HOT_XENLA
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 03-AUG-2022, entry version 64.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; 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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC124888; AAI24889.1; -; mRNA.
DR RefSeq; NP_001121274.1; NM_001127802.1.
DR AlphaFoldDB; Q08B39; -.
DR SMR; Q08B39; -.
DR DNASU; 100158357; -.
DR GeneID; 100158357; -.
DR KEGG; xla:100158357; -.
DR CTD; 100158357; -.
DR Xenbase; XB-GENE-966434; adhfe1.S.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 100158357; Expressed in liver and 12 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:InterPro.
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_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
