Reviewed, UniProtKB/Swiss-Prot P21881 (ODPA_BACSU)

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
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 thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 371	370	Pyruvate dehydrogenase E1 component subunit alpha		PRO_0000162199
Experimental info
	Sequence conflict	179	1	A → R in AAA62681. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21881-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 984AE665278C1462	FASTA	371	41,548
	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

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.
[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: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Strain: 168 / IS58.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M57435 Genomic DNA. Translation: AAA62681.1. AF012285 Genomic DNA. Translation: AAC24932.1. AL009126 Genomic DNA. Translation: CAB13331.1.
PIR	DEBSPA. B36718.
RefSeq	NP_389341.1.
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
SMR	P21881. Positions 14-371.
ModBase	Search...
Genome annotation databases
GeneID	936005.
GenomeReviews	Gene locus BSU14580 in contig AL009126_GR.
KEGG	bsu:BSU14580.
NMPDR	fig|224308.1.peg.1460.
Organism-specific databases
SubtiList	BG10207. pdhA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P21881.
OMA	P21881. ESEEEAW.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1460-MON.
BRENDA	1.2.4.1. 150.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017596. Pyrv_DH_E1_asu_subgrp-x. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_BACSU

Accession

Primary (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:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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