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UniProtKB/Swiss-Prot entry P21881


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA_BACSU
Primary accession number P21881
Secondary accession number Q59227
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonyms EC 1.2.4.1
S complex, 42 kDa subunit
Vegetative protein 220
VEG220
Gene name
Name: pdhA
Synonyms: aceA
OrderedLocusNames: BSU14580
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1697575 [NCBI, ExPASy, EBI, Israel, Japan]
Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.;
"Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase.";
J. Bacteriol. 172:5052-5063(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969500 [NCBI, ExPASy, EBI, Israel, Japan]
Winters P., Caldwell R.M., Enfield L., Ferrari E.;
"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.";
Microbiology 142:3033-3037(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Caldwell R.M., Ferrari E.;
"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[5]
PROTEIN SEQUENCE OF 2-16.
STRAIN=168 / IS58;
PubMed=9298659 [NCBI, ExPASy, EBI, Israel, Japan]
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis.";
Electrophoresis 18:1451-1463(1997).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
  • FUNCTION: 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: Heterodimer of an alpha and a beta chain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57435; AAA62681.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012285; AAC24932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B36718; DEBSPA.
RefSeq NP_389341.1; -.
3D structure databases
HSSP P12694; 1DTW. [HSSP ENTRY / PDB]
SMR P21881; 14-371.
ModBase P21881.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1460-MON; -.
Organism-specific databases
SubtiList BG10207; pdhA. [Micado]
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P21881.
Genome annotation databases
GeneID 936005; -.
GenomeReviews AL009126_GR; BSU14580.
KEGG bsu:BSU14580; -.
NMPDR fig|224308.1.peg.1460; -.
Phylogenomic databases
HOGENOM P21881; -.
Genome annotation databases
CMR P21881; BSU14580.
Other
ProtoNet P21881.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   371  370     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000162199
CONFLICT   179   179        A -> R (in Ref. 1; AAA62681). 
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 41548 Da [This is the MW of the unprocessed precursor] CRC64: 984AE665278C1462 [This is a checksum on the sequence]
        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 

P21881 in FASTA format

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