ID   HOT_XENTR               Reviewed;         463 AA.
AC   Q6P371;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
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            Short=ADHFe1;
DE   Flags: Precursor;
GN   Name=adhfe1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cofactor-independent reversible oxidation of
CC       gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to
CC       reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG).
CC       L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-
CC       KG as hydrogen acceptor, resulting in the formation of D-2-HG (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-hydroxybutanoate + 2-oxoglutarate = (R)-2-
CC         hydroxyglutarate + acetoacetate; Xref=Rhea:RHEA:23048,
CC         ChEBI:CHEBI:11047, ChEBI:CHEBI:13705, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810; EC=1.1.99.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-hydroxybutanoate = (R)-2-hydroxyglutarate +
CC         succinate semialdehyde; Xref=Rhea:RHEA:24734, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16724, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706;
CC         EC=1.1.99.24;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. Hydroxyacid-oxoacid transhydrogenase subfamily. {ECO:0000305}.
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DR   EMBL; BC064162; AAH64162.1; -; mRNA.
DR   RefSeq; NP_989277.1; NM_203946.1.
DR   RefSeq; XP_012819920.1; XM_012964466.2.
DR   AlphaFoldDB; Q6P371; -.
DR   SMR; Q6P371; -.
DR   STRING; 8364.ENSXETP00000063497; -.
DR   PaxDb; Q6P371; -.
DR   DNASU; 394891; -.
DR   GeneID; 394891; -.
DR   KEGG; xtr:394891; -.
DR   CTD; 137872; -.
DR   Xenbase; XB-GENE-966429; adhfe1.
DR   eggNOG; KOG3857; Eukaryota.
DR   InParanoid; Q6P371; -.
DR   OrthoDB; 776004at2759; -.
DR   Reactome; R-XTR-880009; Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0047988; F:hydroxyacid-oxoacid transhydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006539; P:glutamate catabolic process via 2-oxoglutarate; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08190; HOT; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR042157; HOT.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
PE   2: Evidence at transcript level;
KW   Lipid metabolism; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..463
FT                   /note="Hydroxyacid-oxoacid transhydrogenase, mitochondrial"
FT                   /id="PRO_0000323001"
SQ   SEQUENCE   463 AA;  50408 MW;  F6CD5F2B90C513C1 CRC64;
     MAARRDQVIH LLRQLQRASC KCPAHSHTYS QAPVTGRKTE YAFEMAVSNI RYGENVTQEI
     GMDLQNLGAR NVCVMTDRNL VELSPVKAVL NSLVKNNVSF KLYDRVRVEP TDKSFMDAIE
     FAKKGQFDAY VGVGGGSVID TCKAANLYSS SPGADFLDYV NPPIGKGKAV TVPLKPLIAV
     PTTSGTGSET TGIAIFDYEE LKAKTGIASR AIKPTLGLID PVHTLSMPER VVANSGFDVL
     CHSLESYTAL PYNMRSPCPT NPINRPAYQG SNPISDVWAK HALRIVAKYL KRAVRNPDDR
     EARFAMHLAS SFAGVGFGNA GVHLCHGMSY PIAGHVKTYR AKDYEVDHPL VPHGLSVVLT
     SPAVFSFTAL MCPERHLEAA EILGADIRTA KIKEAGLILA DTLRKFLYDL NVDDGLAAVG
     YTTEDIPALV KGTLPQERVT KLSPRAHSEE ELAGLFEASM KLY