ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P21882


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ODPB_BACSU
Primary accession number P21882
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 68)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta
Synonyms EC 1.2.4.1
S complex, 36 kDa subunit
Gene name
Name: pdhB
Synonyms: aceB
OrderedLocusNames: BSU14590
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
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).
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; AAA62682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012285; AAC24933.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13332.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C36718; C36718.
RefSeq NP_389342.1; -.
3D structure databases
HSSP Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]
SMR P21882; 2-325.
ModBase P21882.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1461-MON; -.
Organism-specific databases
SubtiList BG10208; pdhB. [Micado]
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
ProtoNet P21882.
Genome annotation databases
GeneID 939496; -.
GenomeReviews AL009126_GR; BSU14590.
KEGG bsu:BSU14590; -.
NMPDR fig|224308.1.peg.1461; -.
Phylogenomic databases
HOGENOM P21882; -.
Genome annotation databases
CMR P21882; BSU14590.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   325  324     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000162222
BINDING   60    60        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 35474 Da [This is the MW of the unprocessed precursor] CRC64: 887EECA29C0C4E25 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQMTMIQAI TDALRTELKN DENVLVFGED VGVNGGVFRA TEGLQKEFGE DRVFDTPLAE 

        70         80         90        100        110        120 
SGIGGLALGL GLNGFRPVME IQFFGFVYEV MDSVSGQMAR MRYRSGGRWT SPVTIRSPFG 

       130        140        150        160        170        180 
GGVHTPELHA DSLEGLVAQQ PGIKVVIPST PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF 

       190        200        210        220        230        240 
RQEVPEEEYT IELGKADVKR EGTDLSIITY GAMVHESLKA ADELEKDGIS AEVVDLRTVS 

       250        260        270        280        290        300 
PLDIDTIIAS VEKTGRAIVV QEAQKQAGIA ANVVAEINDR AILSLEAPVL RVAAPDTVFP 

       310        320 
FSQAESVWLP NHKDVLETAR KVLEF 

P21882 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!