Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate dehydrogenase complex protein X component, mitochondrial

Gene

PDX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA biosynthetic process from pyruvate Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:YGR193C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase complex protein X component, mitochondrial
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
E3-binding protein
Pyruvate dehydrogenase complex component E3BP
Gene namesi
Name:PDX1
Ordered Locus Names:YGR193C
ORF Names:G7579
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR193c.
EuPathDBiFungiDB:YGR193C.
SGDiS000003425. PDX1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial pyruvate dehydrogenase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
BLAST
Chaini31 – 410380Pyruvate dehydrogenase complex protein X component, mitochondrialPRO_0000020487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

MaxQBiP16451.
PaxDbiP16451.
PeptideAtlasiP16451.

Interactioni

Subunit structurei

Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.

Protein-protein interaction databases

BioGridi33446. 32 interactions.
DIPiDIP-5550N.
IntActiP16451. 8 interactions.
MINTiMINT-508924.
STRINGi4932.YGR193C.

Structurei

3D structure databases

ProteinModelPortaliP16451.
SMRiP16451. Positions 37-120, 169-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 10877Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000246828.
InParanoidiP16451.
OMAiEPIAYIA.
OrthoDBiEOG7W41P8.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSAISKVST LKSCTRYLTK CNYHASAKLL AVKTFSMPAM SPTMEKGGIV
60 70 80 90 100
SWKYKVGEPF SAGDVILEVE TDKSQIDVEA LDDGKLAKIL KDEGSKDVDV
110 120 130 140 150
GEPIAYIADV DDDLATIKLP QEANTANAKS IEIKKPSADS TEATQQHLKK
160 170 180 190 200
ATVTPIKTVD GSQANLEQTL LPSVSLLLAE NNISKQKALK EIAPSGSNGR
210 220 230 240 250
LLKGDVLAYL GKIPQDSVNK VTEFIKKNER LDLSNIKPIQ LKPKIAEQAQ
260 270 280 290 300
TKAADKPKIT PVEFEEQLVF HAPASIPFDK LSESLNSFMK EAYQFSHGTP
310 320 330 340 350
LMDTNSKYFD PIFEDLVTLS PREPRFKFSY DLMQIPKANN MQDTYGQEDI
360 370 380 390 400
FDLLTGSDAT ASSVRPVEKN LPEKNEYILA LNVSVNNKKF NDAEAKAKRF
410
LDYVRELESF
Length:410
Mass (Da):45,362
Last modified:August 1, 1990 - v1
Checksum:i11649CA28C420CDF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti378 – 3781I → M in AAT93002 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28222 Genomic DNA. Translation: AAA34910.1.
X82408 Genomic DNA. Translation: CAA57804.1.
Z72978 Genomic DNA. Translation: CAA97219.1.
AY692983 Genomic DNA. Translation: AAT93002.1.
BK006941 Genomic DNA. Translation: DAA08286.1.
PIRiA36183. DEBYPX.
RefSeqiNP_011709.1. NM_001181322.1.

Genome annotation databases

EnsemblFungiiYGR193C; YGR193C; YGR193C.
GeneIDi853107.
KEGGisce:YGR193C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28222 Genomic DNA. Translation: AAA34910.1.
X82408 Genomic DNA. Translation: CAA57804.1.
Z72978 Genomic DNA. Translation: CAA97219.1.
AY692983 Genomic DNA. Translation: AAT93002.1.
BK006941 Genomic DNA. Translation: DAA08286.1.
PIRiA36183. DEBYPX.
RefSeqiNP_011709.1. NM_001181322.1.

3D structure databases

ProteinModelPortaliP16451.
SMRiP16451. Positions 37-120, 169-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33446. 32 interactions.
DIPiDIP-5550N.
IntActiP16451. 8 interactions.
MINTiMINT-508924.
STRINGi4932.YGR193C.

Proteomic databases

MaxQBiP16451.
PaxDbiP16451.
PeptideAtlasiP16451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR193C; YGR193C; YGR193C.
GeneIDi853107.
KEGGisce:YGR193C.

Organism-specific databases

CYGDiYGR193c.
EuPathDBiFungiDB:YGR193C.
SGDiS000003425. PDX1.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000246828.
InParanoidiP16451.
OMAiEPIAYIA.
OrthoDBiEOG7W41P8.

Enzyme and pathway databases

BioCyciYEAST:YGR193C-MONOMER.

Miscellaneous databases

NextBioi973115.
PROiP16451.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae."
    Behal R.H., Browning K.S., Hall T.B., Reed L.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:8732-8736(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-60 AND 192-206.
  2. "The complete sequence of a 9037 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
    Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.
    Yeast 11:587-591(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex."
    Lawson J.E., Behal R.H., Reed L.J.
    Biochemistry 30:2834-2839(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiODPX_YEAST
AccessioniPrimary (citable) accession number: P16451
Secondary accession number(s): D6VUX5, E9P906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 24, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 414 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.