ID   ODPX_MESAU              Reviewed;          27 AA.
AC   P86238;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Pyruvate dehydrogenase protein X component, mitochondrial {ECO:0000250|UniProtKB:O00330};
DE   AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex {ECO:0000250|UniProtKB:O00330};
DE   AltName: Full=Lipoyl-containing pyruvate dehydrogenase complex component X {ECO:0000250|UniProtKB:O00330};
DE   Flags: Fragment;
GN   Name=PDHX {ECO:0000250|UniProtKB:O00330};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(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 (By similarity).
CC       {ECO:0000250|UniProtKB:O00330}.
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. This core binds multiple copies of pyruvate dehydrogenase
CC       (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
CC       (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). Interacts with SIRT4.
CC       Interacts with DLD. {ECO:0000250|UniProtKB:O00330}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:O00330}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86238; -.
DR   SMR; P86238; -.
DR   STRING; 10036.XP_005064912.1; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   Pfam; PF02817; E3_binding; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Lipoyl; Mitochondrion; Phosphoprotein; Reference proteome.
FT   CHAIN           <1..>27
FT                   /note="Pyruvate dehydrogenase protein X component,
FT                   mitochondrial"
FT                   /id="PRO_0000394422"
FT   DOMAIN          2..>27
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00330"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00330"
FT   NON_TER         1
FT   NON_TER         27
SQ   SEQUENCE   27 AA;  2894 MW;  EFCB3239BBD584E6 CRC64;
     FRLSPAARNI LEKHSLDASQ GTATGPR