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Q9W265 (HOT_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial
Short name=HOT
EC=1.1.99.24
Gene names
Name:T3dh
ORF Names:CG3425
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2-hydroxyglutarate.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.

Sequence caution

The sequence AAL28462.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmolecular hydrogen transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentmitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionhydroxyacid-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 464Probable hydroxyacid-oxoacid transhydrogenase, mitochondrialPRO_0000323005

Experimental info

Sequence conflict1081R → L in AAM11277. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9W265 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2351EA6F02E957CD

FASTA46450,018
        10         20         30         40         50         60 
MSRKNVLGLI NTIVANSCKC PAHSHNYGSA APTASQTGRM EYAFEMSAST VRFGPGVSAE 

        70         80         90        100        110        120 
VGADLRNLGA RKVCLVTDKN VVQLPSVKVA LDSLARNGIN YEVYDETRVE PTDGSMWHAV 

       130        140        150        160        170        180 
EFARGKEFDA FLAIGGGSAM DTAKAANLFS SDANAEFLDY VNCPIGRGKE ISVKLKPLIA 

       190        200        210        220        230        240 
MPTTSGTGSE TTGVAIFDYK KLHAKTGISS KFLKPTLAVI DPLHTLSQPQ RVMAFAGFDV 

       250        260        270        280        290        300 
FCHALESFTA VDYRERGLAP SDPSLRPTYQ GRNPVSDVWA RFALETIRKN FVNAIYQPDN 

       310        320        330        340        350        360 
LEARSQMHLA STMAGVGFGN AGVHLCHGLS YPISGNVRDY KPKGYSADHA LIPHGLSVVI 

       370        380        390        400        410        420 
SAPAVFEFTA PACPDRHLEA AQLLGAEVRG VEKADAGRLL ADTVRGFMQR AGIENGLREL 

       430        440        450        460 
GFSSSDIPAL VEGTLPQERI TKLAPRAQTQ ENLSQLFEKS MEVY

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo and Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAF46832.1.
AY060914 mRNA. Translation: AAL28462.1. Different initiation.
AY094924 mRNA. Translation: AAM11277.1.
RefSeqNP_477209.2. NM_057861.2.
UniGeneDm.33441.

3D structure databases

ProteinModelPortalQ9W265.
SMRQ9W265. Positions 42-461.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9W265.

Proteomic databases

PRIDEQ9W265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071848; FBpp0071759; FBgn0017482.
GeneID37551.
KEGGdme:Dmel_CG3425.
NMPDRfig|7227.3.peg.6828.

Organism-specific databases

CTD37551.
FlyBaseFBgn0017482. T3dh.

Phylogenomic databases

eggNOGinNOG05388.
GeneTreeEMGT00050000017002.
InParanoidQ9W265.
OMAYSKADIP.
OrthoDBEOG4KWH8C.
PhylomeDBQ9W265.

Gene expression databases

ArrayExpressQ9W265.
BgeeQ9W265.

Family and domain databases

InterProIPR001670. ADH_Fe.
[Graphical view]
KOK11173.
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEPS00913. ADH_IRON_1. False negative.
PS00060. ADH_IRON_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio804238.

Entry information

Entry nameHOT_DROME
AccessionPrimary (citable) accession number: Q9W265
Secondary accession number(s): Q8SX03, Q95S86
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents