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A2ATU0 (DHTK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial
EC=1.2.4.2
Alternative name(s):
Dehydrogenase E1 and transketolase domain-containing protein 1
Gene names
Name:Dhtkd1
Synonyms:Kiaa1630
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length921 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence caution

The sequence BAD32501.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionoxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: EC

thiamine pyrophosphate 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? – 921Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrialPRO_0000307937

Experimental info

Sequence conflict241G → S in AAI17995. Ref.2
Sequence conflict4361H → R in AAI17995. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2ATU0 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: E40170D7D26EED65

FASTA921102,793
        10         20         30         40         50         60 
MASAATVAAA GRALRRAVLL LRRGYQTERG VYGYRPRKAK SGEPRGDRAR PSVDHGLARL 

        70         80         90        100        110        120 
VTVYCEHGHK AAQINPLFPG QALLDTVPEI QALVRTLQGP FTTTGLLNLG KEAASLEEVL 

       130        140        150        160        170        180 
AYLNHIYCGP ISIETAQLQS QEERDWFARR FEELKKETFT TEERKYLSKL LLESQEFDHF 

       190        200        210        220        230        240 
LATKFATVKR YGGEGAESMM GFFHELLKLS AYGGITDIII GMPHRGRLNL LTGLLQLPPE 

       250        260        270        280        290        300 
LMFRKMRGLS EFPENVATIG DVLSHLTSSV DLDFGAHQPL HVTMLPNPSH LEAVNPVAVG 

       310        320        330        340        350        360 
KTRGRQQSRE DGDYSPNGSA QPGDKVICLQ VHGDASFCGQ GIVLETFTLS NLPHFRIGGS 

       370        380        390        400        410        420 
IHLIVNNQLG YTTPAERGRS SLYSSDIGKL VGCAIIHVNG DSPEEVVRAT RLAFEYQRQF 

       430        440        450        460        470        480 
RKDVIVDLLC YRQWGHNELD EPFFTNPVMY KIIRARKSIP DTYAEHLIAS GLMTQEEVSD 

       490        500        510        520        530        540 
IKTSYYTKLN DHLANVAHYS PPATNLQARW QGLVQPEACV TTWDTGVPLE LLRFIGVKSV 

       550        560        570        580        590        600 
EVPEELQVHS HLLKMYVQSR MEKVKNGSGL DWATAETLAL GSLLAQGFNV RLSGQDVGRG 

       610        620        630        640        650        660 
TFSQRHAMVV CQDTDDAYIP LNHMDPNQKG FLEVSNSPLS EEAVLGFEYG MSIESPTLLP 

       670        680        690        700        710        720 
LWEAQFGDFF NGAQIIFDTF ISGGEAKWLL QSGLVILLPH GYDGAGPEHS SCRIERFLQM 

       730        740        750        760        770        780 
CDSAEEGVDS DTVNMFVVHP TTPAQYFHLL RRQMIRNFRK PLIVASPKML LRYPAAVSTL 

       790        800        810        820        830        840 
EEMAPGTAFK PVIGDSSVDP KNVKTLIFCS GKHFYALLKQ RESLGTKKHD FAIIRLEELC 

       850        860        870        880        890        900 
PFPLDALQQE MSKYKHVRDV IWSQEEPQNM GPWSFVSPRF EKQLACRLRL VSRPPLPAPA 

       910        920 
VGIGTVHQQQ HEDILSKTFT Q

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-587.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 525-921.
Strain: C57BL/6J.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL928924 Genomic DNA. Translation: CAM20352.1.
BC117994 mRNA. Translation: AAI17995.1.
AK173223 mRNA. Translation: BAD32501.1. Sequence problems.
AK050057 mRNA. Translation: BAC34055.1.
IPIIPI00756386.
RefSeqNP_001074600.1. NM_001081131.2.
UniGeneMm.222517.

3D structure databases

ProteinModelPortalA2ATU0.
SMRA2ATU0. Positions 51-920.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2ATU0.

PTM databases

PhosphoSiteA2ATU0.

Proteomic databases

PRIDEA2ATU0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815.
ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815.
ENSMUST00000169865; ENSMUSP00000129194; ENSMUSG00000025815.
GeneID209692.
KEGGmmu:209692.
UCSCuc008iga.1. mouse.

Organism-specific databases

CTD55526.
MGIMGI:2445096. Dhtkd1.
RougeSearch...

Phylogenomic databases

eggNOGroNOG08803.
GeneTreeENSGT00530000063092.
HOGENOMHBG289950.
HOVERGENHBG001892.
InParanoidA2ATU0.
OMALCSGKHY.
OrthoDBEOG4F7NJB.

Gene expression databases

BgeeA2ATU0.
GenevestigatorA2ATU0.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. 2oxoglutarate_DH_E1. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

NextBio372765.
SOURCESearch...

Entry information

Entry nameDHTK1_MOUSE
AccessionPrimary (citable) accession number: A2ATU0
Secondary accession number(s): Q0VFY3, Q69ZE3, Q8BWT3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 20, 2007
Last modified: December 14, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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