P21881 (ODPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

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 (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

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 Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine 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 [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] [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. , 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.
PIR	DEBSPA. B36718.
RefSeq	NP_389341.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P21881.
SMR	P21881. Positions 14-371.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU14580.
Proteomic databases
PaxDb	P21881.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB13331; CAB13331; BSU14580.
GeneID	936005.
KEGG	bsu:BSU14580.
PATRIC	18974709. VBIBacSub10457_1546.
Organism-specific databases
GenoList	BSU14580. [Micado]
Phylogenomic databases
eggNOG	COG1071.
HOGENOM	HOG000281335.
KO	K00161.
OMA	KEIMYRM.
ProtClustDB	CLSK2460915.
Enzyme and pathway databases
BioCyc	BSUB:BSU14580-MONOMER.
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:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program