[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. PubMed=3182820 [NCBI, ExPASy, EBI, Israel, Japan] Kaufman E.E., Nelson T., Fales H.M., Levin D.M.; "Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria."; J. Biol. Chem. 263:16872-16879(1988).

Comments

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.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.3 mM for GHB;
K_M=0.4 mM for D-2-HG;
K_M=0.018 mM for 2-KG;
K_M=0.005 mM for SSA;
K_M=3 mM for L-3-OHB;
SUBCELLULAR LOCATION: Mitochondrion.
TISSUE SPECIFICITY: Expressed in kidney and liver.
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

BC097945; AAH97945.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001020594.1; -.

UniGene

Rn.17173

3D structure databases

ModBase

Q4QQW3.

Organism-specific databases

RGD

1308863; Adhfe1.

Gene expression databases

ArrayExpress

Q4QQW3; -.

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

Q4QQW3.

Genome annotation databases

Ensembl

ENSRNOG00000007069; Rattus norvegicus. [Contig view]

GeneID

362474; -.

KEGG

rno:362474; -.

Phylogenomic databases

HOVERGEN

Q4QQW3; -.

Other

ProtoNet

Q4QQW3.

UniRef

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

Keywords

Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 467`		`Hydroxyacid-oxoacid transhydrogenase, mitochondrial.`	`PRO_0000322999`

Sequence information

Length: 467 AA [This is the length of the unprocessed precursor]

Molecular weight: 50226 Da [This is the MW of the unprocessed precursor]

CRC64: 97F4EB2243EBE7DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAARARVT HLLRHLQSTA CQCPTHSHTY SQVPGLSPSG KTTDYAFEMA VSNIRYGAGV 

        70         80         90        100        110        120 
TKEVGMDLQN MGAKNVCLMT DKNLSQLPPV QIVMDSLSKN GISFQVYDNV RVEPTDGSFM 

       130        140        150        160        170        180 
DAIEFAKKGA FDAYVAVGGG STMDTCKAAN LYACSPHSEF LDYVNAPIGK GKPVTVPLKP 

       190        200        210        220        230        240 
LIAVPTTSGT GSETTGVAIF DYEHLKVKTG IASRAIKPTL GLVDPLHTLH MPCQVVANSG 

       250        260        270        280        290        300 
FDVLCHALES YTAIPYSMRS PCPSNPIQRP AYQGSNPISD IWAVHALRIV AKYLKRAVRN 

       310        320        330        340        350        360 
PDDLEARSSM HLASAFAGIG FGNAGVHLCH GMSYPISGLV KTYKAKEYNV DHPLVPHGLS 

       370        380        390        400        410        420 
VVLTSPAVFT FTAQMFPERH LETAEILGAN IRTAKIQDAG PVLADALRKF LFDLNVDDGL 

       430        440        450        460 
AALGYSKDDI PSLVKGTLPQ ERVTKLAPRA QSEEDLSALF EASMKLY

Q4QQW3 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