P32473 (ODPB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
EC=1.2.4.1

Alternative name(s):
Pyruvate dehydrogenase complex component E1 beta
Short name=PDHE1-B

Gene names

Name:	PDB1
Ordered Locus Names:	YBR221C
ORF Names:	YBR1511

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Subunit structure	Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 9970 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7947791. Source: SGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial nucleoid Inferred from direct assay PubMed 15692048. Source: SGD mitochondrial pyruvate dehydrogenase complex Inferred from direct assay PubMed 2007123. Source: SGD
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from mutant phenotype Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion Ref.1
	Chain	34 – 366	333	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000020461
Sites
	Binding site	95	1	Thiamine pyrophosphate By similarity
Experimental info
	Sequence conflict	160	1	V → L in AAA34583. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32473 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 547FD49ED2CB8A97	FASTA	366	40,054
	10 20 30 40 50 60 MFSRLPTSLA RNVARRAPTS FVRPSAAAAA LRFSSTKTMT VREALNSAMA EELDRDDDVF 70 80 90 100 110 120 LIGEEVAQYN GAYKVSKGLL DRFGERRVVD TPITEYGFTG LAVGAALKGL KPIVEFMSFN 130 140 150 160 170 180 FSMQAIDHVV NSAAKTHYMS GGTQKCQMVF RGPNGAAVGV GAQHSQDFSP WYGSIPGLKV 190 200 210 220 230 240 LVPYSAEDAR GLLKAAIRDP NPVVFLENEL LYGESFEISE EALSPEFTLP YKAKIEREGT 250 260 270 280 290 300 DISIVTYTRN VQFSLEAAEI LQKKYGVSAE VINLRSIRPL DTEAIIKTVK KTNHLITVES 310 320 330 340 350 360 TFPSFGVGAE IVAQVMESEA FDYLDAPIQR VTGADVPTPY AKELEDFAFP DTPTIVKAVK EVLSIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of PDH beta 1, the structural gene for the pyruvate dehydrogenase beta subunit from Saccharomyces cerevisiae." Miran S.G., Lawson J.E., Reed L.J. Proc. Natl. Acad. Sci. U.S.A. 90:1252-1256(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-54 AND 206-219.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M98476 Genomic DNA. Translation: AAA34583.1. Z36090 Genomic DNA. Translation: CAA85184.1. AY692982 Genomic DNA. Translation: AAT93001.1. BK006936 Genomic DNA. Translation: DAA07337.1.
PIR	S46097.
RefSeq	NP_009780.1. NM_001178569.1.
3D structure databases
ProteinModelPortal	P32473.
SMR	P32473. Positions 39-365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1499N.
IntAct	P32473. 33 interactions.
MINT	MINT-409839.
STRING	4932.YBR221C.
2D gel databases
SWISS-2DPAGE	P32473.
Proteomic databases
PaxDb	P32473.
PeptideAtlas	P32473.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR221C; YBR221C; YBR221C.
GeneID	852522.
KEGG	sce:YBR221C.
Organism-specific databases
CYGD	YBR221c.
SGD	S000000425. PDB1.
Phylogenomic databases
eggNOG	COG0022.
GeneTree	ENSGT00530000063423.
HOGENOM	HOG000281450.
KO	K00162.
OMA	QHSQDYS.
OrthoDB	EOG42RHGZ.
Gene expression databases
Genevestigator	P32473.
GermOnline	YBR221C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR027110. PDHB. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
PANTHER	PTHR11624:SF11. PTHR11624:SF11. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
ProtoNet	Search...
Other
NextBio	971562.

Entry information

Entry name

ODPB_YEAST

Accession

Primary (citable) accession number: P32473
Secondary accession number(s): D6VQL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program