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Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 2 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) (By similarity).By similarity

Catalytic activityi

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

Cofactori

thiamine diphosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis, Stress response

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha (EC:1.2.4.1)
Gene namesi
Name:pdhAImported
ORF Names:BCE_G9241_3962
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 371370Pyruvate dehydrogenase E1 component subunit alphaPRO_0000271255Add
BLAST

Expressioni

Inductioni

By acid stress. Under acid-stress, this protein is expressed at a higher level in wild-type B.cereus than in the acid-sensitive mutant strain NB1.1 Publication

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.Curated

Protein-protein interaction databases

STRINGi226900.BC3973.

Structurei

3D structure databases

ProteinModelPortaliQ4MTG0.
SMRiQ4MTG0. Positions 10-371.
ModBaseiSearch...
MobiDBiSearch...

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.

Q4MTG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTKTKKTLF NVDEQMKAIA AQFETLQILN EKGEVVNEAA MPELSDDQLK
60 70 80 90 100
ELMRRMVYTR VLDQRSISLN RQGRLGFYAP TAGQEASQLA SHFALEAEDF
110 120 130 140 150
ILPGYRDVPQ LVWHGLPLYQ AFLFSRGHFM GNQMPENVNA LAPQIIIGAQ
160 170 180 190 200
IIQTAGVALG MKLRGKKSVA ITYTGDGGAS QGDFYEGMNF AGAFKAPAIF
210 220 230 240 250
VVQNNRYAIS TPVEKQSAAK TVAQKAVAAG IYGIQVDGMD PLAVYAATAF
260 270 280 290 300
ARERAVNGEG PTLIETLTFR YGPHTMAGDD PTRYRTKDIE NEWEQKDPIV
310 320 330 340 350
RFRAFLENKG LWSQEVEEKV IEEAKEDIKQ AIAKADQAPK QKVTDLMEIM
360 370
YEKMPYNLAE QYEIYKEKES K
Length:371
Mass (Da):41,441
Last modified:January 23, 2007 - v3
Checksum:i884A8A94D6084451
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEK01000007 Genomic DNA. Translation: EAL15457.1.
RefSeqiWP_000536893.1. NZ_KN050656.1.

Genome annotation databases

EnsemblBacteriaiEAL15457; EAL15457; BCE_G9241_3962.
GeneIDi22938186.
PATRICi24955467. VBIBacCer116370_1693.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEK01000007 Genomic DNA. Translation: EAL15457.1.
RefSeqiWP_000536893.1. NZ_KN050656.1.

3D structure databases

ProteinModelPortaliQ4MTG0.
SMRiQ4MTG0. Positions 10-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC3973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEAL15457; EAL15457; BCE_G9241_3962.
GeneIDi22938186.
PATRICi24955467. VBIBacCer116370_1693.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G9241Imported.
  2. "Acid stress in the food pathogen Bacillus cereus."
    Browne N., Dowds B.C.A.
    J. Appl. Microbiol. 92:404-414(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, INDUCTION.
    Strain: NCIMB 11796 / DSM 6261 Publication.

Entry informationi

Entry nameiODPA_BACCE
AccessioniPrimary (citable) accession number: Q4MTG0
Secondary accession number(s): P83068, P83070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 43 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.