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P21881 (ODPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 106. 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 alpha

EC=1.2.4.1
Alternative name(s):
S complex, 42 kDa subunit
Vegetative protein 220
Short name=VEG220
Gene names
Name:pdhA
Synonyms:aceA
Ordered Locus Names:BSU14580
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length371 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).

The B.subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 371370Pyruvate dehydrogenase E1 component subunit alpha
PRO_0000162199

Experimental info

Sequence conflict1791A → R in AAA62681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21881 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 984AE665278C1462

FASTA37141,548
        10         20         30         40         50         60 
MAAKTKKAIV DSKKQFDAIK KQFETFQILN EKGEVVNEAA MPDLTDDQLK ELMRRMVFTR 

        70         80         90        100        110        120 
VLDQRSISLN RQGRLGFYAP TAGQEASQIA THFALEKEDF VLPGYRDVPQ LIWHGLPLYQ 

       130        140        150        160        170        180 
AFLFSRGHFR GNQMPDDVNA LSPQIIIGAQ YIQTAGVALG LKKRGKKAVA ITYTGDGGAS 

       190        200        210        220        230        240 
QGDFYEGINF AGAYKAPAIF VVQNNRYAIS TPVEKQSAAE TIAQKAVAAG IVGVQVDGMD 

       250        260        270        280        290        300 
PLAVYAATAE ARERAINGEG PTLIETLTFR YGPHTMAGDD PTKYRTKEIE NEWEQKDPLV 

       310        320        330        340        350        360 
RFRAFLENKG LWSEEEEAKV IEDAKEEIKQ AIKKADAEPK QKVTDLMKIM YEKMPHNLEE 

       370 
QFEIYTQKES K 

« Hide

References

« Hide 'large scale' references
[1]"Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase."
Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.
J. Bacteriol. 172:5052-5063(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area."
Winters P., Caldwell R.M., Enfield L., Ferrari E.
Microbiology 142:3033-3037(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome."
Caldwell R.M., Ferrari E.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
Strain: 168 / IS58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57435 Genomic DNA. Translation: AAA62681.1.
AF012285 Genomic DNA. Translation: AAC24932.1.
AL009126 Genomic DNA. Translation: CAB13331.1.
PIRDEBSPA. B36718.
RefSeqNP_389341.1. NC_000964.3.

3D structure databases

ProteinModelPortalP21881.
SMRP21881. Positions 14-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21881. 1 interaction.
MINTMINT-8365401.
STRING224308.BSU14580.

Proteomic databases

PaxDbP21881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13331; CAB13331; BSU14580.
GeneID936005.
KEGGbsu:BSU14580.
PATRIC18974709. VBIBacSub10457_1546.

Organism-specific databases

GenoListBSU14580. [Micado]

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281335.
KOK00161.
OMAPICVPIA.
OrthoDBEOG6VMTKR.
ProtClustDBCLSK2460915.

Enzyme and pathway databases

BioCycBSUB:BSU14580-MONOMER.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017596. Pyrv_DH_E1_asu_subgrp-x.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_BACSU
AccessionPrimary (citable) accession number: P21881
Secondary accession number(s): Q59227
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList