Reviewed, UniProtKB/Swiss-Prot P21882 (ODPB_BACSU)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1
Alternative name(s):
    S complex, 36 kDa subunit

Gene names

Name:	pdhB
Synonyms:	aceB
Ordered Locus Names:	BSU14590

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 325	324	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000162222
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21882-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 887EECA29C0C4E25	FASTA	325	35,474
	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

References

	« Hide 'large scale' referencesShow '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: 1697575] [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: 8969500] [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. , 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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M57435 Genomic DNA. Translation: AAA62682.1. AF012285 Genomic DNA. Translation: AAC24933.1. AL009126 Genomic DNA. Translation: CAB13332.1.
PIR	C36718.
RefSeq	NP_389342.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
SMR	P21882. Positions 2-325.
ModBase	Search...
PTM databases
PhosSite	P21882.
Genome annotation databases
GeneID	939496.
GenomeReviews	Gene locus BSU14590 in contig AL009126_GR.
KEGG	bsu:BSU14590.
NMPDR	fig|224308.1.peg.1461.
Organism-specific databases
SubtiList	BG10208. pdhB. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P21882.
OMA	P21882. LFYELEA.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1461-MON.
BRENDA	1.2.4.1. 150.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR015941. Transketolase_C-like. IPR005475. Transketolase_central-reg. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPB_BACSU

Accession

Primary (citable) accession number: P21882

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)