ODPX_HUMAN
ID ODPX_HUMAN Reviewed; 501 AA.
AC O00330; B4DW62; D3DR11; E9PB14; E9PBP7; O60221; Q96FV8; Q99783;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Pyruvate dehydrogenase protein X component, mitochondrial;
DE AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE AltName: Full=E3-binding protein;
DE Short=E3BP;
DE AltName: Full=Lipoyl-containing pyruvate dehydrogenase complex component X;
DE AltName: Full=proX;
DE Flags: Precursor;
GN Name=PDHX; Synonyms=PDX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-23.
RX PubMed=9242632; DOI=10.1074/jbc.272.32.19746;
RA Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., Popov K.M.;
RT "Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate
RT dehydrogenase complex. DNA-derived amino acid sequence, expression, and
RT reconstitution of the pyruvate dehydrogenase complex.";
RL J. Biol. Chem. 272:19746-19751(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN PDHXD.
RC TISSUE=Liver;
RX PubMed=9399911; DOI=10.1086/301653;
RA Aral B., Benelli C., Ait-Ghezala G., Amessou M., Fouque F., Maunoury C.,
RA Creau N., Kamoun P., Marsac C.;
RT "Mutations in PDX1, the human lipoyl-containing component X of the pyruvate
RT dehydrogenase-complex gene on chromosome 11p1, in congenital lactic
RT acidosis.";
RL Am. J. Hum. Genet. 61:1318-1326(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9467010; DOI=10.1093/hmg/7.3.501;
RA Ling M., McEachern G., Seyda A., Mackay N., Scherer S.W., Bratinova S.,
RA Beatty B., Giovannucci-Uzielli M.L., Robinson B.H.;
RT "Detection of a homozygous four base pair deletion in the protein X gene in
RT a case of pyruvate dehydrogenase complex deficiency.";
RL Hum. Mol. Genet. 7:501-505(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Aral B., Dey R., Marsac C.;
RT "Human gene sequence for PDX1, the human lipoyl-containing component X of
RT the pyruvate dehydrogenase complex.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-370.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-501 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [10]
RP SUBUNIT.
RX PubMed=14638692; DOI=10.1074/jbc.m308172200;
RA Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
RT "Organization of the cores of the mammalian pyruvate dehydrogenase complex
RT formed by E2 and E2 plus the E3-binding protein and their capacities to
RT bind the E1 and E3 components.";
RL J. Biol. Chem. 279:6921-6933(2004).
RN [11]
RP INTERACTION WITH DLD, AND MUTAGENESIS OF ASN-190; ARG-208 AND ILE-210.
RX PubMed=20160912; DOI=10.1016/j.molcatb.2009.05.001;
RA Patel M.S., Korotchkina L.G., Sidhu S.;
RT "Interaction of E1 and E3 components with the core proteins of the human
RT pyruvate dehydrogenase complex.";
RL J. Mol. Catal., B Enzym. 61:2-6(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP INTERACTION WITH DLD.
RX PubMed=20385101; DOI=10.1016/j.bbrc.2010.04.038;
RA Park Y.H., Patel M.S.;
RT "Characterization of interactions of dihydrolipoamide dehydrogenase with
RT its binding protein in the human pyruvate dehydrogenase complex.";
RL Biochem. Biophys. Res. Commun. 395:416-419(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH SIRT4, LIPOYLATION AT LYS-97, AND DELIPOYLATION AT LYS-97.
RX PubMed=25525879; DOI=10.1016/j.cell.2014.11.046;
RA Mathias R.A., Greco T.M., Oberstein A., Budayeva H.G., Chakrabarti R.,
RA Rowland E.A., Kang Y., Shenk T., Cristea I.M.;
RT "Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex
RT activity.";
RL Cell 159:1615-1625(2014).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 54-274 IN COMPLEX WITH DLD.
RX PubMed=16263718; DOI=10.1074/jbc.m507850200;
RA Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K.,
RA Korotchkina L.G., Patel M.S.;
RT "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide
RT dehydrogenase in the human pyruvate dehydrogenase complex.";
RL J. Biol. Chem. 281:648-655(2006).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 174-230 IN COMPLEX WITH DLD, AND
RP MUTAGENESIS OF ARG-183; SER-185; PRO-186; ALA-187; ARG-189; ASN-190;
RP GLU-193; ARG-208; ILE-210; LYS-213 AND GLU-214.
RX PubMed=16442803; DOI=10.1016/j.str.2006.01.001;
RA Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R.,
RA Chuang D.T.;
RT "Structural insight into interactions between dihydrolipoamide
RT dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase
RT complex.";
RL Structure 14:611-621(2006).
RN [20]
RP STRUCTURE BY NMR OF 57-141.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid
RT dehydrogenase.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (18.3 ANGSTROMS) OF INNER CORE OF THE
RP COMPLEX, AND SUBUNIT.
RX PubMed=20361979; DOI=10.1016/j.jmb.2010.03.043;
RA Vijayakrishnan S., Kelly S.M., Gilbert R.J., Callow P., Bhella D.,
RA Forsyth T., Lindsay J.G., Byron O.;
RT "Solution structure and characterisation of the human pyruvate
RT dehydrogenase complex core assembly.";
RL J. Mol. Biol. 399:71-93(2010).
CC -!- FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to
CC the dihydrolipoamide transacetylase (E2) core of the pyruvate
CC dehydrogenase complexes of eukaryotes. This specific binding is
CC essential for a functional PDH complex.
CC -!- SUBUNIT: Part of the inner core of the multimeric pyruvate
CC dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX
CC molecules (PubMed:14638692, PubMed:20361979). This core binds multiple
CC copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1),
CC dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
CC dehydrogenase (DLD, E3) (PubMed:14638692). Interacts with SIRT4
CC (PubMed:25525879). Interacts with DLD (PubMed:20385101,
CC PubMed:16263718, PubMed:16442803, PubMed:20160912, PubMed:20361979).
CC {ECO:0000269|PubMed:14638692, ECO:0000269|PubMed:16263718,
CC ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:20160912,
CC ECO:0000269|PubMed:20361979, ECO:0000269|PubMed:20385101,
CC ECO:0000269|PubMed:25525879}.
CC -!- INTERACTION:
CC O00330; Q6RW13: AGTRAP; NbExp=5; IntAct=EBI-751566, EBI-741181;
CC O00330; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-751566, EBI-7062247;
CC O00330; P09622: DLD; NbExp=7; IntAct=EBI-751566, EBI-353366;
CC O00330; Q9Y6E7: SIRT4; NbExp=4; IntAct=EBI-751566, EBI-2606540;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00330-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00330-2; Sequence=VSP_045271;
CC Name=3;
CC IsoId=O00330-3; Sequence=VSP_053817;
CC -!- PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD
CC complex activity. {ECO:0000269|PubMed:25525879}.
CC -!- DISEASE: Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD)
CC [MIM:245349]: A metabolic disorder characterized by decreased activity
CC of the pyruvate dehydrogenase complex without observable reduction in
CC the activities of enzymes E1, E2, or E3. Clinical features include
CC hypotonia and psychomotor retardation. {ECO:0000269|PubMed:9399911}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF001437; AAB66315.1; -; mRNA.
DR EMBL; Y13145; CAA73606.1; -; mRNA.
DR EMBL; U82328; AAC39661.1; -; mRNA.
DR EMBL; AJ298105; CAC18649.1; -; Genomic_DNA.
DR EMBL; AK301384; BAG62924.1; -; mRNA.
DR EMBL; AC107928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68158.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68160.1; -; Genomic_DNA.
DR EMBL; BC010389; AAH10389.1; -; mRNA.
DR EMBL; U79296; AAB50223.1; -; mRNA.
DR CCDS; CCDS53616.1; -. [O00330-2]
DR CCDS; CCDS7896.1; -. [O00330-1]
DR RefSeq; NP_001128496.1; NM_001135024.1. [O00330-3]
DR RefSeq; NP_001159630.1; NM_001166158.1. [O00330-2]
DR RefSeq; NP_003468.2; NM_003477.2. [O00330-1]
DR PDB; 1ZY8; X-ray; 2.59 A; K/L/M/N/O=54-274.
DR PDB; 2DNC; NMR; -; A=57-141.
DR PDB; 2F5Z; X-ray; 2.18 A; K/L/M/N/O=173-228.
DR PDB; 2F60; X-ray; 1.55 A; K=173-228.
DR PDB; 6H60; EM; 6.00 A; A=1-501.
DR PDBsum; 1ZY8; -.
DR PDBsum; 2DNC; -.
DR PDBsum; 2F5Z; -.
DR PDBsum; 2F60; -.
DR PDBsum; 6H60; -.
DR AlphaFoldDB; O00330; -.
DR SMR; O00330; -.
DR BioGRID; 113737; 98.
DR ComplexPortal; CPX-6233; Mitochondrial pyruvate dehydrogenase complex, somatic variant.
DR ComplexPortal; CPX-6242; Mitochondrial pyruvate dehydrogenase complex, testis-specific variant.
DR DIP; DIP-29026N; -.
DR IntAct; O00330; 28.
DR MINT; O00330; -.
DR STRING; 9606.ENSP00000227868; -.
DR iPTMnet; O00330; -.
DR PhosphoSitePlus; O00330; -.
DR SwissPalm; O00330; -.
DR BioMuta; PDHX; -.
DR EPD; O00330; -.
DR jPOST; O00330; -.
DR MassIVE; O00330; -.
DR MaxQB; O00330; -.
DR PaxDb; O00330; -.
DR PeptideAtlas; O00330; -.
DR PRIDE; O00330; -.
DR ProteomicsDB; 19121; -.
DR ProteomicsDB; 19268; -.
DR ProteomicsDB; 47851; -. [O00330-1]
DR Antibodypedia; 25893; 303 antibodies from 35 providers.
DR DNASU; 8050; -.
DR Ensembl; ENST00000227868.9; ENSP00000227868.4; ENSG00000110435.13. [O00330-1]
DR Ensembl; ENST00000430469.6; ENSP00000415695.2; ENSG00000110435.13. [O00330-2]
DR GeneID; 8050; -.
DR KEGG; hsa:8050; -.
DR MANE-Select; ENST00000227868.9; ENSP00000227868.4; NM_003477.3; NP_003468.2.
DR UCSC; uc001mvt.4; human. [O00330-1]
DR CTD; 8050; -.
DR DisGeNET; 8050; -.
DR GeneCards; PDHX; -.
DR GeneReviews; PDHX; -.
DR HGNC; HGNC:21350; PDHX.
DR HPA; ENSG00000110435; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; PDHX; -.
DR MIM; 245349; phenotype.
DR MIM; 608769; gene.
DR neXtProt; NX_O00330; -.
DR OpenTargets; ENSG00000110435; -.
DR Orphanet; 255182; Pyruvate dehydrogenase E3-binding protein deficiency.
DR PharmGKB; PA134976445; -.
DR VEuPathDB; HostDB:ENSG00000110435; -.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000156046; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; O00330; -.
DR OMA; QVTVIKH; -.
DR OrthoDB; 747232at2759; -.
DR PhylomeDB; O00330; -.
DR TreeFam; TF332256; -.
DR BioCyc; MetaCyc:ENSG00000110435-MON; -.
DR BRENDA; 1.2.1.104; 2681.
DR PathwayCommons; O00330; -.
DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR SignaLink; O00330; -.
DR SIGNOR; O00330; -.
DR BioGRID-ORCS; 8050; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; PDHX; human.
DR EvolutionaryTrace; O00330; -.
DR GeneWiki; E3_binding_protein; -.
DR GenomeRNAi; 8050; -.
DR Pharos; O00330; Tbio.
DR PRO; PR:O00330; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O00330; protein.
DR Bgee; ENSG00000110435; Expressed in biceps brachii and 206 other tissues.
DR ExpressionAtlas; O00330; baseline and differential.
DR Genevisible; O00330; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:ComplexPortal.
DR GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Lipoyl; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 54..501
FT /note="Pyruvate dehydrogenase protein X component,
FT mitochondrial"
FT /id="PRO_0000020484"
FT DOMAIN 56..132
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 183..220
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 142..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:25525879"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKZ9"
FT VAR_SEQ 2..53
FT /note="AASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLR
FT -> QSGGAEGSPGAGRTGRGPGSGKAPPAEISSGAPDFPG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053817"
FT VAR_SEQ 115..341
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045271"
FT VARIANT 23
FT /note="R -> C (in dbSNP:rs1049306)"
FT /evidence="ECO:0000269|PubMed:9242632"
FT /id="VAR_046619"
FT VARIANT 101
FT /note="T -> A (in dbSNP:rs11539202)"
FT /id="VAR_046620"
FT VARIANT 370
FT /note="D -> V (in dbSNP:rs17850649)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046621"
FT MUTAGEN 183
FT /note="R->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 185
FT /note="S->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 186
FT /note="P->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 187
FT /note="A->M: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 189
FT /note="R->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 190
FT /note="N->A: Decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803,
FT ECO:0000269|PubMed:20160912"
FT MUTAGEN 190
FT /note="N->K: Moderately decreased interaction with DLD."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 193
FT /note="E->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 208
FT /note="R->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 208
FT /note="R->D: Decreased interaction with DLD."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 210
FT /note="I->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 210
FT /note="I->R: Decreased interaction with DLD."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 210
FT /note="I->S: Decreased interaction with DLD."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 213
FT /note="K->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT MUTAGEN 214
FT /note="E->A: Strongly decreased DLD binding."
FT /evidence="ECO:0000269|PubMed:16442803"
FT CONFLICT 41
FT /note="A -> R (in Ref. 3; AAC39661)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> S (in Ref. 1; AAB66315 and 2; CAA73606)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> S (in Ref. 5; BAG62924)"
FT /evidence="ECO:0000305"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2DNC"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2DNC"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2F60"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:2F60"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2F60"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2F60"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:2F60"
SQ SEQUENCE 501 AA; 54122 MW; 9CF0C1DAE9E12EF9 CRC64;
MAASWRLGCD PRLLRYLVGF PGRRSVGLVK GALGWSVSRG ANWRWFHSTQ WLRGDPIKIL
MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV TLDASDDGIL AKIVVEEGSK
NIRLGSLIGL IVEEGEDWKH VEIPKDVGPP PPVSKPSEPR PSPEPQISIP VKKEHIPGTL
RFRLSPAARN ILEKHSLDAS QGTATGPRGI FTKEDALKLV QLKQTGKITE SRPTPAPTAT
PTAPSPLQAT AGPSYPRPVI PPVSTPGQPN AVGTFTEIPA SNIRRVIAKR LTESKSTVPH
AYATADCDLG AVLKVRQDLV KDDIKVSVND FIIKAAAVTL KQMPDVNVSW DGEGPKQLPF
IDISVAVATD KGLLTPIIKD AAAKGIQEIA DSVKALSKKA RDGKLLPEEY QGGSFSISNL
GMFGIDEFTA VINPPQACIL AVGRFRPVLK LTEDEEGNAK LQQRQLITVT MSSDSRVVDD
ELATRFLKSF KANLENPIRL A
