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Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

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

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-RKP21873.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001621982 – 369Pyruvate dehydrogenase E1 component subunit alphaAdd BLAST368

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-29596N.
IntActiP21873. 1 interactor.

Structurei

Secondary structure

1369
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 19Combined sources10
Helixi36 – 38Combined sources3
Helixi44 – 69Combined sources26
Helixi83 – 91Combined sources9
Beta strandi98 – 100Combined sources3
Beta strandi102 – 104Combined sources3
Helixi106 – 111Combined sources6
Helixi116 – 124Combined sources9
Helixi127 – 130Combined sources4
Helixi147 – 161Combined sources15
Beta strandi168 – 173Combined sources6
Helixi175 – 178Combined sources4
Helixi180 – 191Combined sources12
Beta strandi196 – 202Combined sources7
Beta strandi204 – 206Combined sources3
Helixi211 – 213Combined sources3
Helixi221 – 226Combined sources6
Beta strandi231 – 235Combined sources5
Helixi239 – 254Combined sources16
Beta strandi260 – 265Combined sources6
Beta strandi274 – 277Combined sources4
Helixi279 – 281Combined sources3
Helixi285 – 292Combined sources8
Helixi296 – 306Combined sources11
Helixi312 – 334Combined sources23
Helixi341 – 346Combined sources6
Helixi354 – 366Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W85X-ray2.00A/C/E/G2-369[»]
1W88X-ray2.30A/C/E/G2-369[»]
3DUFX-ray2.50A/C/E/G1-369[»]
3DV0X-ray2.50A/C/E/G1-369[»]
3DVAX-ray2.35A/C/E/G1-369[»]
ProteinModelPortaliP21873.
SMRiP21873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21873.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017596. PdhA/BkdA.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03181. PDH_E1_alph_x. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P21873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVKTFQFPF AEQLEKVAEQ FPTFQILNEE GEVVNEEAMP ELSDEQLKEL
60 70 80 90 100
MRRMVYTRIL DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL
110 120 130 140 150
PGYRDVPQII WHGLPLYQAF LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI
160 170 180 190 200
QAAGVALGLK MRGKKAVAIT YTGDGGTSQG DFYEGINFAG AFKAPAIFVV
210 220 230 240 250
QNNRFAISTP VEKQTVAKTL AQKAVAAGIP GIQVDGMDPL AVYAAVKAAR
260 270 280 290 300
ERAINGEGPT LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF
310 320 330 340 350
RKFLEAKGLW SEEEENNVIE QAKEEIKEAI KKADETPKQK VTDLISIMFE
360
ELPFNLKEQY EIYKEKESK
Length:369
Mass (Da):41,469
Last modified:January 23, 2007 - v2
Checksum:iDBF43982C0E1926D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37628.1.
PIRiS10798. DEBSPF.
RefSeqiWP_033016215.1. NZ_LUCR01000041.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53560 Genomic DNA. Translation: CAA37628.1.
PIRiS10798. DEBSPF.
RefSeqiWP_033016215.1. NZ_LUCR01000041.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W85X-ray2.00A/C/E/G2-369[»]
1W88X-ray2.30A/C/E/G2-369[»]
3DUFX-ray2.50A/C/E/G1-369[»]
3DV0X-ray2.50A/C/E/G1-369[»]
3DVAX-ray2.35A/C/E/G1-369[»]
ProteinModelPortaliP21873.
SMRiP21873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29596N.
IntActiP21873. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP21873.

Miscellaneous databases

EvolutionaryTraceiP21873.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017596. PdhA/BkdA.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODPA_GEOSE
AccessioniPrimary (citable) accession number: P21873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 96 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.