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: -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.

Miscellaneous

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

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA biosynthetic process from pyruvate Source: SGD

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR193C
SGDiS000003425 PDX1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000002048731 – 410Pyruvate dehydrogenase complex protein X component, mitochondrialAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

MaxQBiP16451
PaxDbiP16451
PRIDEiP16451

PTM databases

SwissPalmiP16451

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

BioGridi3344670 interactors.
DIPiDIP-5550N
IntActiP16451 19 interactors.
MINTiP16451
STRINGi4932.YGR193C

Structurei

3D structure databases

ProteinModelPortaliP16451
SMRiP16451
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 108Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini169 – 210Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST42

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

HOGENOMiHOG000246828
InParanoidiP16451
OMAiKMPAMSP
OrthoDBiEOG092C3YQ0

Family and domain databases

Gene3Di4.10.320.101 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR000089 Biotin_lipoyl
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti378I → M in AAT93002 (PubMed:17322287).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiODPX_YEAST
AccessioniPrimary (citable) accession number: P16451
Secondary accession number(s): D6VUX5, E9P906
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: March 28, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome