PDC5_YEAST - dbPTM
PDC5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDC5_YEAST
UniProt AC P16467
Protein Name Pyruvate decarboxylase isozyme 2
Gene Name PDC5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 563
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Second most abundant 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..
Protein Sequence MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKLLETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQFPVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYSYKTKNIVEFHSDHIKIRNATFPGVQMKFALQKLLDAIPEVVKDYKPVAVPARVPITKSTPANTPMKQEWMWNHLGNFLREGDIVIAETGTSAFGINQTTFPTDVYAIVQVLWGSIGFTVGALLGATMAAEELDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYIFVLNNNGYTIEKLIHGPHAEYNEIQGWDHLALLPTFGARNYETHRVATTGEWEKLTQDKDFQDNSKIRMIEVMLPVFDAPQNLVKQAQLTAATNAKQ
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
8UbiquitinationMSEITLGKYLFERLS
CCCCHHHHHHHHHHH		41.7224961812
41AcetylationLDKLYEVKGMRWAGN
HHHHHHHCCCCCCCC		34.7417397211
179UbiquitinationVDLNVPAKLLETPID
EECCCCHHHCCCCCC		47.7517644757
190AcetylationTPIDLSLKPNDAEAE
CCCCCCCCCCCHHHH		38.1022865919
223PhosphorylationILADACASRHDVKAE
EEEHHHCCCCCCHHH		29.9923749301
259PhosphorylationIDEQHPRYGGVYVGT
CCCCCCCCCCEEEEC		23.7628889911
266PhosphorylationYGGVYVGTLSRPEVK
CCCEEEECCCCHHHH		16.12-
278PhosphorylationEVKKAVESADLILSI
HHHHHHHHHHHHHHH		22.0819779198
290PhosphorylationLSIGALLSDFNTGSF
HHHHHHHHCCCCCCC		40.7919779198
294PhosphorylationALLSDFNTGSFSYSY
HHHHCCCCCCCCCEE		33.9128889911
296PhosphorylationLSDFNTGSFSYSYKT
HHCCCCCCCCCEEEC		14.6928889911
300PhosphorylationNTGSFSYSYKTKNIV
CCCCCCCEEECCCEE		20.9627214570
302UbiquitinationGSFSYSYKTKNIVEF
CCCCCEEECCCEEEE		47.2722817900
304UbiquitinationFSYSYKTKNIVEFHS
CCCEEECCCEEEEEC		40.2922817900
311PhosphorylationKNIVEFHSDHIKIRN
CCEEEEECCCEEECC		35.8828889911
320PhosphorylationHIKIRNATFPGVQMK
CEEECCCCCCCHHHH		33.6322369663
463UbiquitinationTMIRWGLKPYIFVLN
HHHHCCCCCEEEEEC		31.6624961812
478UbiquitinationNNGYTIEKLIHGPHA
CCCEEEEHHCCCCCH		49.2217644757
522PhosphorylationTGEWEKLTQDKDFQD
CCCHHHHCCCCCCCC		45.87-
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 PDC5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDC5_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 PDC5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDC6_YEASTPDC6genetic
9748245
PDC6_YEASTPDC6genetic
16941010
G3P3_YEASTTDH3genetic
20093466
DS1P2_YEASTYSR3genetic
20093466
CORO_YEASTCRN1genetic
20093466
ERG2_YEASTERG2genetic
20093466
DCOR_YEASTSPE1genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
PDC5_YEASTPDC5physical
22940862
PDC1_YEASTPDC1physical
22940862
MTH1_YEASTMTH1genetic
22978798
MGA2_YEASTMGA2genetic
27708008
MET5_YEASTMET5genetic
27708008
ERG2_YEASTERG2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDC5_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND MASSSPECTROMETRY.

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