ID   HOT_XENLA               Reviewed;         463 AA.
AC   Q08B39;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. Hydroxyacid-oxoacid transhydrogenase subfamily.
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DR   EMBL; BC124888; AAI24889.1; -; mRNA.
DR   RefSeq; NP_001121274.1; -.
DR   UniGene; Xl.15864; -.
DR   GeneID; 100158357; -.
DR   KEGG; xla:100158357; -.
DR   Xenbase; XB-FEAT-966428; adhfe1.
DR   HOVERGEN; Q08B39; -.
DR   BRENDA; 1.1.99.24; 648.
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; ADH_Fe.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; FALSE_NEG.
DR   PROSITE; PS00060; ADH_IRON_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    463       Hydroxyacid-oxoacid transhydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000323000.
SQ   SEQUENCE   463 AA;  50172 MW;  5E373B5086BA88AE CRC64;
     MAAGRDGVIH LLRQLQRASC RCPAHSHTYS QAPATARTTD YAFEMAVSSI RYGENVTQEI
     GMDLQNWGTR NVCVMTDRNL SELSPVKAVL NSLVKNGINF KLYDSVRVEP TDKSFMDAIE
     FAKKGQFDAF VAVGGGSVID TCKAANLYSS SPDSDFLDYV NPPIGKGKAV TVPLKPLIAV
     PTTSGTGSET TGIAIFDYEE LKAKTGIASR AIKPTLGLID PAHTLSMPER VVANSGFDVL
     CHSLESYTAL PYNMRSPCPT NPINRPAYQG SNPISDVWAK HALRIVAKFL KRAVRNPDDR
     EARFAMHLAS SFAGVGFGNA GVHLCHGMSY PIAGHVKTYR AKDYKVDHPL VPHGLSVVLT
     SPAVFSFTGL MCPERHLEAA EILGADLRTA KIKDAGLILA DTLRKFLYDL NVDDGLAAVG
     YTAEDIPALV KGTLPQERVT KLSPRAHSEE ELAALFEASM KLY
//