Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P21873 (ODPA_BACST)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit alpha
    EC=1.2.4.1
Gene names
Name: pdhA
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. 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 structure

Heterodimer of an alpha and a beta chain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 369368Pyruvate dehydrogenase E1 component subunit alpha
PRO_0000162198

Secondary structure

................................................. 369
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21873-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DBF43982C0E1926D

FASTA36941,469
        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 

« Hide

References

[1]"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."
Hawkins C.F., Borges A., Perham R.N.
Eur. J. Biochem. 191:337-346(1990) [PubMed: 2200674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35; 54-111 AND 269-331.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
+Additional computationally mapped references.

Cross-references

Sequence databases

X53560 Genomic DNA. Translation: CAA37628.1.
PIRDEBSPF. S10798.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1W85X-ray2.00A/C/E/G2-368[»]
1W88X-ray2.30A/C/E/G2-368[»]
3DUFX-ray2.50A/C/E/G1-369[»]
3DV0X-ray2.50A/C/E/G1-369[»]
3DVAX-ray2.35A/C/E/G1-369[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.4.1. 266715.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017596. Pyrv_DH_E1_asu_subgrp-x.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_BACST
AccessionPrimary (citable) accession number: P21873
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents