ID   HOT_ANOGA               Reviewed;         464 AA.
AC   Q7Q547;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 31.
DE   RecName: Full=Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial;
DE            Short=HOT;
DE            EC=1.1.99.24;
DE   Flags: Precursor;
GN   ORFNames=AGAP006646;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   MEDLINE=22251359; PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B.,
RA   Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P.,
RA   Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V.,
RA   Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S.,
RA   Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M.,
RA   Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I.,
RA   Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z.,
RA   Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R.,
RA   Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E.,
RA   Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F.,
RA   Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R.,
RA   Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C.,
RA   Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V.,
RA   Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D.,
RA   Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H.,
RA   Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A.,
RA   Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F.,
RA   Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S.,
RA   Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C.,
RA   Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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: 2-oxoglutaric acid + 4-hydroxybutanoic acid =
CC       (R)-2-hydroxyglutaric acid + succinic semialdehyde.
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; AAAB01008960; EAA10782.3; -; Genomic_DNA.
DR   RefSeq; XP_316676.3; -.
DR   GeneID; 1277230; -.
DR   KEGG; aga:AgaP_AGAP006646; -.
DR   VectorBase; AGAP006646; Anopheles gambiae.
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   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; Fe_AlcDHase.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; FALSE_NEG.
DR   PROSITE; PS00060; ADH_IRON_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    464       Probable hydroxyacid-oxoacid
FT                                transhydrogenase, mitochondrial.
FT                                /FTId=PRO_0000323004.
SQ   SEQUENCE   464 AA;  49722 MW;  05C5103EC6A471D4 CRC64;
     MWNRGRIVSL MRTVSSGSCS CPAHSRPVAI SQQTSCSAEK DTAFEMSSST IRYGPGVTRE
     LGHDLQNLGA KSVCVVSDRN VLQLPSVKVG LDAIVRAGIE PVLFDAVRVE PTNESLQTAI
     DFARSHRFDA FVAIGGGSAI DTCKVANLYS ADREAEFLDY VNVPIGRAKE VTVPLKPLIA
     VPTTAGTGSE TTGVAIFDHK PLHAKTGISS KALRPILGLV DPLHTLSQPE KVAAYCGFDV
     FCHALESFTA IPYTERGPAP ANPKLRPPYQ GSNPISDVWA RFALQTISRH FRRAVYAPDD
     LEARSQMHLA STMAGVGFGN AGVHLCHGLS YPIAGLVKQF IPDGYTGAHP IIPHGLSVVM
     TAPSVFRFTG ASCPDRHLEA AGILGADVAK SHRNDAGAIL ADTVRRYMHD LKIENGLSAL
     GFNYSDIPAL VKGTLPQERI TKLAPRAQSE EDLAGLFEQS LTVY
//