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Protein

Pyruvate dehydrogenase protein X component, mitochondrial

Gene

Pdhx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_293106. Pyruvate metabolism.
REACT_306383. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pdhx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1351627. Pdhx.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 501448Pyruvate dehydrogenase protein X component, mitochondrialPRO_0000020485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei194 – 1941N6-acetyllysineBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei394 – 3941N6-succinyllysine1 Publication

Post-translational modificationi

Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BKZ9.
PaxDbiQ8BKZ9.
PRIDEiQ8BKZ9.

2D gel databases

REPRODUCTION-2DPAGEIPI00222767.

PTM databases

PhosphoSiteiQ8BKZ9.

Expressioni

Gene expression databases

BgeeiQ8BKZ9.
CleanExiMM_PDHX.
ExpressionAtlasiQ8BKZ9. baseline and differential.
GenevisibleiQ8BKZ9. MM.

Interactioni

Subunit structurei

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). Interacts with SIRT4.By similarity

Protein-protein interaction databases

IntActiQ8BKZ9. 2 interactions.
MINTiMINT-1867323.
STRINGi10090.ENSMUSP00000011058.

Structurei

3D structure databases

ProteinModelPortaliQ8BKZ9.
SMRiQ8BKZ9. Positions 57-144, 183-224, 266-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13277Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 21432Interaction with DLDBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi150 – 17122Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00790000123047.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BKZ9.
KOiK13997.
OMAiSWRLGCD.
OrthoDBiEOG7K3TKW.
PhylomeDBiQ8BKZ9.
TreeFamiTF332256.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BKZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASWRLHCN QPLLRYLLGF SSRRSLGLAQ GAAAWPVDRG ASWRWFHSTQ
60 70 80 90 100
LLQADPIKVL MPSLSPTMEQ GNIVKWLRKE GEAVSAGDSL CEIETDKAVV
110 120 130 140 150
TLDANDDGIL AKIVVEEGAK NIQLGSLIAL MVEEGEDWKQ VEIPKDVSAP
160 170 180 190 200
PPVSKPPAPT QPSPQPQIPC PARKEHKGTA RFRLSPAARN ILEKHSLDAS
210 220 230 240 250
QGTATGPRGI FTKEDALKLV ELKQMGKITE SRPASAPPPS LSASVPPQAT
260 270 280 290 300
AGPSYPRPMT PPVSIPGQPN AAGTFTEIPA SNIRRVIAKR LTESKSTVPH
310 320 330 340 350
AYATADCDLG AVLKVRRDLV KDDIKVSVND FIIRAAAVTL KQMPGVNVTW
360 370 380 390 400
DGEGPKQLPS VDISVAVATD KGLITPIIKD AAAKGIQEIA DSVKVLSKKA
410 420 430 440 450
RDGKLMPEEY QGGSFSISNL GMFGIDEFAA VINPPQACIL AVGRFRPVLK
460 470 480 490 500
LTEDEEGNPQ LQQHQLITVT MSSDSRVVDD ELATRFLETF KANLENPMRL

G
Length:501
Mass (Da):53,999
Last modified:March 1, 2003 - v1
Checksum:i3FD1FA752EAC5092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047670 mRNA. Translation: BAC33120.1.
BC061231 mRNA. Translation: AAH61231.1.
CCDSiCCDS16473.1.
RefSeqiNP_780303.1. NM_175094.5.
UniGeneiMm.315011.

Genome annotation databases

EnsembliENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
GeneIDi27402.
KEGGimmu:27402.
UCSCiuc008lil.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047670 mRNA. Translation: BAC33120.1.
BC061231 mRNA. Translation: AAH61231.1.
CCDSiCCDS16473.1.
RefSeqiNP_780303.1. NM_175094.5.
UniGeneiMm.315011.

3D structure databases

ProteinModelPortaliQ8BKZ9.
SMRiQ8BKZ9. Positions 57-144, 183-224, 266-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BKZ9. 2 interactions.
MINTiMINT-1867323.
STRINGi10090.ENSMUSP00000011058.

PTM databases

PhosphoSiteiQ8BKZ9.

2D gel databases

REPRODUCTION-2DPAGEIPI00222767.

Proteomic databases

MaxQBiQ8BKZ9.
PaxDbiQ8BKZ9.
PRIDEiQ8BKZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
GeneIDi27402.
KEGGimmu:27402.
UCSCiuc008lil.3. mouse.

Organism-specific databases

CTDi8050.
MGIiMGI:1351627. Pdhx.

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00790000123047.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BKZ9.
KOiK13997.
OMAiSWRLGCD.
OrthoDBiEOG7K3TKW.
PhylomeDBiQ8BKZ9.
TreeFamiTF332256.

Enzyme and pathway databases

ReactomeiREACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_293106. Pyruvate metabolism.
REACT_306383. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi305398.
PROiQ8BKZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BKZ9.
CleanExiMM_PDHX.
ExpressionAtlasiQ8BKZ9. baseline and differential.
GenevisibleiQ8BKZ9. MM.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiODPX_MOUSE
AccessioniPrimary (citable) accession number: Q8BKZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 109 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.