Reviewed, UniProtKB/Swiss-Prot Q7Q547 (HOT_ANOGA)

Names and origin

Protein names

Recommended name:
    Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial
      Short name=HOT
    EC=1.1.99.24

Gene names

ORF Names:

AGAP006646

Organism

Anopheles gambiae (African malaria mosquito) [Complete proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (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. 2-oxoglutaric acid + 4-hydroxybutanoic acid = (R)-2-hydroxyglutaric acid + succinic semialdehyde.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	molecular hydrogen transport Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	hydroxyacid-oxoacid transhydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 464		Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial		PRO_0000323004

Sequences

	Sequence		Length	Mass (Da)
	Q7Q547-1 [UniParc]. Last modified January 9, 2007. Version 3. Checksum: 05C5103EC6A471D4	FASTA	464	49,722
	10 20 30 40 50 60 MWNRGRIVSL MRTVSSGSCS CPAHSRPVAI SQQTSCSAEK DTAFEMSSST IRYGPGVTRE 70 80 90 100 110 120 LGHDLQNLGA KSVCVVSDRN VLQLPSVKVG LDAIVRAGIE PVLFDAVRVE PTNESLQTAI 130 140 150 160 170 180 DFARSHRFDA FVAIGGGSAI DTCKVANLYS ADREAEFLDY VNVPIGRAKE VTVPLKPLIA 190 200 210 220 230 240 VPTTAGTGSE TTGVAIFDHK PLHAKTGISS KALRPILGLV DPLHTLSQPE KVAAYCGFDV 250 260 270 280 290 300 FCHALESFTA IPYTERGPAP ANPKLRPPYQ GSNPISDVWA RFALQTISRH FRRAVYAPDD 310 320 330 340 350 360 LEARSQMHLA STMAGVGFGN AGVHLCHGLS YPIAGLVKQF IPDGYTGAHP IIPHGLSVVM 370 380 390 400 410 420 TAPSVFRFTG ASCPDRHLEA AGILGADVAK SHRNDAGAIL ADTVRRYMHD LKIENGLSAL 430 440 450 460 GFNYSDIPAL VKGTLPQERI TKLAPRAQSE EDLAGLFEQS LTVY

References

[1]

"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAAB01008960 Genomic DNA. Translation: EAA10782.3.
RefSeq	XP_316676.3.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1277230.
KEGG	aga:AgaP_AGAP006646.
VectorBase	AGAP006646. Anopheles gambiae.
Phylogenomic databases
OMA	Q7Q547. YSKADIP.
Enzyme and pathway databases
BRENDA	1.1.99.24. 165157.
Family and domain databases
InterPro	IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view]
Pfam	PF00465. Fe-ADH. 1 hit. [Graphical view]
PROSITE	PS00913. ADH_IRON_1. False negative. PS00060. ADH_IRON_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HOT_ANOGA

Accession

Primary (citable) accession number: Q7Q547

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	January 9, 2007
Last modified:	June 16, 2009
This is version 35 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)