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YEAST:PDC1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) PDC1
Protein Name(s) Pyruvate decarboxylase isozyme 1
External Links
UniProt P06169
EMBL X04675
X77316
X94607
Z73216
Z73217
X77312
X77315
BK006945
PIR S64871
RefSeq NP_013145.1
PDB 1PVD
1PYD
1QPB
2VK1
2VK8
2W93
PDBsum 1PVD
1PYD
1QPB
2VK1
2VK8
2W93
ProteinModelPortal P06169
SMR P06169
BioGrid 31319
DIP DIP-6773N
IntAct P06169
MINT MINT-667063
COMPLUYEAST-2DPAGE P06169
SWISS-2DPAGE P06169
MaxQB P06169
PaxDb P06169
PeptideAtlas P06169
EnsemblFungi [example_ID YLR044C]
GeneID 850733
KEGG sce:YLR044C
SGD S000004034
eggNOG COG3961
GeneTree ENSGT00550000075465
InParanoid P06169
KO K01568
OMA LADACCS
OrthoDB EOG779P6S
BioCyc MetaCyc:MONOMER3O-117
YEAST:MONOMER3O-117
BRENDA 4.1.1.1
SABIO-RK P06169
UniPathway UPA00206
UPA00866
EvolutionaryTrace P06169
NextBio 966831
Proteomes UP000002311
Genevestigator P06169
GO GO:0005829
GO:0005634
GO:0047433
GO:0000287
GO:0004737
GO:0030976
GO:0000949
GO:0009083
GO:0019655
GO:0006559
GO:0006090
GO:0006569
Gene3D 3.40.50.1220
3.40.50.970
InterPro IPR029035
IPR029061
IPR012000
IPR012001
IPR000399
IPR012110
IPR011766
PANTHER PTHR18968:SF4
Pfam PF02775
PF00205
PF02776
PIRSF PIRSF036565
SUPFAM SSF52467
SSF52518
PROSITE PS00187

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005634

nucleus

PMID:14562095[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:14562095[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0047433

branched-chain-2-oxoacid decarboxylase activity

PMID:9546164[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019655

glycolytic fermentation to ethanol

PMID:2404950[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006569

tryptophan catabolic process

PMID:12499363[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000002788
SGD:S000003319
SGD:S000004124

P

Seeded From UniProt

complete

involved_in

GO:0006559

L-phenylalanine catabolic process

PMID:12499363[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000002788
SGD:S000003319
SGD:S000004124

P

Seeded From UniProt

complete

involved_in

GO:0006090

pyruvate metabolic process

PMID:2404950[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:2665820[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:16850348[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004737

pyruvate decarboxylase activity

PMID:23423327[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004737

pyruvate decarboxylase activity

PMID:2404950[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000949

aromatic amino acid family catabolic process to alcohol via Ehrlich pathway

PMID:12499363[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000002788
SGD:S000003319
SGD:S000004124

P

Seeded From UniProt

complete

enables

GO:0047433

branched-chain-2-oxoacid decarboxylase activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000004034
SGD:S000004124

F

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000438887
SGD:S000002238
SGD:S000002788

F

Seeded From UniProt

complete

involved_in

GO:0006569

tryptophan catabolic process

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000002788
SGD:S000003319
SGD:S000004034
SGD:S000004124

P

Seeded From UniProt

complete

involved_in

GO:0006559

L-phenylalanine catabolic process

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000002788
SGD:S000003319
SGD:S000004034
SGD:S000004124

P

Seeded From UniProt

complete

involved_in

GO:0006090

pyruvate metabolic process

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000004034
SGD:S000004124

P

Seeded From UniProt

complete

involved_in

GO:0006067

ethanol metabolic process

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000003319

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000438887
SGD:S000004034
TAIR:locus:2123827
TAIR:locus:2160170

C

Seeded From UniProt

complete

enables

GO:0004737

pyruvate decarboxylase activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000003319
SGD:S000004034
SGD:S000004124

F

Seeded From UniProt

complete

involved_in

GO:0000949

aromatic amino acid family catabolic process to alcohol via Ehrlich pathway

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001826953
SGD:S000002788
SGD:S000003319
SGD:S000004034
SGD:S000004124

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000399
InterPro:IPR012000

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011766

F

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012110

F

Seeded From UniProt

complete

enables

GO:0030976

thiamine pyrophosphate binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000399
InterPro:IPR011766
InterPro:IPR012000
InterPro:IPR012001

F

Seeded From UniProt

complete

enables

GO:0047433

branched-chain-2-oxoacid decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.72

F

Seeded From UniProt

complete

enables

GO:0047434

indolepyruvate decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.74

F

Seeded From UniProt

complete

enables

GO:0050177

phenylpyruvate decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.43

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

involved_in

GO:0006569

tryptophan catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0823

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0006559

L-phenylalanine catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0585

P

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0210

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0009083

branched-chain amino acid catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0101

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

involved_in

GO:0000955

amino acid catabolic process via Ehrlich pathway

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00866

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
  2. ↑ ter Schure, EG et al. (1998) Pyruvate decarboxylase catalyzes decarboxylation of branched-chain 2-oxo acids but is not essential for fusel alcohol production by Saccharomyces cerevisiae. Appl. Environ. Microbiol. 64 1303-7 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Seeboth, PG et al. (1990) pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: cloning of PDC5, a gene homologous to PDC1. J. Bacteriol. 172 678-85 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Dickinson, JR et al. (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J. Biol. Chem. 278 8028-34 PubMed GONUTS page
  5. ↑ van Urk, H et al. (1989) Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621. Biochim. Biophys. Acta 992 78-86 PubMed GONUTS page
  6. ↑ Mojzita, D & Hohmann, S (2006) Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces cerevisiae. Mol. Genet. Genomics 276 147-61 PubMed GONUTS page
  7. ↑ Agarwal, PK et al. (2013) Comparison of pyruvate decarboxylases from Saccharomyces cerevisiae and Komagataella pastoris (Pichia pastoris). Appl. Microbiol. Biotechnol. 97 9439-49 PubMed GONUTS page
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 8.7 8.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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