PDC6_YEAST - dbPTM
PDC6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDC6_YEAST
UniProt AC P26263
Protein Name Pyruvate decarboxylase isozyme 3
Gene Name PDC6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 563
Subcellular Localization Cytoplasm .
Protein Description Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it cannot compensate for the other two pyruvate decarboxylases to sustain fermentation..
Protein Sequence MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIRLIELKLPVFDAPESLIKQAQLTAATNAKQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSEITLGKY
------CCCCHHHHH		37.39-
2Phosphorylation------MSEITLGKY
------CCCCHHHHH		37.3928152593
5Phosphorylation---MSEITLGKYLFE
---CCCCHHHHHHHH		25.9619823750
8UbiquitinationMSEITLGKYLFERLK
CCCCHHHHHHHHHHH		41.7224961812
9PhosphorylationSEITLGKYLFERLKQ
CCCHHHHHHHHHHHC		18.1521440633
218PhosphorylationSKNPVILSDACASRH
CCCCEEECHHHHHHC		16.4324909858
223PhosphorylationILSDACASRHNVKKE
EECHHHHHHCCCCHH		33.6824909858
251PhosphorylationVTPLGKGSIDEQHPR
ECCCCCCCCCCCCCC		30.2823749301
259PhosphorylationIDEQHPRYGGVYVGT
CCCCCCCCCCEEEEE		23.7628889911
266PhosphorylationYGGVYVGTLSKQDVK
CCCEEEEECCHHHHH		20.15-
294PhosphorylationALLSDFNTGSFSYSY
HHHHCCCCCCCEEEE		33.9128889911
296PhosphorylationLSDFNTGSFSYSYKT
HHCCCCCCCEEEEEC		14.6928889911
300PhosphorylationNTGSFSYSYKTKNVV
CCCCCEEEEECCCEE		20.9627214570
353PhosphorylationSVPVPTKTPANKGVP
CCCCCCCCCCCCCCC		30.06-
463UbiquitinationTMIRWGLKPYLFVLN
HHHHCCCCCEEEEEC		27.9023749301
478UbiquitinationNDGYTIEKLIHGPHA
CCCCEEHHHCCCCCC		49.2217644757
522PhosphorylationTGEWDALTTDSEFQK
CCCCCCCCCCCHHHH		30.2227017623
523PhosphorylationGEWDALTTDSEFQKN
CCCCCCCCCCHHHHC		38.0827017623
525PhosphorylationWDALTTDSEFQKNSV
CCCCCCCCHHHHCCC		37.9127017623
562UbiquitinationLTAATNAKQ------
HHHHHCCCC------		59.6223749301
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PDC6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDC6_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PDC6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACON2_YEASTACO2genetic
21623372
MET22_YEASTMET22genetic
21623372
THDH_YEASTILV1genetic
21623372
POS5_YEASTPOS5genetic
21623372
MTH1_YEASTMTH1genetic
22978798
SLX5_YEASTSLX5genetic
27708008
MRX3_YEASTYBL095Wgenetic
27708008
HPC2_YEASTHPC2genetic
27708008
ODPB_YEASTPDB1genetic
27708008
RM01_YEASTMRPL1genetic
27708008
DHAS_YEASTHOM2genetic
27708008
ODPA_YEASTPDA1genetic
27708008
ATC1_YEASTPMR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
TBP7_YEASTYTA7genetic
27708008
YOR1_YEASTYOR1genetic
27708008
PIH1_YEASTPIH1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
LRP1_YEASTLRP1genetic
27708008
DSE2_YEASTDSE2genetic
27708008
YIQ6_YEASTYIL166Cgenetic
27708008
JEM1_YEASTJEM1genetic
27708008
GSH1_YEASTGSH1genetic
27708008
FRA1_YEASTFRA1genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
ERG3_YEASTERG3genetic
27708008
LIPB_YEASTLIP2genetic
27708008
VPS9_YEASTVPS9genetic
27708008
HDA1_YEASTHDA1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
FAR11_YEASTFAR11genetic
27708008
IZH2_YEASTIZH2genetic
27708008
MDM12_YEASTMDM12genetic
27708008
SGT2_YEASTSGT2genetic
27708008
CY1_YEASTCYT1genetic
27708008
TCB1_YEASTTCB1genetic
27708008
YOR31_YEASTYOR131Cgenetic
27708008
LIPA_YEASTLIP5genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDC6_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294; SER-296 ANDSER-300, AND MASS SPECTROMETRY.

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