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P21874 (ODPB_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta

EC=1.2.4.1
Gene names
Name:pdhB
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length325 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.

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 325324Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162221

Sites

Binding site601Thiamine pyrophosphate By similarity

Secondary structure

........................................................................ 325
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21874 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AD1F2D4F82D652AC

FASTA32535,460
        10         20         30         40         50         60 
MAQMTMVQAI TDALRIELKN DPNVLIFGED VGVNGGVFRA TEGLQAEFGE DRVFDTPLAE 

        70         80         90        100        110        120 
SGIGGLAIGL ALQGFRPVPE IQFFGFVYEV MDSICGQMAR IRYRTGGRYH MPITIRSPFG 

       130        140        150        160        170        180 
GGVHTPELHS DSLEGLVAQQ PGLKVVIPST PYDAKGLLIS AIRDNDPVIF LEHLKLYRSF 

       190        200        210        220        230        240 
RQEVPEGEYT IPIGKADIKR EGKDITIIAY GAMVHESLKA AAELEKEGIS AEVVDLRTVQ 

       250        260        270        280        290        300 
PLDIETIIGS VEKTGRAIVV QEAQRQAGIA ANVVAEINER AILSLEAPVL RVAAPDTVYP 

       310        320 
FAQAESVWLP NFKDVIETAK KVMNF 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]"Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
Borges A., Hawkins C.F., Packman L.C., Perham R.N.
Eur. J. Biochem. 194:95-102(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53560 Genomic DNA. Translation: CAA37629.1.
PIRS14230.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W85X-ray2.00B/D/F/H2-325[»]
1W88X-ray2.30B/D/F/H2-325[»]
3DUFX-ray2.50B/D/F/H1-325[»]
3DV0X-ray2.50B/D/F/H1-325[»]
3DVAX-ray2.35B/D/F/H1-325[»]
ProteinModelPortalP21874.
SMRP21874. Positions 2-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29597N.
IntActP21874. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP21874.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP21874.

Entry information

Entry nameODPB_GEOSE
AccessionPrimary (citable) accession number: P21874
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references