ID HOT_CAEEL Reviewed; 465 AA.
AC Q9U2M4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 01-MAY-2013, entry version 69.
DE RecName: Full=Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial;
DE Short=HOT;
DE EC=1.1.99.24;
DE Flags: Precursor;
GN ORFNames=Y38F1A.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
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: 4-hydroxybutanoate + 2-oxoglutarate = succinic
CC semialdehyde + (R)-2-hydroxyglutarate.
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; AL032639; CAA21631.2; -; Genomic_DNA.
DR PIR; E88343; E88343.
DR PIR; T26686; T26686.
DR RefSeq; NP_496764.1; NM_064363.4.
DR ProteinModelPortal; Q9U2M4; -.
DR SMR; Q9U2M4; 53-458.
DR DIP; DIP-24327N; -.
DR MINT; MINT-1044715; -.
DR STRING; 6239.Y38F1A.6.1; -.
DR PaxDb; Q9U2M4; -.
DR EnsemblMetazoa; Y38F1A.6.1; Y38F1A.6.1; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.2; Y38F1A.6.2; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.3; Y38F1A.6.3; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.4; Y38F1A.6.4; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.5; Y38F1A.6.5; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.6; Y38F1A.6.6; Y38F1A.6.
DR EnsemblMetazoa; Y38F1A.6.7; Y38F1A.6.7; Y38F1A.6.
DR GeneID; 174942; -.
DR KEGG; cel:CELE_Y38F1A.6; -.
DR UCSC; Y38F1A.6.1; c. elegans.
DR CTD; 174942; -.
DR WormBase; Y38F1A.6; CE24222; WBGene00012608; -.
DR eggNOG; COG1454; -.
DR GeneTree; ENSGT00390000003849; -.
DR HOGENOM; HOG000243335; -.
DR InParanoid; Q9U2M4; -.
DR KO; K11173; -.
DR OMA; MAYPIAG; -.
DR NextBio; 886136; -.
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 InterPro; IPR001670; ADH_Fe.
DR InterPro; IPR018211; ADH_Fe_CS.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 465 Probable hydroxyacid-oxoacid
FT transhydrogenase, mitochondrial.
FT /FTId=PRO_0000324756.
SQ SEQUENCE 465 AA; 50506 MW; CB9A08D7376E2949 CRC64;
MSASLARGIL SKMGGSCCPH HAPATNPFKL AKLHGNNKST DYAFEMVCST LRFGKGVTLE
IGYDVRNLGA KKTLLITDKN VQNTIAFKNA EQALKMVNIE YEVFDDVLIE PTVNSMQKAI
AFAKSKQFDS FIAVGGGSVI DTTKAAALYA SNPEADFLDF VGPPFGKSMQ PKNPMLPLIA
VPTTAGTGSE TTAAAIMDLP EHKCKTGIRL RCIKPYLAVV DPLNVMSMPR NVAIYSGFDV
LCHALESFTA LPFDQRSPRP ENPGVRPLYQ GSNPISDVWS KEALRIIGKY FRRSIFDPTD
EEARTEMLKA SSFAGIGFGN AGVHLCHGLS YPISSQAKSC VADDYPKEKN LIPHGLSVMT
TAVADFEFTT AACPDRHLIS AQTLGADIPN NASNEYISRT LCDRLRGYMR DFGVPNGLKG
MGFEFSDIEM LTEAASHSVP NIAISPKSAD REIISTLYEK SLTVY
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