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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

SABIO-RKP21874.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 325324Pyruvate dehydrogenase E1 component subunit betaPRO_0000162221Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-29597N.
IntActiP21874. 1 interaction.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi6 – 2015Combined sources
Beta strandi24 – 285Combined sources
Beta strandi32 – 343Combined sources
Turni40 – 434Combined sources
Helixi44 – 485Combined sources
Turni50 – 523Combined sources
Beta strandi53 – 553Combined sources
Helixi60 – 7213Combined sources
Beta strandi76 – 805Combined sources
Helixi84 – 896Combined sources
Helixi91 – 955Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 1044Combined sources
Turni105 – 1073Combined sources
Beta strandi114 – 1196Combined sources
Beta strandi121 – 1233Combined sources
Turni127 – 1293Combined sources
Helixi134 – 1374Combined sources
Beta strandi144 – 1463Combined sources
Helixi151 – 16313Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1736Combined sources
Turni174 – 1763Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi203 – 2097Combined sources
Helixi213 – 22614Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi237 – 2415Combined sources
Helixi244 – 25411Combined sources
Beta strandi257 – 2648Combined sources
Beta strandi267 – 2693Combined sources
Helixi270 – 28112Combined sources
Helixi282 – 2843Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi296 – 2994Combined sources
Helixi302 – 3043Combined sources
Helixi305 – 3084Combined sources
Helixi312 – 32312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP21874.
SMRiP21874. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21874.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQMTMVQAI TDALRIELKN DPNVLIFGED VGVNGGVFRA TEGLQAEFGE
60 70 80 90 100
DRVFDTPLAE SGIGGLAIGL ALQGFRPVPE IQFFGFVYEV MDSICGQMAR
110 120 130 140 150
IRYRTGGRYH MPITIRSPFG GGVHTPELHS DSLEGLVAQQ PGLKVVIPST
160 170 180 190 200
PYDAKGLLIS AIRDNDPVIF LEHLKLYRSF RQEVPEGEYT IPIGKADIKR
210 220 230 240 250
EGKDITIIAY GAMVHESLKA AAELEKEGIS AEVVDLRTVQ PLDIETIIGS
260 270 280 290 300
VEKTGRAIVV QEAQRQAGIA ANVVAEINER AILSLEAPVL RVAAPDTVYP
310 320
FAQAESVWLP NFKDVIETAK KVMNF
Length:325
Mass (Da):35,460
Last modified:January 23, 2007 - v2
Checksum:iAD1F2D4F82D652AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37629.1.
PIRiS14230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37629.1.
PIRiS14230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP21874.
SMRiP21874. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29597N.
IntActiP21874. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP21874.

Miscellaneous databases

EvolutionaryTraceiP21874.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiODPB_GEOSE
AccessioniPrimary (citable) accession number: P21874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.