Reviewed, UniProtKB/Swiss-Prot A2ATU0 (DHTK1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	921 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamin pyrophosphate 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	? – 921		Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial		PRO_0000307937
Experimental info
	Sequence conflict	24	1	G → S in AAI17995. Ref.2
	Sequence conflict	436	1	H → R in AAI17995. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A2ATU0-1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: E40170D7D26EED65	FASTA	921	102,793
	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

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. , 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. , 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
EMBLGenBankDDBJ	AL928924 Genomic DNA. Translation: CAM20352.1. BC117994 mRNA. Translation: AAI17995.1. AK173223 mRNA. Translation: BAD32501.1. Sequence problems. AK050057 mRNA. Translation: BAC34055.1.
IPI	IPI00756386.
RefSeq	NP_001074600.1.
UniGene	Mm.222517
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A2ATU0.
PTM databases
PhosphoSite	A2ATU0.
Proteomic databases
PRIDE	A2ATU0.
Genome annotation databases
Ensembl	ENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815; Mus musculus. [Genome view] ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815; Mus musculus. [Genome view]
GeneID	209692.
KEGG	mmu:209692.
UCSC	uc008iga.1. mouse. uc008igb.1. mouse.
Organism-specific databases
CTD	209692.
MGI	MGI:2445096. Dhtkd1.
Rouge	Search...
Phylogenomic databases
HOVERGEN	A2ATU0.
OMA	MIRNFRK.
Enzyme and pathway databases
BRENDA	1.2.4.2. 244.
Gene expression databases
Bgee	A2ATU0.
Genevestigator	A2ATU0.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	372765.
SOURCE	Search...

Entry information

Entry name

DHTK1_MOUSE

Accession

Primary (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:	November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)