ID ODPX_BOVIN Reviewed; 501 AA.
AC P22439; Q0P576;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=Pyruvate dehydrogenase protein X component;
DE AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE AltName: Full=E3-binding protein;
DE Short=E3BP;
DE AltName: Full=proX;
DE Flags: Precursor;
GN Name=PDHX; Synonyms=PDX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 54-81 AND 184-201, AND VARIANT GLY-72.
RX PubMed=2914903; DOI=10.1016/s0021-9258(18)94165-7;
RA Rahmatullah M., Gopalakrishnan S., Andrews P.C., Chang C.L., Radke G.A.,
RA Roche T.E.;
RT "Subunit associations in the mammalian pyruvate dehydrogenase complex.
RT Structure and role of protein X and the pyruvate dehydrogenase component
RT binding domain of the dihydrolipoyl transacetylase component.";
RL J. Biol. Chem. 264:2221-2227(1989).
RN [3]
RP PROTEIN SEQUENCE OF 54-75, AND VARIANT GLY-66.
RX PubMed=2759236; DOI=10.1016/0014-5793(89)80919-6;
RA Neagle J., de Marcucci O., Dunbar B., Lindsay J.G.;
RT "Component X of mammalian pyruvate dehydrogenase complex: structural and
RT functional relationship to the lipoate acetyltransferase (E2) component.";
RL FEBS Lett. 253:11-15(1989).
RN [4]
RP PROTEIN SEQUENCE OF 54-75.
RX PubMed=1505515; DOI=10.1002/j.1460-2075.1992.tb05400.x;
RA Rice J.E., Dunbar B., Lindsay J.G.;
RT "Sequences directing dihydrolipoamide dehydrogenase (E3) binding are
RT located on the 2-oxoglutarate dehydrogenase (E1) component of the mammalian
RT 2-oxoglutarate dehydrogenase multienzyme complex.";
RL EMBO J. 11:3229-3235(1992).
RN [5]
RP 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:20361979). This core binds multiple copies of
CC pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide
CC acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (By
CC similarity). Interacts with SIRT4 (By similarity). Interacts with DLD
CC (By similarity). {ECO:0000250|UniProtKB:O00330,
CC ECO:0000269|PubMed:20361979}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD
CC complex activity. {ECO:0000250|UniProtKB:O00330}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC120413; AAI20414.1; -; mRNA.
DR PIR; A32040; A32040.
DR RefSeq; NP_001069219.1; NM_001075751.1.
DR AlphaFoldDB; P22439; -.
DR SMR; P22439; -.
DR CORUM; P22439; -.
DR STRING; 9913.ENSBTAP00000024307; -.
DR PaxDb; 9913-ENSBTAP00000024307; -.
DR PeptideAtlas; P22439; -.
DR Ensembl; ENSBTAT00000024307.6; ENSBTAP00000024307.5; ENSBTAG00000018261.6.
DR GeneID; 517402; -.
DR KEGG; bta:517402; -.
DR CTD; 8050; -.
DR VEuPathDB; HostDB:ENSBTAG00000018261; -.
DR VGNC; VGNC:32695; PDHX.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000156046; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; P22439; -.
DR OMA; TIKQKPW; -.
DR OrthoDB; 5483022at2759; -.
DR TreeFam; TF332256; -.
DR Reactome; R-BTA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-BTA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-BTA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-BTA-70268; Pyruvate metabolism.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000018261; Expressed in infraspinatus muscle and 106 other cell types or tissues.
DR ExpressionAtlas; P22439; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Lipoyl; Mitochondrion;
KW 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 /id="PRO_0000162301"
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 141..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..252
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:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00330"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKZ9"
FT VARIANT 66
FT /note="P -> G"
FT /evidence="ECO:0000269|PubMed:2759236"
FT VARIANT 72
FT /note="N -> G"
FT /evidence="ECO:0000269|PubMed:2914903"
FT CONFLICT 55
FT /note="D -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 53886 MW; A52F1813706AAD5B CRC64;
MAASWRLGCD PRLLRCLLGF GSRRSPELVK GAARWSVGRG ASWRWFHSTQ WLRADPIKIL
MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV TLDASDDGIL AKIVVAEGSK
NIRLGSLIGL LVEEGEDWKH VEIPKDTGPP PPAAKPSVPP PSAEPQIATP VKKEHPPGKV
QFRLSPAARN ILEKHALDAN QGTATGPRGI FTKEDALKLV QLKQTGKITE PRPTAALPTT
PAAPLPPQAA ATASYPRPMI PPVSTPGQPN VEGTFTEIPA SNIRRVIAKR LTESKSTIPH
AYATTDCDLG AVLTARQNLV RDDIKVSVND FIIKAAAVTL KQMPNVNASW DGEGAKQLPS
IDISVAVATD RGLITPVIKD AAAKGLQEIA DSVKALSKKA RDGKLLPEEY QGGSFSISNL
GMFGIDEFTA VINPPQACIL AVGRFRPVLK LTQDEEGNAQ LQQRQLITVT MSSDSRVVDD
ELATRFLESF KANLENPLRL A
//
