PDC1/YLR044C Protein Information Help

Standard Name Pdc1p 1, 2
Systematic Name Ylr044cp
ORF Classification Verified
Description Major of three pyruvate decarboxylase isozymes, key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde; subject to glucose-, ethanol-, and autoregulation; involved in amino acid catabolism (1, 3, 4, 5, 6, 7)
Name Description Pyruvate DeCarboxylase 8
Experimental Data
Molecules/cell 8970 9
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 563
Molecular Weight (Da) 61,495
Isoelectric Point (pI) 6.12

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Pdc1p (InterPro)
Physical Interactions There are 67 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052E05 | P06169
MIPS: YLR044C
NCBI: 1181265 | 1360375 | 157879677 | 157879678 | 2204264 | 222142966 | 222142967 | 222142968 | 222142969 | 222142974 | 222142975 | 222142976 | 222142977 | 222446954 | 222446955 | 222446956 | 222446957 | 30923172 | 4109 | 515236 | 515237 | 6323073 | 7245976 | 7245977 | 871533 | NP_013145.1
GenBank/EMBL/DDBJ: DAA09362.1 | X04675 | X77312 | X77315 | X77316 | X94607 | Z73216 | Z73217
External Classifications EC: 4.1.1.- [Carboxy-Lyases]
EC: 4.1.1.1 [Pyruvate decarboxylase]
EC: 4.1.1.72 [Branched-chain-2-oxoacid decarboxylase]
EC: 4.1.1.74 [Indolepyruvate decarboxylase]
Amino Acid Sequence (or in FASTA format)
       1  MSEITLGKYL FERLKQVNVN TVFGLPGDFN LSLLDKIYEV EGMRWAGNAN
      51  ELNAAYAADG YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG
     101  VPSISAQAKQ LLLHHTLGNG DFTVFHRMSA NISETTAMIT DIATAPAEID
     151  RCIRTTYVTQ RPVYLGLPAN LVDLNVPAKL LQTPIDMSLK PNDAESEKEV
     201  IDTILALVKD AKNPVILADA CCSRHDVKAE TKKLIDLTQF PAFVTPMGKG
     251  SIDEQHPRYG GVYVGTLSKP EVKEAVESAD LILSVGALLS DFNTGSFSYS
     301  YKTKNIVEFH SDHMKIRNAT FPGVQMKFVL QKLLTTIADA AKGYKPVAVP
     351  ARTPANAAVP ASTPLKQEWM WNQLGNFLQE GDVVIAETGT SAFGINQTTF
     401  PNNTYGISQV LWGSIGFTTG ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT
     451  VQEISTMIRW GLKPYLFVLN NDGYTIEKLI HGPKAQYNEI QGWDHLSLLP
     501  TFGAKDYETH RVATTGEWDK LTQDKSFNDN SKIRMIEIML PVFDAPQNLV
     551  EQAKLTAATN AKQ*                                       

external links for Pdc1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Pdc1p
1) Kellermann E, et al.  (1986) Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae. Nucleic Acids Res 14(22):8963-77
2) Schmitt HD, et al.  (1983) The synthesis of yeast pyruvate decarboxylase is regulated by large variations in the messenger RNA level. Mol Gen Genet 192(1-2):247-52
3) Hohmann S  (1991) Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae. J Bacteriol 173(24):7963-9
4) Liesen T, et al.  (1996) ERA, a novel cis-acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae. Mol Microbiol 21(3):621-32
5) Hohmann S and Cederberg H  (1990) Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5. Eur J Biochem 188(3):615-21
6) Pronk JT, et al.  (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33
7) Dickinson JR, et al.  (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34
8) Schmitt HD and Zimmermann FK  (1982) Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis. J Bacteriol 151(3):1146-52
9) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41