Protein Overview: PDX1

General Information:
Name(s) found:	PDX1 / YGR193C [SGD]
Description(s) found: SHOW ONLY BEST	gi\|755798\|emb\|CAA57804.1\| G7579 [Saccharomyces cerevisiae] [NCBI NR] pir\|\|DEBYPX pyruvate dehydrogenase complex protein X precursor - yeast (Saccharomyces cerevisiae) [NCBI NR] gi\|6321632\|ref\|NP_011709.1\| Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferas [NCBI NR] gi\|172268\|gb\|AAA34910.1\| protein X precursor [NCBI NR] gi\|1323343\|emb\|CAA97219.1\| PDX1 [Saccharomyces cerevisiae] [NCBI NR] gi\|129072\|sp\|P16451.1\|ODPX_YEAST RecName: Full=Pyruvate dehydrogenase complex protein X component, mitochondrial; AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex; AltName: Full=E3-binding protein; AltName: Fu [NCBI NR] Pyruvate dehydrogenase complex protein X component, mitochondrial OS=Saccharomyces cerevisiae GN=PDX1 PE=1 SV=1 [Swiss-Prot] PDX1 Pyruvate dehydrogenase complex protein X [mips] Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core [SGD] PDX1, Chr VII from 884504-885736, reverse complement [yeast_orfs2] Chr VII from 884504-885736, reverse complement [yeastorf3.fasta] Chr VII from 884511-885743, reverse complement [yeastorf4.fasta] Chr VII from 885743-884511, reverse complement [yeastorf5.fasta] (P16451) Pyruvate dehydrogenase protein X component, mitochondrial precursor (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (E3-binding protein) (E3BP) [4932.FASTACCERV.txt] PDX1 SGDID:S0003425, Chr VII from 885744-884512, reverse complement, Verified ORF [yeastflysequest.fasta] PDX1 SGDID:S0003425, Chr VII from 885746-884514, reverse complement, Verified ORF [10112005cervSGD.fasta] Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core [Saccharomyces c [nrdb_11152004_Chlamydomonas] PDX1 SGDID:S000003425, Chr VII from 885746-884514, reverse complement, Verified ORF, "Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding a [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta] protein X precursor [nr-271106-contam.fasta] G7579 [Saccharomyces cerevisiae] [nr-271106-contam.fasta] PDX1 [Saccharomyces cerevisiae] [nr-271106-contam.fasta] Pyruvate dehydrogenase complex protein X component, mitochondrial precursor (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (E3-binding protein) (Pyruvate dehydrogenase complex component E3BP) [nr-271106-contam.fasta] Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core; Pdx1p [Saccharo [nr-271106-contam.fasta] PDX1 SGDID:S000003425, Chr VII from 885746-884514, reverse complement, Verified ORF, "Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core" [yeast-bovrabprots.fasta] [chemostatdb.fasta] Pyruvate dehydrogenase complex protein X component, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PDX1 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta] PDX1 SGDID:S000003425, Chr VII from 885741-884509, Genome Release 64-1-1, reverse complement, Verified ORF, "Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core" [yeast-030211-contam.fasta] PDX1 SGDID:S000003425, Chr VII from 885741-884509, Genome Release 64-2-1, reverse complement, Verified ORF, "E3-binding protein of the mitochondrial pyruvate dehydrogenase complex; plays a structural role in the complex by binding and positioning dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide acetyltransferase (E2) core" [20141208_orf_trans.fasta] YGR193C SGDID:S000003425, Chr VII from 885741-884509, Genome Release 64-1-1, reverse complement, Verified ORF, "Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
Organism:	Saccharomyces cerevisiae
Length:	410 amino acids
Gene Ontology:
Cellular Component:	mitochondrial pyruvate dehydrogenase complex [TAS] mitochondrion [IDA ][TAS]
Biological Process:	acetyl-CoA biosynthetic process from pyruvate [TAS]
Molecular Function:	protein binding [IDA][IMP]

Sequence:

Sequence:
[PDR BLAST]
[ProtParam]

      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MLSAISKVST LKSCTRYLTK CNYHASAKLL AVKTFSMPAM SPTMEKGGIV SWKYKVGEPF  60
   61 SAGDVILEVE TDKSQIDVEA LDDGKLAKIL KDEGSKDVDV GEPIAYIADV DDDLATIKLP 120
  121 QEANTANAKS IEIKKPSADS TEATQQHLKK ATVTPIKTVD GSQANLEQTL LPSVSLLLAE 180
  181 NNISKQKALK EIAPSGSNGR LLKGDVLAYL GKIPQDSVNK VTEFIKKNER LDLSNIKPIQ 240
  241 LKPKIAEQAQ TKAADKPKIT PVEFEEQLVF HAPASIPFDK LSESLNSFMK EAYQFSHGTP 300
  301 LMDTNSKYFD PIFEDLVTLS PREPRFKFSY DLMQIPKANN MQDTYGQEDI FDLLTGSDAT 360
  361 ASSVRPVEKN LPEKNEYILA LNVSVNNKKF NDAEAKAKRF LDYVRELESF

Protein Complex Data

	PUBLICATION	TOPOLOGY	COCOMPLEXED PROTEINS
View Details	Riffle et al. (2010) (Unpublished Data)		LAT1 PDA1 PDX1
View Details	(MIPS) Mewes HW, et al. (2004)		LAT1 LPD1 PDA1 PDB1 PDX1
View Details	Gavin AC, et al. (2006)		LAT1 PDA1 PDB1 PDX1
View Details	Gavin AC, et al. (2002)		APM1 CYM1 DOA4 DUR1,2 HSP42 LAT1 LPD1 PDA1 PDB1 PDX1 PRP46 RPN11 TCM62
View Details	Ho Y, et al. (2002)		ATP3 AVO1 CCT5 CLU1 DHH1 DPB2 FUN12 GAL7 GPH1 HHF1, HHF2 IDH1 ILV2 MET16 MKK2 NOG2 NPA3 PDX1 PHO85 PUF3 RAD16 RPN12 SIS1 SLX1 SRP54 STI1 TEM1 TFC7 VMA8 YER077C YGR266W YKR051W YKU80 YLR271W YPR003C
View Details	Qiu et al. (2008)		LAT1 LPD1 PDA1 PDB1 PDX1

Mass Spectrometry Data

The following runs contain data for this protein:

	BAIT	COMMENTS	PUBLICATION
View Run	DAD1	Dam1-765 complex purified from yeast with Dad1-TAP	Shimogawa MM, et al. (2006)
View Run	BOI1	Sample boi 1 with ha tag from october 2005	McCusker D, et al (2007)
View Run	VAM3	sample: hx3	Hao Xu, et al. (2010)
View Run	VAM3	Sample: HX11 - both fusion and trans-SNARE complex formation take place.	Hao Xu, et al. (2010)
View Run	VAM3	Sample: HX12 - trans-SNARE complex formation and fusion are inhibited (control).	Hao Xu, et al. (2010)
View Run	VAM3	Sample: HX13 - trans-SNARE complex forms but fusion is blocked.	Hao Xu, et al. (2010)
View Run	VAM3	Sample: HX14 - mixture in detergent (control).	Hao Xu, et al. (2010)

Yeast Two-Hybrid Data

The following interactions contain this protein:

SHOWING SINGLE HITS. [ Hide Single Hits ]

[View our yeast two-hybrid interpretation guidelines.]

	BAIT	PREY	HITS	PUBLICATION
View Screen	KAP104	PDX1	1	Unpublished Fields Lab Data
View Screen	PTC4	PDX1	1	Unpublished Fields Lab Data
View Screen	SWI5	PDX1	1	Unpublished Fields Lab Data
View Screen	AIM13	PDX1	1	Unpublished Fields Lab Data
View Screen	MET18	PDX1	1	Unpublished Fields Lab Data
View Screen	GSP1	PDX1	1	Unpublished Fields Lab Data

Microscopy / Localization Data

New Feature: Upload Your Own Microscopy Data

	PROTEIN(S)	PUBLICATION
View Data	PDX1	Huh WK, et al. (2003)

Protein Structure Data

[What does the above image mean?]
[View Top Sequence Alignments] [Show Ginzu Version Information]

Domains predicted:

#		Region(s)	Method	Confidence	Match Description
1	View Details	[1..147]	PSI-BLAST	163.522879	Ipoyl domain of dihydrolipoamide acetyltransferase
2	View Details	[148..218]	PSI-BLAST	4.045757	E3-binding domain of dihydrolipoamide succinyltransferase
3	View Details	[219..410]	PSI-BLAST	39.39794	Dihydrolipoamide succinyltransferase

Functions predicted (by domain):

Gene Ontology predictions

No functions predicted.

Term	Confidence	Notes
dihydrolipoyllysine-residue acetyltransferase activity	9.65061123545754	bayes_pls_golite062009
dihydrolipoamide S-acyltransferase activity	9.64995677986911	bayes_pls_golite062009
S-acetyltransferase activity	9.49696044977584	bayes_pls_golite062009
S-acyltransferase activity	8.45313874919036	bayes_pls_golite062009
pyruvate dehydrogenase activity	8.17557182322815	bayes_pls_golite062009
pyruvate dehydrogenase (acetyl-transferring) activity	6.40483178382327	bayes_pls_golite062009
acetyltransferase activity	6.08159176722072	bayes_pls_golite062009
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor	5.93985773477717	bayes_pls_golite062009
transferase activity, transferring acyl groups other than amino-acyl groups	5.74314131636952	bayes_pls_golite062009
acyltransferase activity	5.72047003788767	bayes_pls_golite062009
transferase activity, transferring acyl groups	4.60481199262496	bayes_pls_golite062009
S-succinyltransferase activity	4.10308166636667	bayes_pls_golite062009
dihydrolipoyllysine-residue succinyltransferase activity	4.10308166636667	bayes_pls_golite062009
carnitine O-acyltransferase activity	2.87366177129153	bayes_pls_golite062009
succinyltransferase activity	2.08404693277798	bayes_pls_golite062009
oxidoreductase activity, acting on the aldehyde or oxo group of donors	1.78431187655869	bayes_pls_golite062009
catalytic activity	1.51562638409295	bayes_pls_golite062009
O-acyltransferase activity	1.33852311685118	bayes_pls_golite062009
O-palmitoyltransferase activity	1.22729402619659	bayes_pls_golite062009
carnitine O-palmitoyltransferase activity	1.22729402619659	bayes_pls_golite062009
transferase activity	1.08341671157927	bayes_pls_golite062009
carnitine O-acetyltransferase activity	1.00868366840715	bayes_pls_golite062009
O-acetyltransferase activity	0.1424856707148	bayes_pls_golite062009

No functions predicted.

Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076

Philius Transmembrane Prediction:

Protein predicted to be:	GLOBULAR (No transmembrane regions or signal peptide)
Confidence of classification:	0.99

Source: Reynolds et al. (2008)

TMHMM	2.0c	PSIPRED	v2.61
SignalP	3.0	COILS	1999
DISOPRED	v0.1	NCBI nr	06/2007
PSI-BLAST	2.2.18	FFAS	ffas03
PDB	06/2007	Pfam	22
HMMER	2.3.2