipin
RT   phospholipases.";
RL   Genes Dev. 29:1903-1914(2015).
RN   [19]
RP   INVOLVEMENT IN HSD10MD.
RX   PubMed=25575635; DOI=10.1016/j.mito.2014.12.005;
RA   Chatfield K.C., Coughlin C.R. II, Friederich M.W., Gallagher R.C.,
RA   Hesselberth J.R., Lovell M.A., Ofman R., Swanson M.A., Thomas J.A.,
RA   Wanders R.J., Wartchow E.P., Van Hove J.L.;
RT   "Mitochondrial energy failure in HSD10 disease is due to defective mtDNA
RT   transcript processing.";
RL   Mitochondrion 21:1-10(2015).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [21]
RP   FUNCTION, AND INTERACTION WITH TRMT10C.
RX   PubMed=29040705; DOI=10.1093/nar/gkx902;
RA   Reinhard L., Sridhara S., Haellberg B.M.;
RT   "The MRPP1/MRPP2 complex is a tRNA-maturation platform in human
RT   mitochondria.";
RL   Nucleic Acids Res. 45:12469-12480(2017).
RN   [22] {ECO:0007744|PDB:1U7T}
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
RX   PubMed=15342248; DOI=10.1016/j.jmb.2004.07.071;
RA   Kissinger C.R., Rejto P.A., Pelletier L.A., Thomson J.A., Showalter R.E.,
RA   Abreo M.A., Agree C.S., Margosiak S., Meng J.J., Aust R.M., Vanderpool D.,
RA   Li B., Tempczyk-Russell A., Villafranca J.E.;
RT   "Crystal structure of human ABAD/HSD10 with a bound inhibitor: implications
RT   for design of Alzheimer's disease therapeutics.";
RL   J. Mol. Biol. 342:943-952(2004).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=15087549; DOI=10.1126/science.1091230;
RA   Lustbader J.W., Cirilli M., Lin C., Xu H.W., Takuma K., Wang N.,
RA   Caspersen C., Chen X., Pollak S., Chaney M., Trinchese F., Liu S.,
RA   Gunn-Moore F., Lue L.-F., Walker D.G., Kuppusamy P., Zewier Z.L.,
RA   Arancio O., Stern D., Yan S.-S., Wu H.;
RT   "ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's
RT   disease.";
RL   Science 304:448-452(2004).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBUNIT, VARIANTS HSD10MD GLY-86; CYS-130 AND HIS-165, AND CHARACTERIZATION
RP   OF VARIANTS HSD10MD GLY-86; CYS-130 AND HIS-165.
RX   PubMed=20077426; DOI=10.1002/emmm.200900055;
RA   Rauschenberger K., Schoeler K., Sass J.O., Sauer S., Djuric Z., Rumig C.,
RA   Wolf N.I., Okun J.G., Koelker S., Schwarz H., Fischer C., Grziwa B.,
RA   Runz H., Nuemann A., Shafqat N., Kavanagh K.L., Haemmerling G.,
RA   Wanders R.J., Shield J.P., Wendel U., Stern D., Nawroth P., Hoffmann G.F.,
RA   Bartram C.R., Arnold B., Bierhaus A., Oppermann U., Steinbeisser H.,
RA   Zschocke J.;
RT   "A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type 10 is
RT   required for mitochondrial integrity and cell survival.";
RL   EMBO Mol. Med. 2:51-62(2010).
RN   [25]
RP   VARIANTS HSD10MD VAL-122 AND CYS-130.
RX   PubMed=12696021; DOI=10.1086/375116;
RA   Ofman R., Ruiter J.P.N., Feenstra M., Duran M., Poll-The B.T., Zschocke J.,
RA   Ensenauer R., Lehnert W., Sass J.O., Sperl W., Wanders R.J.A.;
RT   "2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by
RT   mutations in the HADH2 gene.";
RL   Am. J. Hum. Genet. 72:1300-1307(2003).
RN   [26]
RP   VARIANTS HSD10MD CYS-130 AND SER-247, AND CHARACTERIZATION OF VARIANT
RP   HSD10MD SER-247.
RX   PubMed=16148061; DOI=10.1203/01.pdr.0000176916.94328.cd;
RA   Perez-Cerda C., Garcia-Villoria J., Ofman R., Sala P.R., Merinero B.,
RA   Ramos J., Garcia-Silva M.T., Beseler B., Dalmau J., Wanders R.J.A.,
RA   Ugarte M., Ribes A.;
RT   "2-methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-linked
RT   inborn error of isoleucine metabolism that may mimic a mitochondrial
RT   disease.";
RL   Pediatr. Res. 58:488-491(2005).
RN   [27]
RP   ERRATUM OF PUBMED:16148061.
RA   Perez-Cerda C., Garcia-Villoria J., Ofman R., Sala P.R., Merinero B.,
RA   Ramos J., Garcia-Silva M.T., Beseler B., Dalmau J., Wanders R.J.,
RA   Ugarte M., Ribes A.;
RL   Pediatr. Res. 59:162-162(2006).
RN   [28]
RP   VARIANTS HSD10MD CYS-130; SER-210; GLN-226 AND SER-247, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=18996107; DOI=10.1016/j.clinbiochem.2008.10.006;
RA   Garcia-Villoria J., Navarro-Sastre A., Fons C., Perez-Cerda C.,
RA   Baldellou A., Fuentes-Castello M.A., Gonzalez I., Hernandez-Gonzalez A.,
RA   Fernandez C., Campistol J., Delpiccolo C., Cortes N., Messeguer A.,
RA   Briones P., Ribes A.;
RT   "Study of patients and carriers with 2-methyl-3-hydroxybutyryl-CoA
RT   dehydrogenase (MHBD) deficiency: difficulties in the diagnosis.";
RL   Clin. Biochem. 42:27-33(2009).
RN   [29]
RP   VARIANTS HSD10MD CYS-130 AND GLN-249, CHARACTERIZATION OF VARIANTS HSD10MD
RP   CYS-130 AND GLN-249, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND PATHWAY.
RX   PubMed=19706438; DOI=10.1073/pnas.0902377106;
RA   Yang S.Y., He X.Y., Olpin S.E., Sutton V.R., McMenamin J., Philipp M.,
RA   Denman R.B., Malik M.;
RT   "Mental retardation linked to mutations in the HSD17B10 gene interfering
RT   with neurosteroid and isoleucine metabolism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:14820-14824(2009).
RN   [30]
RP   VARIANT HSD10MD ALA-65.
RX   PubMed=22132097; DOI=10.1371/journal.pone.0027348;
RA   Seaver L.H., He X.Y., Abe K., Cowan T., Enns G.M., Sweetman L., Philipp M.,
RA   Lee S., Malik M., Yang S.Y.;
RT   "A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory
RT   epilepsy, choreoathetosis and learning disability.";
RL   PLoS ONE 6:E27348-E27348(2011).
RN   [31]
RP   VARIANTS HSD10MD CYS-130 AND HIS-165, CHARACTERIZATION OF VARIANT HSD10MD
RP   CYS-130, AND FUNCTION.
RX   PubMed=24549042; DOI=10.1093/hmg/ddu072;
RA   Deutschmann A.J., Amberger A., Zavadil C., Steinbeisser H., Mayr J.A.,
RA   Feichtinger R.G., Oerum S., Yue W.W., Zschocke J.;
RT   "Mutation or knock-down of 17beta-hydroxysteroid dehydrogenase type 10
RT   cause loss of MRPP1 and impaired processing of mitochondrial heavy strand
RT   transcripts.";
RL   Hum. Mol. Genet. 23:3618-3628(2014).
RN   [32]
RP   VARIANTS HSD10MD CYS-130; SER-210; GLN-226 AND SER-247, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBUNIT, MUTAGENESIS OF LYS-172, AND CHARACTERIZATION OF VARIANTS
RP   HSD10MD CYS-130; SER-210; GLN-226 AND SER-247.
RX   PubMed=25925575; DOI=10.1093/nar/gkv408;
RA   Vilardo E., Rossmanith W.;
RT   "Molecular insights into HSD10 disease: impact of SDR5C1 mutations on the
RT   human mitochondrial RNase P complex.";
RL   Nucleic Acids Res. 43:5112-5119(2015).
RN   [33]
RP   VARIANT HSD10MD GLU-212, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP   TRMT10C, AND CHARACTERIZATION OF VARIANT HSD10MD GLU-212.
RX   PubMed=26950678; DOI=10.1080/15476286.2016.1159381;
RA   Falk M.J., Gai X., Shigematsu M., Vilardo E., Takase R., McCormick E.,
RA   Christian T., Place E., Pierce E.A., Consugar M., Gamper H.B.,
RA   Rossmanith W., Hou Y.M.;
RT   "A novel HSD17B10 mutation impairing the activities of the mitochondrial
RT   RNase P complex causes X-linked intractable epilepsy and neurodevelopmental
RT   regression.";
RL   RNA Biol. 13:477-485(2016).
RN   [34]
RP   VARIANTS HSD10MD LEU-12 AND MET-176, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CHARACTERIZATION OF VARIANTS
RP   HSD10MD LEU-12 AND MET-176.
RX   PubMed=28888424; DOI=10.1016/j.bbadis.2017.09.002;
RA   Oerum S., Roovers M., Leichsenring M., Acquaviva-Bourdain C., Beermann F.,
RA   Gemperle-Britschgi C., Fouilhoux A., Korwitz-Reichelt A., Bailey H.J.,
RA   Droogmans L., Oppermann U., Sass J.O., Yue W.W.;
RT   "Novel patient missense mutations in the HSD17B10 gene affect dehydrogenase
RT   and mitochondrial tRNA modification functions of the encoded protein.";
RL   Biochim. Biophys. Acta 1863:3294-3302(2017).
CC   -!- FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty
CC       acid, branched-chain amino acid and steroid metabolism (PubMed:9553139,
CC       PubMed:10600649, PubMed:12917011, PubMed:20077426, PubMed:18996107,
CC       PubMed:19706438, PubMed:25925575, PubMed:26950678, PubMed:28888424).
CC       Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid
CC       beta-oxidation, a major degradation pathway of fatty acids. Catalyzes
CC       the 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 (PubMed:9553139,
CC       PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678).
CC       Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain
CC       amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-
CC       methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in
CC       isoleucine degradation pathway (PubMed:20077426, PubMed:18996107,
CC       PubMed:19706438). Has hydroxysteroid dehydrogenase activity toward
CC       steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-,
CC       17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy
CC       bile acids (PubMed:10600649, PubMed:12917011). 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 (PubMed:19706438,
CC       PubMed:28888424). Has phospholipase C-like activity toward cardiolipin
CC       and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head
CC       group of cardiolipin to form a ketone intermediate that undergoes
CC       nucleophilic attack by water and fragments into diacylglycerol,
CC       dihydroxyacetone and orthophosphate. Has higher affinity for
CC       cardiolipin with oxidized fatty acids and may degrade these species
CC       during the oxidative stress response to protect cells from apoptosis
CC       (PubMed:26338420). By interacting with intracellular amyloid-beta, it
CC       may contribute to the neuronal dysfunction associated with Alzheimer
CC       disease (AD) (PubMed:9338779). Essential for structural and functional
CC       integrity of mitochondria (PubMed:20077426).
CC       {ECO:0000269|PubMed:10600649, ECO:0000269|PubMed:12917011,
CC       ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:19706438,
CC       ECO:0000269|PubMed:20077426, ECO:0000269|PubMed:25925575,
CC       ECO:0000269|PubMed:26338420, ECO:0000269|PubMed:26950678,
CC       ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:9553139}.
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 (PubMed:18984158,
CC       PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424).
CC       Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial
CC       ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions
CC       that are independent of the ribonuclease P activity (PubMed:23042678,
CC       PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of
CC       N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9,
CC       respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic
CC       subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). The MRPP1-
CC       MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-
CC       end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-
CC       MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by
CC       ELAC2, retains the tRNA product after ELAC2 processing and presents the
CC       nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1
CC       enzyme (PubMed:29040705). Associates with mitochondrial DNA complexes
CC       at the nucleoids to initiate RNA processing and ribosome assembly.
CC       {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23042678,
CC       ECO:0000269|PubMed:24549042, ECO:0000269|PubMed:24703694,
CC       ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678,
CC       ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:29040705}.
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:10600649, ECO:0000269|PubMed:12917011,
CC         ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678,
CC         ECO:0000269|PubMed:9553139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC         Evidence={ECO:0000305|PubMed:12917011};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434;
CC         Evidence={ECO:0000305|PubMed:10600649, ECO:0000305|PubMed:12917011,
CC         ECO:0000305|PubMed:25925575, ECO:0000305|PubMed:26950678,
CC         ECO:0000305|PubMed:9553139};
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:0000269|PubMed:18996107, ECO:0000269|PubMed:19706438,
CC         ECO:0000269|PubMed:20077426};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13282;
CC         Evidence={ECO:0000305|PubMed:18996107, ECO:0000305|PubMed:19706438,
CC         ECO:0000305|PubMed:20077426};
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:0000269|PubMed:12917011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930;
CC         Evidence={ECO:0000305|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:0000305|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:10600649, ECO:0000269|PubMed:12917011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC         Evidence={ECO:0000305|PubMed:10600649, ECO:0000305|PubMed:12917011};
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:0000269|PubMed:12917011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410;
CC         Evidence={ECO:0000305|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:10600649, ECO:0000269|PubMed:12917011,
CC         ECO:0000269|PubMed:9553139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800;
CC         Evidence={ECO:0000305|PubMed:12917011};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801;
CC         Evidence={ECO:0000305|PubMed:10600649, ECO:0000305|PubMed:25925575,
CC         ECO:0000305|PubMed:9553139};
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:0000269|PubMed:9553139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196;
CC         Evidence={ECO:0000305};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31197;
CC         Evidence={ECO:0000305|PubMed:9553139};
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:0000269|PubMed:9553139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC         Evidence={ECO:0000305};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31161;
CC         Evidence={ECO:0000305|PubMed:9553139};
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:0000305|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:0000305|PubMed:12917011};
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:0000269|PubMed:19706438, ECO:0000269|PubMed:28888424};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981;
CC         Evidence={ECO:0000305|PubMed:19706438, ECO:0000305|PubMed:28888424};
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:0000305|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:0000305|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:0000305|PubMed:12917011};
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:0000269|PubMed:12917011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037;
CC         Evidence={ECO:0000305|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:0000305|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:0000305|PubMed:12917011};
CC   -!- ACTIVITY REGULATION: The phospholipase C-like activity toward
CC       cardiolipin is inhibited by amyloid-beta peptide.
CC       {ECO:0000269|PubMed:26338420}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH
CC         7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=85.2 uM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD,
CC         at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=41 uM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and
CC         25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=5 uM for 5-alpha-pregnan-20-beta-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=219 uM for isoursodeoxycholic acid (in the presence of 1 mM NAD,
CC         at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=36.4 uM for chenodeoxycholic acid (in the presence of 1 mM NAD, at
CC         pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=1.7 uM for dehydrocorticosterone (in the presence of 1 mM NAD, at
CC         pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=30.6 uM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0
CC         and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=42.3 uM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH
CC         9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
CC         KM=69 uM for DL-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:28888424};
CC         KM=7.7 uM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone
CC         {ECO:0000269|PubMed:28888424};
CC         KM=30 uM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone
CC         {ECO:0000269|PubMed:19706438};
CC         KM=140 uM for tetramyristoyl cardiolipin
CC         {ECO:0000269|PubMed:26338420};
CC         KM=148 uM for tetralinoleoyl cardiolipin
CC         {ECO:0000269|PubMed:26338420};
CC         KM=40 uM for oxidized tetralinoleoyl cardiolipin
CC         {ECO:0000269|PubMed:26338420};
CC         KM=7.1 uM for (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA
CC         {ECO:0000269|PubMed:19706438};
CC         Vmax=14.8 umol/min/mg enzyme toward (2S,3S)-3-hydroxy-2-
CC         methylbutanoyl-CoA {ECO:0000269|PubMed:19706438};
CC         Vmax=150 umol/min/mg enzyme 3alpha-hydroxy-5alpha-pregnan-20-
CC         one/allopregnanolone {ECO:0000269|PubMed:19706438};
CC         Note=kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA
CC         (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone
CC         (PubMed:28888424). {ECO:0000269|PubMed:28888424};
CC       pH dependence:
CC         Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees
CC         Celsius, and 7.0 for the reductase reaction at 25 degrees Celsius.
CC         {ECO:0000269|PubMed:12917011};
CC   -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC       {ECO:0000269|PubMed:19706438}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000269|PubMed:10600649, ECO:0000269|PubMed:12917011,
CC       ECO:0000269|PubMed:9553139}.
CC   -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:10600649,
CC       ECO:0000269|PubMed:12917011}.
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000269|PubMed:12917011}.
CC   -!- SUBUNIT: Homotetramer (PubMed:15342248, PubMed:20077426,
CC       PubMed:25925575). Component of mitochondrial ribonuclease P, a complex
CC       composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3
CC       (PubMed:18984158, PubMed:25925575, PubMed:26950678, PubMed:28888424).
CC       Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the
CC       mitochondrial ribonuclease P complex (PubMed:23042678,
CC       PubMed:29040705). {ECO:0000269|PubMed:15342248,
CC       ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:20077426,
CC       ECO:0000269|PubMed:23042678, ECO:0000269|PubMed:25925575,
CC       ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424,
CC       ECO:0000269|PubMed:29040705}.
CC   -!- INTERACTION:
CC       Q99714; P05067: APP; NbExp=7; IntAct=EBI-79964, EBI-77613;
CC       Q99714; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-79964, EBI-821758;
CC       Q99714; P13639: EEF2; NbExp=3; IntAct=EBI-79964, EBI-352560;
CC       Q99714; Q12931: TRAP1; NbExp=3; IntAct=EBI-79964, EBI-1055869;
CC       Q99714; Q7L0Y3: TRMT10C; NbExp=22; IntAct=EBI-79964, EBI-2107046;
CC       Q99714-2; P05067: APP; NbExp=3; IntAct=EBI-25939412, EBI-77613;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12917011,
CC       ECO:0000269|PubMed:18984158}. Mitochondrion matrix, mitochondrion
CC       nucleoid {ECO:0000269|PubMed:24703694}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99714-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99714-2; Sequence=VSP_007830;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues but is
CC       overexpressed in neurons affected in AD. {ECO:0000269|PubMed:9338779}.
CC   -!- DISEASE: HDS10 mitochondrial disease (HSD10MD) [MIM:300438]: An X-
CC       linked multisystemic disorder with highly variable severity. Age at
CC       onset ranges from the neonatal period to early childhood. Features
CC       include progressive neurodegeneration, psychomotor retardation, loss of
CC       mental and motor skills, seizures, cardiomyopathy, and visual and
CC       hearing impairment. Some patients manifest lactic acidosis and
CC       metabolic acidosis. {ECO:0000269|PubMed:12696021,
CC       ECO:0000269|PubMed:16148061, ECO:0000269|PubMed:17236142,
CC       ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:19706438,
CC       ECO:0000269|PubMed:20077426, ECO:0000269|PubMed:22132097,
CC       ECO:0000269|PubMed:24549042, ECO:0000269|PubMed:25575635,
CC       ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26338420,
CC       ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; U96132; AAC51812.1; -; mRNA.
DR   EMBL; U73514; AAB68958.1; -; mRNA.
DR   EMBL; AF069134; AAC39900.1; -; mRNA.
DR   EMBL; AF035555; AAC15902.1; -; mRNA.
DR   EMBL; AF037438; AAC16419.1; -; Genomic_DNA.
DR   EMBL; CR456723; CAG33004.1; -; mRNA.
DR   EMBL; Z97054; CAI42652.1; -; Genomic_DNA.
DR   EMBL; Z97054; CAI42653.1; -; Genomic_DNA.
DR   EMBL; CH471154; EAW93157.1; -; Genomic_DNA.
DR   EMBL; CH471154; EAW93158.1; -; Genomic_DNA.
DR   EMBL; BC000372; AAH00372.1; -; mRNA.
DR   EMBL; BC008708; AAH08708.1; -; mRNA.
DR   EMBL; AY092415; AAM18189.1; -; mRNA.
DR   CCDS; CCDS14354.1; -. [Q99714-1]
DR   CCDS; CCDS35300.1; -. [Q99714-2]
DR   RefSeq; NP_001032900.1; NM_001037811.2. [Q99714-2]
DR   RefSeq; NP_004484.1; NM_004493.2. [Q99714-1]
DR   PDB; 1SO8; X-ray; 2.30 A; A=1-261.
DR   PDB; 1U7T; X-ray; 2.00 A; A/B/C/D=1-261.
DR   PDB; 2O23; X-ray; 1.20 A; A/B=1-261.
DR   PDB; 7ONU; EM; 3.00 A; A/B/C/D=1-261.
DR   PDBsum; 1SO8; -.
DR   PDBsum; 1U7T; -.
DR   PDBsum; 2O23; -.
DR   PDBsum; 7ONU; -.
DR   AlphaFoldDB; Q99714; -.
DR   SMR; Q99714; -.
DR   BioGRID; 109278; 501.
DR   ComplexPortal; CPX-6155; Mitochondrial ribonuclease P complex.
DR   ComplexPortal; CPX-6161; Mitochondrial tRNA:m(1)R9 methyltransferase complex.
DR   CORUM; Q99714; -.
DR   IntAct; Q99714; 208.
DR   MINT; Q99714; -.
DR   STRING; 9606.ENSP00000168216; -.
DR   BindingDB; Q99714; -.
DR   ChEMBL; CHEMBL4159; -.
DR   DrugBank; DB02820; 1-Azepan-1-Yl-2-Phenyl-2-(4-Thioxo-1,4-Dihydro-Pyrazolo[3,4-D]Pyrimidin-5-Yl)Ethanone Adduct.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB09568; Omega-3-carboxylic acids.
DR   SwissLipids; SLP:000000787; -.
DR   GlyGen; Q99714; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99714; -.
DR   MetOSite; Q99714; -.
DR   PhosphoSitePlus; Q99714; -.
DR   SwissPalm; Q99714; -.
DR   BioMuta; HSD17B10; -.
DR   DMDM; 2492759; -.
DR   REPRODUCTION-2DPAGE; IPI00017726; -.
DR   REPRODUCTION-2DPAGE; Q99714; -.
DR   UCD-2DPAGE; Q99714; -.
DR   CPTAC; CPTAC-522; -.
DR   CPTAC; CPTAC-523; -.
DR   EPD; Q99714; -.
DR   jPOST; Q99714; -.
DR   MassIVE; Q99714; -.
DR   MaxQB; Q99714; -.
DR   PaxDb; Q99714; -.
DR   PeptideAtlas; Q99714; -.
DR   PRIDE; Q99714; -.
DR   ProteomicsDB; 78427; -. [Q99714-1]
DR   ProteomicsDB; 78428; -. [Q99714-2]
DR   TopDownProteomics; Q99714-1; -. [Q99714-1]
DR   TopDownProteomics; Q99714-2; -. [Q99714-2]
DR   Antibodypedia; 357; 565 antibodies from 42 providers.
DR   DNASU; 3028; -.
DR   Ensembl; ENST00000168216.11; ENSP00000168216.6; ENSG00000072506.14. [Q99714-1]
DR   Ensembl; ENST00000375304.9; ENSP00000364453.5; ENSG00000072506.14. [Q99714-2]
DR   GeneID; 3028; -.
DR   KEGG; hsa:3028; -.
DR   MANE-Select; ENST00000168216.11; ENSP00000168216.6; NM_004493.3; NP_004484.1.
DR   UCSC; uc004dsl.2; human. [Q99714-1]
DR   CTD; 3028; -.
DR   DisGeNET; 3028; -.
DR   GeneCards; HSD17B10; -.
DR   HGNC; HGNC:4800; HSD17B10.
DR   HPA; ENSG00000072506; Low tissue specificity.
DR   MalaCards; HSD17B10; -.
DR   MIM; 300256; gene.
DR   MIM; 300438; phenotype.
DR   neXtProt; NX_Q99714; -.
DR   OpenTargets; ENSG00000072506; -.
DR   Orphanet; 85295; HSD10 disease, atypical type.
DR   Orphanet; 391428; HSD10 disease, infantile type.
DR   Orphanet; 391457; HSD10 disease, neonatal type.
DR   PharmGKB; PA162391638; -.
DR   VEuPathDB; HostDB:ENSG00000072506; -.
DR   eggNOG; KOG1199; Eukaryota.
DR   GeneTree; ENSGT00940000155170; -.
DR   HOGENOM; CLU_010194_42_0_1; -.
DR   InParanoid; Q99714; -.
DR   OMA; QGIRVCT; -.
DR   PhylomeDB; Q99714; -.
DR   TreeFam; TF354307; -.
DR   BioCyc; MetaCyc:HS01071-MON; -.
DR   BRENDA; 1.1.1.135; 2681.
DR   BRENDA; 1.1.1.178; 2681.
DR   BRENDA; 1.1.1.35; 2681.
DR   BRENDA; 1.1.1.62; 2681.
DR   PathwayCommons; Q99714; -.
DR   Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
DR   Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR   Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
DR   SABIO-RK; Q99714; -.
DR   SignaLink; Q99714; -.
DR   UniPathway; UPA00221; -.
DR   UniPathway; UPA00364; -.
DR   UniPathway; UPA00659; -.
DR   BioGRID-ORCS; 3028; 144 hits in 725 CRISPR screens.
DR   ChiTaRS; HSD17B10; human.
DR   EvolutionaryTrace; Q99714; -.
DR   GeneWiki; HSD17B10; -.
DR   GenomeRNAi; 3028; -.
DR   Pharos; Q99714; Tchem.
DR   PRO; PR:Q99714; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q99714; protein.
DR   Bgee; ENSG00000072506; Expressed in right lobe of liver and 110 other tissues.
DR   ExpressionAtlas; Q99714; baseline and differential.
DR   Genevisible; Q99714; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR   GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:CAFA.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR   GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA: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; IDA:UniProtKB.
DR   GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; IDA: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; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR   GO; GO:0106283; F:ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB.
DR   GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0062173; P:brexanolone metabolic process; IDA:UniProtKB.
DR   GO; GO:0008207; P:C21-steroid hormone metabolic process; IDA:UniProtKB.
DR   GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006550; P:isoleucine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; IDA:UniProtKB.
DR   GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IDA:UniProtKB.
DR   GO; GO:0070901; P:mitochondrial tRNA methylation; IDA:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA: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   3D-structure; Acetylation; Alternative splicing; Disease variant;
KW   Fatty acid metabolism; Intellectual disability; Lipid metabolism;
KW   Mitochondrion; Mitochondrion nucleoid; NAD; Neurodegeneration;
KW   Oxidoreductase; Reference proteome; Steroid metabolism; tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           2..261
FT                   /note="3-hydroxyacyl-CoA dehydrogenase type-2"
FT                   /id="PRO_0000054810"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:15087549"
FT   BINDING         20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15087549"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:15342248,
FT                   ECO:0007744|PDB:1U7T"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:25944712"
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   VAR_SEQ         191..199
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_007830"
FT   VARIANT         12
FT                   /note="V -> L (in HSD10MD; decreased dehydrogenase
FT                   activity; decreased tRNA methylation; decreased
FT                   mitochondrial tRNA 5'-end processing)"
FT                   /evidence="ECO:0000269|PubMed:28888424"
FT                   /id="VAR_080049"
FT   VARIANT         65
FT                   /note="V -> A (in HSD10MD; unknown pathological
FT                   significance; dbSNP:rs104886492)"
FT                   /evidence="ECO:0000269|PubMed:22132097"
FT                   /id="VAR_078863"
FT   VARIANT         86
FT                   /note="D -> G (in HSD10MD; decreased 3-hydroxy-2-
FT                   methylbutyryl-CoA dehydrogenase activity; no effect on
FT                   NAD(+) binding; complete loss of phospholipase C-like
FT                   activity toward cardiolipin; dbSNP:rs587777651)"
FT                   /evidence="ECO:0000269|PubMed:20077426,
FT                   ECO:0000269|PubMed:26338420"
FT                   /id="VAR_078864"
FT   VARIANT         122
FT                   /note="L -> V (in HSD10MD; dbSNP:rs28935476)"
FT                   /evidence="ECO:0000269|PubMed:12696021"
FT                   /id="VAR_015987"
FT   VARIANT         130
FT                   /note="R -> C (in HSD10MD; decreased stability; decreased
FT                   3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity;
FT                   decreased mitochondrial tRNA 5'-end processing; decreased
FT                   tRNA methylation; does not affect homotetramerization;
FT                   complete loss of phospholipase C-like activity toward
FT                   cardiolipin; dbSNP:rs28935475)"
FT                   /evidence="ECO:0000269|PubMed:12696021,
FT                   ECO:0000269|PubMed:16148061, ECO:0000269|PubMed:18996107,
FT                   ECO:0000269|PubMed:19706438, ECO:0000269|PubMed:20077426,
FT                   ECO:0000269|PubMed:24549042, ECO:0000269|PubMed:25925575,
FT                   ECO:0000269|PubMed:26338420"
FT                   /id="VAR_015988"
FT   VARIANT         165
FT                   /note="Q -> H (in HSD10MD; loss of 3-hydroxy-2-
FT                   methylbutyryl-CoA dehydrogenase activity; does not bind
FT                   NAD(+); complete loss of phospholipase C-like activity
FT                   toward cardiolipin)"
FT                   /evidence="ECO:0000269|PubMed:20077426,
FT                   ECO:0000269|PubMed:24549042, ECO:0000269|PubMed:26338420"
FT                   /id="VAR_078865"
FT   VARIANT         176
FT                   /note="V -> M (in HSD10MD; decreased dehydrogenase
FT                   activity; strongly decreased tRNA methylation; strongly
FT                   decreased mitochondrial tRNA 5'-end processing)"
FT                   /evidence="ECO:0000269|PubMed:28888424"
FT                   /id="VAR_080050"
FT   VARIANT         210
FT                   /note="P -> S (in HSD10MD; decreased 3-hydroxyacyl-CoA
FT                   dehydrogenase activity; decreased mitochondrial tRNA 5'-end
FT                   processing; decreased tRNA methylation; does not affect
FT                   homotetramerization)"
FT                   /evidence="ECO:0000269|PubMed:18996107,
FT                   ECO:0000269|PubMed:25925575"
FT                   /id="VAR_080051"
FT   VARIANT         212
FT                   /note="K -> E (in HSD10MD; 4-fold decrease of 3-
FT                   hydroxyacyl-CoA dehydrogenase activity; decreased
FT                   interaction with TRMT10C; decreased function in
FT                   mitochondrial tRNA methylation; decreased function in
FT                   mitochondrial tRNA processing; dbSNP:rs886041974)"
FT                   /evidence="ECO:0000269|PubMed:26950678"
FT                   /id="VAR_078866"
FT   VARIANT         226
FT                   /note="R -> Q (in HSD10MD; strongly decreased 3-
FT                   hydroxyacyl-CoA dehydrogenase activity; abolished
FT                   mitochondrial tRNA 5'-end processing; abolished tRNA
FT                   methylation; impaired homotetramerization;
FT                   dbSNP:rs1556894502)"
FT                   /evidence="ECO:0000269|PubMed:18996107,
FT                   ECO:0000269|PubMed:25925575"
FT                   /id="VAR_080052"
FT   VARIANT         247
FT                   /note="N -> S (in HSD10MD; strongly decreased 3-
FT                   hydroxyacyl-CoA dehydrogenase activity; abolished
FT                   mitochondrial tRNA 5'-end processing; abolished tRNA
FT                   methylation; impaired homotetramerization;
FT                   dbSNP:rs122461163)"
FT                   /evidence="ECO:0000269|PubMed:16148061,
FT                   ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:25925575"
FT                   /id="VAR_032093"
FT   VARIANT         249
FT                   /note="E -> Q (in HSD10MD; decreased 3-hydroxy-2-
FT                   methylbutyryl-CoA dehydrogenase activity;
FT                   dbSNP:rs62626305)"
FT                   /evidence="ECO:0000269|PubMed:19706438"
FT                   /id="VAR_078867"
FT   MUTAGEN         20
FT                   /note="S->F: Decreased dehydrogenase activity. Does not
FT                   affect mitochondrial tRNA 5'-end processing. Does not
FT                   affect tRNA methylation."
FT                   /evidence="ECO:0000269|PubMed:23042678,
FT                   ECO:0000269|PubMed:25925575"
FT   MUTAGEN         172
FT                   /note="K->A: Abolishes dehydrogenase activity. Does not
FT                   affect mitochondrial tRNA 5'-end processing. Does not
FT                   affect tRNA methylation. Does not affect
FT                   homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23042678,
FT                   ECO:0000269|PubMed:25925575"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           47..54
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           68..82
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           123..136
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           157..160
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           166..186
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           204..208
FT                   /evidence="ECO:0007829|PDB:1U7T"
FT   HELIX           216..219
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   HELIX           230..242
FT                   /evidence="ECO:0007829|PDB:2O23"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:2O23"
SQ   SEQUENCE   261 AA;  26923 MW;  9E74F242E3E6FEF1 CRC64;
     MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF
     APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV
     NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL
     PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI
     IENPFLNGEV IRLDGAIRMQ P
 
 
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