ID   Y1564_DICDI             Reviewed;         413 AA.
AC   Q86AD5; Q55AS9;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Pyruvate dehydrogenase complex subunit homolog DDB_G0271564, mitochondrial;
DE   Flags: Precursor;
GN   Name=pdhX; ORFNames=DDB_G0271564;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000006; EAL71646.1; -; Genomic_DNA.
DR   RefSeq; XP_645617.1; XM_640525.1.
DR   AlphaFoldDB; Q86AD5; -.
DR   SMR; Q86AD5; -.
DR   STRING; 44689.DDB0230192; -.
DR   PaxDb; Q86AD5; -.
DR   EnsemblProtists; EAL71646; EAL71646; DDB_G0271564.
DR   GeneID; 8618072; -.
DR   KEGG; ddi:DDB_G0271564; -.
DR   dictyBase; DDB_G0271564; pdhX.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_016733_10_2_1; -.
DR   InParanoid; Q86AD5; -.
DR   OMA; GHWAMRF; -.
DR   PhylomeDB; Q86AD5; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DDI-70268; Pyruvate metabolism.
DR   PRO; PR:Q86AD5; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:dictyBase.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:dictyBase.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   PANTHER; PTHR23151; PTHR23151; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..413
FT                   /note="Pyruvate dehydrogenase complex subunit homolog
FT                   DDB_G0271564, mitochondrial"
FT                   /id="PRO_0000391458"
FT   DOMAIN          29..67
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
SQ   SEQUENCE   413 AA;  45747 MW;  442B3D7F29623075 CRC64;
     MNRILKQVSN TKGKGIRFYS SSSQLDSEYM FPSVRRLLVE YGINSSKEVT ATGPQNRLLK
     GDVLAYIKTK NLSPVDRLSL IASSVKSSQP SSSSSPSIVD SPTLTSQIKD QIKIVTTITN
     DKNKSKVIYE DIPNNNIRRV IATKLSQSKQ QVPHFYMTVE CELDNVLAMR KSMPENVKIS
     VNDFVLRACA LALRDNPQAN SKWSDEHGEA ILNPTVDISF AVSTDRGLIT PIITNTDKKQ
     LLAISNESKQ LALKARDGKL KPEEFIGGTF SVSNLGMFGI TSFNAIINYP QAGILAIGTG
     RKVLRPPSTY QPIETNLNAS YGSEGKSEII NTNGPLTTEQ LEKLFDNTVS KKQDIKQQII
     NEQPQPPKYE QPKVANVMDV TLSGDNRVFD DEIAGKFLSS FKYYLSNPQN MIL