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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)DescriptionActionsGraphical viewLength
Binding sitei60Thiamine pyrophosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001622212 – 325Pyruvate dehydrogenase E1 component subunit betaAdd BLAST324

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-29597N.
IntActiP21874. 1 interactor.

Structurei

Secondary structure

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 20Combined sources15
Beta strandi24 – 28Combined sources5
Beta strandi32 – 34Combined sources3
Turni40 – 43Combined sources4
Helixi44 – 48Combined sources5
Turni50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Helixi60 – 72Combined sources13
Beta strandi76 – 80Combined sources5
Helixi84 – 89Combined sources6
Helixi91 – 95Combined sources5
Helixi98 – 100Combined sources3
Helixi101 – 104Combined sources4
Turni105 – 107Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi121 – 123Combined sources3
Turni127 – 129Combined sources3
Helixi134 – 137Combined sources4
Beta strandi144 – 146Combined sources3
Helixi151 – 163Combined sources13
Beta strandi164 – 166Combined sources3
Beta strandi168 – 173Combined sources6
Turni174 – 176Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi197 – 200Combined sources4
Beta strandi203 – 209Combined sources7
Helixi213 – 226Combined sources14
Beta strandi231 – 235Combined sources5
Beta strandi237 – 241Combined sources5
Helixi244 – 254Combined sources11
Beta strandi257 – 264Combined sources8
Beta strandi267 – 269Combined sources3
Helixi270 – 281Combined sources12
Helixi282 – 284Combined sources3
Beta strandi290 – 294Combined sources5
Beta strandi296 – 299Combined sources4
Helixi302 – 304Combined sources3
Helixi305 – 308Combined sources4
Helixi312 – 323Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
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.
RefSeqiWP_033016213.1. NZ_LUCR01000041.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37629.1.
PIRiS14230.
RefSeqiWP_033016213.1. NZ_LUCR01000041.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29597N.
IntActiP21874. 1 interactor.

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/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
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...

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 2, 2016
This is version 100 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

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 one 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.