FUNCTION: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG (By similarity).
CATALYTIC ACTIVITY: (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate.
CATALYTIC ACTIVITY: 2-oxoglutaric acid + 4-hydroxybutanoic acid = (R)-2-hydroxyglutaric acid + succinic semialdehyde.
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CM000071; EAL26233.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001361654.1; -.

3D structure databases

ModBase

Q28XT3.

Organism-specific databases

FlyBase

FBgn0077457; Dpse\GA17444.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0047988;	Molecular function: hydroxyacid-oxoacid transhydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0015993;	Biological process: molecular hydrogen transport (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001670; Fe_AlcDHase.
Graphical view of domain structure.

Pfam

PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00913; ADH_IRON_1; FALSE_NEG.
PS00060; ADH_IRON_2; FALSE_NEG.

BLOCKS

Q28XT3.

Genome annotation databases

4805213; -.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 465`		`Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial.`	`PRO_0000323006`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 50087 Da [This is the MW of the unprocessed precursor]

CRC64: 9CABFA3F023E9BD7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRKNVLNLI NTIVANSCKC PAHSHNYGSA APTGVQTGQK EYAFEANSAS TVRFGPGVSV 

        70         80         90        100        110        120 
EVGADLRNLG AKKVCLVTDR NVAKLPSVKV ALDSLARHGI NYEVYDETRV EPTDASLWHA 

       130        140        150        160        170        180 
ADYARQNEFD AFLAIGGGSV MDTAKAANLF SSDREAEFLD YVNCPIGKGK EISVKLKPLI 

       190        200        210        220        230        240 
AMPTTSGTGS ETTGVAIFDY KRLHAKTGIS SKYLKPTLAI IDPLHTLSQP ERVMAFAGFD 

       250        260        270        280        290        300 
VFCHALESFT AVDYRERGPA PSDPSLRPTY QGRNPISDVW ARFALETIRK NFINAIYEPG 

       310        320        330        340        350        360 
NLEARSQMHL ASTMAGVGFG NAGVHLCHGL SYPISGNVRN YKPAGYTADH ALIPHGLSVV 

       370        380        390        400        410        420 
ISAPAVFEFT APACPDRHLE AAKLLGAKVD GVRASDAGRL LADTVRGFMQ RAGIENGLRE 

       430        440        450        460 
LGFSSSDVPN LVDGTLPQER ITKLAPRAQT QENLAQLFEN SMVAY

Q28XT3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools