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Protein

Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial

Gene

Dhtkd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: GO_Central
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. generation of precursor metabolites and energy Source: UniProtKB
  2. glycolytic process Source: UniProtKB-KW
  3. hematopoietic progenitor cell differentiation Source: MGI
  4. tricarboxylic acid cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
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 namesi
Name:Dhtkd1
Synonyms:Kiaa1630
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2445096. Dhtkd1.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
  2. oxoglutarate dehydrogenase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 921Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrialPRO_0000307937
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841N6-succinyllysine1 Publication
Modified residuei189 – 1891N6-succinyllysine1 Publication
Modified residuei801 – 8011N6-succinyllysine1 Publication
Modified residuei819 – 8191N6-succinyllysine1 Publication

Proteomic databases

MaxQBiA2ATU0.
PaxDbiA2ATU0.
PRIDEiA2ATU0.

PTM databases

PhosphoSiteiA2ATU0.

Expressioni

Gene expression databases

BgeeiA2ATU0.
GenevestigatoriA2ATU0.

Interactioni

Protein-protein interaction databases

IntActiA2ATU0. 2 interactions.
MINTiMINT-1839549.

Structurei

3D structure databases

ProteinModelPortaliA2ATU0.
SMRiA2ATU0. Positions 60-919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiA2ATU0.
KOiK15791.
OMAiEHSSCRM.
OrthoDBiEOG7CZK4Z.
PhylomeDBiA2ATU0.
TreeFamiTF314198.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2ATU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAATVAAA GRALRRAVLL LRRGYQTERG VYGYRPRKAK SGEPRGDRAR
60 70 80 90 100
PSVDHGLARL VTVYCEHGHK AAQINPLFPG QALLDTVPEI QALVRTLQGP
110 120 130 140 150
FTTTGLLNLG KEAASLEEVL AYLNHIYCGP ISIETAQLQS QEERDWFARR
160 170 180 190 200
FEELKKETFT TEERKYLSKL LLESQEFDHF LATKFATVKR YGGEGAESMM
210 220 230 240 250
GFFHELLKLS AYGGITDIII GMPHRGRLNL LTGLLQLPPE LMFRKMRGLS
260 270 280 290 300
EFPENVATIG DVLSHLTSSV DLDFGAHQPL HVTMLPNPSH LEAVNPVAVG
310 320 330 340 350
KTRGRQQSRE DGDYSPNGSA QPGDKVICLQ VHGDASFCGQ GIVLETFTLS
360 370 380 390 400
NLPHFRIGGS IHLIVNNQLG YTTPAERGRS SLYSSDIGKL VGCAIIHVNG
410 420 430 440 450
DSPEEVVRAT RLAFEYQRQF RKDVIVDLLC YRQWGHNELD EPFFTNPVMY
460 470 480 490 500
KIIRARKSIP DTYAEHLIAS GLMTQEEVSD IKTSYYTKLN DHLANVAHYS
510 520 530 540 550
PPATNLQARW QGLVQPEACV TTWDTGVPLE LLRFIGVKSV EVPEELQVHS
560 570 580 590 600
HLLKMYVQSR MEKVKNGSGL DWATAETLAL GSLLAQGFNV RLSGQDVGRG
610 620 630 640 650
TFSQRHAMVV CQDTDDAYIP LNHMDPNQKG FLEVSNSPLS EEAVLGFEYG
660 670 680 690 700
MSIESPTLLP LWEAQFGDFF NGAQIIFDTF ISGGEAKWLL QSGLVILLPH
710 720 730 740 750
GYDGAGPEHS SCRIERFLQM CDSAEEGVDS DTVNMFVVHP TTPAQYFHLL
760 770 780 790 800
RRQMIRNFRK PLIVASPKML LRYPAAVSTL EEMAPGTAFK PVIGDSSVDP
810 820 830 840 850
KNVKTLIFCS GKHFYALLKQ RESLGTKKHD FAIIRLEELC PFPLDALQQE
860 870 880 890 900
MSKYKHVRDV IWSQEEPQNM GPWSFVSPRF EKQLACRLRL VSRPPLPAPA
910 920
VGIGTVHQQQ HEDILSKTFT Q
Length:921
Mass (Da):102,793
Last modified:February 20, 2007 - v1
Checksum:iE40170D7D26EED65
GO

Sequence cautioni

The sequence BAD32501.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → S in AAI17995 (PubMed:15489334).Curated
Sequence conflicti436 – 4361H → R in AAI17995 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928924 Genomic DNA. Translation: CAM20352.1.
BC117994 mRNA. Translation: AAI17995.1.
AK173223 mRNA. Translation: BAD32501.1. Sequence problems.
AK050057 mRNA. Translation: BAC34055.1.
CCDSiCCDS38040.1.
RefSeqiNP_001074600.1. NM_001081131.2.
UniGeneiMm.222517.

Genome annotation databases

EnsembliENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815.
ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815.
GeneIDi209692.
KEGGimmu:209692.
UCSCiuc008iga.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928924 Genomic DNA. Translation: CAM20352.1.
BC117994 mRNA. Translation: AAI17995.1.
AK173223 mRNA. Translation: BAD32501.1. Sequence problems.
AK050057 mRNA. Translation: BAC34055.1.
CCDSiCCDS38040.1.
RefSeqiNP_001074600.1. NM_001081131.2.
UniGeneiMm.222517.

3D structure databases

ProteinModelPortaliA2ATU0.
SMRiA2ATU0. Positions 60-919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiA2ATU0. 2 interactions.
MINTiMINT-1839549.

PTM databases

PhosphoSiteiA2ATU0.

Proteomic databases

MaxQBiA2ATU0.
PaxDbiA2ATU0.
PRIDEiA2ATU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815.
ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815.
GeneIDi209692.
KEGGimmu:209692.
UCSCiuc008iga.1. mouse.

Organism-specific databases

CTDi55526.
MGIiMGI:2445096. Dhtkd1.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiA2ATU0.
KOiK15791.
OMAiEHSSCRM.
OrthoDBiEOG7CZK4Z.
PhylomeDBiA2ATU0.
TreeFamiTF314198.

Miscellaneous databases

ChiTaRSiDhtkd1. mouse.
NextBioi372765.
PROiA2ATU0.
SOURCEiSearch...

Gene expression databases

BgeeiA2ATU0.
GenevestigatoriA2ATU0.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 525-921.
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-184; LYS-189; LYS-801 AND LYS-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHTK1_MOUSE
AccessioniPrimary (citable) accession number: A2ATU0
Secondary accession number(s): Q0VFY3, Q69ZE3, Q8BWT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 20, 2007
Last modified: March 4, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.