ID   HOT_RAT                 Reviewed;         467 AA.
AC   Q4QQW3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-NOV-2008, entry version 24.
DE   RecName: Full=Hydroxyacid-oxoacid transhydrogenase, mitochondrial;
DE            Short=HOT;
DE            EC=1.1.99.24;
DE   AltName: Full=Alcohol dehydrogenase iron-containing protein 1;
DE   Flags: Precursor;
GN   Name=Adhfe1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=3182820;
RA   Kaufman E.E., Nelson T., Fales H.M., Levin D.M.;
RT   "Isolation and characterization of a hydroxyacid-oxoacid
RT   transhydrogenase from rat kidney mitochondria.";
RL   J. Biol. Chem. 263:16872-16879(1988).
CC   -!- FUNCTION: Catalyzes the cofactor-independent reversible oxidation
CC       of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA)
CC       coupled to reduction of 2-ketoglutarate (2-KG) to D-2-
CC       hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a
CC       substrate for HOT when using 2-KG as hydrogen acceptor, resulting
CC       in the formation of D-2-HG (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoate + 2-oxoglutarate =
CC       acetoacetate + (R)-2-hydroxyglutarate.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutaric acid + 4-hydroxybutanoic acid =
CC       (R)-2-hydroxyglutaric acid + succinic semialdehyde.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 mM for GHB;
CC         KM=0.4 mM for D-2-HG;
CC         KM=0.018 mM for 2-KG;
CC         KM=0.005 mM for SSA;
CC         KM=3 mM for L-3-OHB;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney and liver.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. Hydroxyacid-oxoacid transhydrogenase subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC097945; AAH97945.1; -; mRNA.
DR   RefSeq; NP_001020594.1; -.
DR   UniGene; Rn.17173; -.
DR   Ensembl; ENSRNOG00000007069; Rattus norvegicus.
DR   GeneID; 362474; -.
DR   KEGG; rno:362474; -.
DR   RGD; 1308863; Adhfe1.
DR   HOVERGEN; Q4QQW3; -.
DR   NextBio; 680067; -.
DR   ArrayExpress; Q4QQW3; -.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0047988; F:hydroxyacid-oxoacid transhydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0015993; P:molecular hydrogen transport; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; Fe_AlcDHase.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; FALSE_NEG.
DR   PROSITE; PS00060; ADH_IRON_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    467       Hydroxyacid-oxoacid transhydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000322999.
SQ   SEQUENCE   467 AA;  50226 MW;  97F4EB2243EBE7DB CRC64;
     MAAAARARVT HLLRHLQSTA CQCPTHSHTY SQVPGLSPSG KTTDYAFEMA VSNIRYGAGV
     TKEVGMDLQN MGAKNVCLMT DKNLSQLPPV QIVMDSLSKN GISFQVYDNV RVEPTDGSFM
     DAIEFAKKGA FDAYVAVGGG STMDTCKAAN LYACSPHSEF LDYVNAPIGK GKPVTVPLKP
     LIAVPTTSGT GSETTGVAIF DYEHLKVKTG IASRAIKPTL GLVDPLHTLH MPCQVVANSG
     FDVLCHALES YTAIPYSMRS PCPSNPIQRP AYQGSNPISD IWAVHALRIV AKYLKRAVRN
     PDDLEARSSM HLASAFAGIG FGNAGVHLCH GMSYPISGLV KTYKAKEYNV DHPLVPHGLS
     VVLTSPAVFT FTAQMFPERH LETAEILGAN IRTAKIQDAG PVLADALRKF LFDLNVDDGL
     AALGYSKDDI PSLVKGTLPQ ERVTKLAPRA QSEEDLSALF EASMKLY
//