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UniProtKB/Swiss-Prot entry P21873

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA_BACST
Primary accession number P21873
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 62)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonym EC 1.2.4.1
Gene name
Name: pdhA
From
Bacillus stearothermophilus (Geobacillus stearothermophilus) [TaxID: 1422] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924;
PubMed=2200674 [NCBI, ExPASy, EBI, Israel, Japan]
Hawkins C.F., Borges A., Perham R.N.;
"Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.";
Eur. J. Biochem. 191:337-346(1990).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Heterodimer of an alpha and a beta chain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X53560; CAA37628.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S10798; DEBSPF.
3D structure databases
PDB
1W85; X-ray; 2.00 A; A/C/E/G=1-369.[ExPASy / RCSB / EBI]
1W88; X-ray; 2.30 A; A/C/E/G=1-369.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1W85; -.
1W88; -.
ModBase P21873.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
ProtoNet P21873.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycolysis; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   369  368     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000162198
MOD_RES   284   284        Phosphoserine. 
HELIX   10    19  10      
HELIX   36    38  3      
HELIX   44    69  26      
HELIX   83    91  9      
STRAND   98   100  3      
HELIX   106   111  6      
HELIX   116   124  9      
HELIX   127   130  4      
HELIX   147   161  15      
STRAND   168   173  6      
HELIX   175   178  4      
HELIX   180   191  12      
STRAND   196   202  7      
STRAND   204   206  3      
HELIX   211   213  3      
HELIX   221   226  6      
STRAND   231   235  5      
HELIX   239   254  16      
STRAND   260   265  6      
HELIX   285   292  8      
HELIX   296   306  11      
HELIX   312   334  23      
HELIX   341   346  6      
HELIX   354   366  13      
Sequence information
Length: 369 AA [This is the length of the unprocessed precursor] Molecular weight: 41469 Da [This is the MW of the unprocessed precursor] CRC64: DBF43982C0E1926D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGVKTFQFPF AEQLEKVAEQ FPTFQILNEE GEVVNEEAMP ELSDEQLKEL MRRMVYTRIL 

        70         80         90        100        110        120 
DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL PGYRDVPQII WHGLPLYQAF 

       130        140        150        160        170        180 
LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI QAAGVALGLK MRGKKAVAIT YTGDGGTSQG 

       190        200        210        220        230        240 
DFYEGINFAG AFKAPAIFVV QNNRFAISTP VEKQTVAKTL AQKAVAAGIP GIQVDGMDPL 

       250        260        270        280        290        300 
AVYAAVKAAR ERAINGEGPT LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF 

       310        320        330        340        350        360 
RKFLEAKGLW SEEEENNVIE QAKEEIKEAI KKADETPKQK VTDLISIMFE ELPFNLKEQY 


EIYKEKESK
P21873 in FASTA format

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