ID ODPX_YEAST Reviewed; 410 AA.
AC P16451; D6VUX5; E9P906;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 27-MAR-2024, entry version 199.
DE RecName: Full=Pyruvate dehydrogenase complex protein X component, mitochondrial;
DE AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE AltName: Full=E3-binding protein;
DE AltName: Full=Pyruvate dehydrogenase complex component E3BP;
DE Flags: Precursor;
GN Name=PDX1; OrderedLocusNames=YGR193C; ORFNames=G7579;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-60 AND
RP 192-206.
RX PubMed=2682658; DOI=10.1073/pnas.86.22.8732;
RA Behal R.H., Browning K.S., Hall T.B., Reed L.J.;
RT "Cloning and nucleotide sequence of the gene for protein X from
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8732-8736(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7645350; DOI=10.1002/yea.320110609;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 11:587-591(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP MUTAGENESIS.
RX PubMed=2007123; DOI=10.1021/bi00225a015;
RA Lawson J.E., Behal R.H., Reed L.J.;
RT "Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene
RT encoding the protein X component of the pyruvate dehydrogenase complex.";
RL Biochemistry 30:2834-2839(1991).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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: Eukaryotic pyruvate dehydrogenase (PDH) complexes are
CC organized as a core consisting of the oligomeric dihydrolipoamide
CC acetyl-transferase (E2), around which are arranged multiple copies of
CC pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and
CC protein X (E3BP) bound by non-covalent bonds.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M28222; AAA34910.1; -; Genomic_DNA.
DR EMBL; X82408; CAA57804.1; -; Genomic_DNA.
DR EMBL; Z72978; CAA97219.1; -; Genomic_DNA.
DR EMBL; AY692983; AAT93002.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08286.1; -; Genomic_DNA.
DR PIR; A36183; DEBYPX.
DR RefSeq; NP_011709.1; NM_001181322.1.
DR AlphaFoldDB; P16451; -.
DR SMR; P16451; -.
DR BioGRID; 33446; 93.
DR ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR DIP; DIP-5550N; -.
DR IntAct; P16451; 10.
DR MINT; P16451; -.
DR STRING; 4932.YGR193C; -.
DR SwissPalm; P16451; -.
DR MaxQB; P16451; -.
DR PaxDb; 4932-YGR193C; -.
DR PeptideAtlas; P16451; -.
DR EnsemblFungi; YGR193C_mRNA; YGR193C; YGR193C.
DR GeneID; 853107; -.
DR KEGG; sce:YGR193C; -.
DR AGR; SGD:S000003425; -.
DR SGD; S000003425; PDX1.
DR VEuPathDB; FungiDB:YGR193C; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_035825_2_1_1; -.
DR InParanoid; P16451; -.
DR OMA; NRFEVYD; -.
DR OrthoDB; 52212at2759; -.
DR BioCyc; YEAST:YGR193C-MONOMER; -.
DR BioGRID-ORCS; 853107; 1 hit in 10 CRISPR screens.
DR PRO; PR:P16451; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P16451; Protein.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:SGD.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
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:SF82; PYRUVATE DEHYDROGENASE COMPLEX PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 Direct protein sequencing; Lipoyl; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2682658"
FT CHAIN 31..410
FT /note="Pyruvate dehydrogenase complex protein X component,
FT mitochondrial"
FT /id="PRO_0000020487"
FT DOMAIN 32..108
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 169..210
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT MOD_RES 73
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 378
FT /note="I -> M (in Ref. 5; AAT93002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45362 MW; 11649CA28C420CDF CRC64;
MLSAISKVST LKSCTRYLTK CNYHASAKLL AVKTFSMPAM SPTMEKGGIV SWKYKVGEPF
SAGDVILEVE TDKSQIDVEA LDDGKLAKIL KDEGSKDVDV GEPIAYIADV DDDLATIKLP
QEANTANAKS IEIKKPSADS TEATQQHLKK ATVTPIKTVD GSQANLEQTL LPSVSLLLAE
NNISKQKALK EIAPSGSNGR LLKGDVLAYL GKIPQDSVNK VTEFIKKNER LDLSNIKPIQ
LKPKIAEQAQ TKAADKPKIT PVEFEEQLVF HAPASIPFDK LSESLNSFMK EAYQFSHGTP
LMDTNSKYFD PIFEDLVTLS PREPRFKFSY DLMQIPKANN MQDTYGQEDI FDLLTGSDAT
ASSVRPVEKN LPEKNEYILA LNVSVNNKKF NDAEAKAKRF LDYVRELESF
//
