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Q8BKZ9 (ODPX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase protein X component, mitochondrial
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
Lipoyl-containing pyruvate dehydrogenase complex component X
Gene names
Name:Pdhx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex By similarity.

Subunit structure

Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion By similarity
Chain54 – 501448Pyruvate dehydrogenase protein X component, mitochondrial
PRO_0000020485

Regions

Domain57 – 13175Lipoyl-binding
Region183 – 21432Interaction with DLD By similarity
Compositional bias150 – 17122Pro-rich

Amino acid modifications

Modified residue971N6-lipoyllysine By similarity
Modified residue1941N6-acetyllysine By similarity
Modified residue3941N6-succinyllysine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BKZ9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3FD1FA752EAC5092

FASTA50153,999
        10         20         30         40         50         60 
MAASWRLHCN QPLLRYLLGF SSRRSLGLAQ GAAAWPVDRG ASWRWFHSTQ LLQADPIKVL 

        70         80         90        100        110        120 
MPSLSPTMEQ GNIVKWLRKE GEAVSAGDSL CEIETDKAVV TLDANDDGIL AKIVVEEGAK 

       130        140        150        160        170        180 
NIQLGSLIAL MVEEGEDWKQ VEIPKDVSAP PPVSKPPAPT QPSPQPQIPC PARKEHKGTA 

       190        200        210        220        230        240 
RFRLSPAARN ILEKHSLDAS QGTATGPRGI FTKEDALKLV ELKQMGKITE SRPASAPPPS 

       250        260        270        280        290        300 
LSASVPPQAT AGPSYPRPMT PPVSIPGQPN AAGTFTEIPA SNIRRVIAKR LTESKSTVPH 

       310        320        330        340        350        360 
AYATADCDLG AVLKVRRDLV KDDIKVSVND FIIRAAAVTL KQMPGVNVTW DGEGPKQLPS 

       370        380        390        400        410        420 
VDISVAVATD KGLITPIIKD AAAKGIQEIA DSVKVLSKKA RDGKLMPEEY QGGSFSISNL 

       430        440        450        460        470        480 
GMFGIDEFAA VINPPQACIL AVGRFRPVLK LTEDEEGNPQ LQQHQLITVT MSSDSRVVDD 

       490        500 
ELATRFLETF KANLENPMRL G 

« Hide

References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Corpus striatum.
[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].
Tissue: Brain.
[3]"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-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK047670 mRNA. Translation: BAC33120.1.
BC061231 mRNA. Translation: AAH61231.1.
CCDSCCDS16473.1.
RefSeqNP_780303.1. NM_175094.5.
UniGeneMm.315011.

3D structure databases

ProteinModelPortalQ8BKZ9.
SMRQ8BKZ9. Positions 57-144, 183-224, 266-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BKZ9. 2 interactions.
MINTMINT-1867323.
STRING10090.ENSMUSP00000011058.

PTM databases

PhosphoSiteQ8BKZ9.

2D gel databases

REPRODUCTION-2DPAGEIPI00222767.

Proteomic databases

MaxQBQ8BKZ9.
PaxDbQ8BKZ9.
PRIDEQ8BKZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
GeneID27402.
KEGGmmu:27402.
UCSCuc008lil.3. mouse.

Organism-specific databases

CTD8050.
MGIMGI:1351627. Pdhx.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00740000115591.
HOGENOMHOG000281566.
HOVERGENHBG005063.
InParanoidQ8BKZ9.
KOK13997.
OMASWRLGCD.
OrthoDBEOG7K3TKW.
PhylomeDBQ8BKZ9.
TreeFamTF332256.

Gene expression databases

BgeeQ8BKZ9.
CleanExMM_PDHX.
GenevestigatorQ8BKZ9.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDHX. mouse.
NextBio305398.
PROQ8BKZ9.
SOURCESearch...

Entry information

Entry nameODPX_MOUSE
AccessionPrimary (citable) accession number: Q8BKZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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