Reviewed, UniProtKB/Swiss-Prot Q4MTG0 (ODPA_BACCE)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha
    EC=1.2.4.1

Gene names

Name:	pdhA
ORF Names:	BCE_G9241_3962

Organism

Bacillus cereus

Taxonomic identifier

1396 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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) By similarity. UniProtKB P21873
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. UniProtKB P21873
Cofactor	Thiamine pyrophosphate By similarity. UniProtKB P21873
Subunit structure	Heterodimer of an alpha and a beta chain.
Induction	By acid stress. Under acid-stress, this protein is expressed at a higher level in wild-type B.cereus than in the acid-sensitive mutant strain NB1. Ref.2

Ontologies

Keywords
Biological process	Glycolysis Stress response
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	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 response to stress 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.2
	Chain	2 – 371	370	Pyruvate dehydrogenase E1 component subunit alpha		PRO_0000271255

Sequences

	Sequence		Length	Mass (Da)
	Q4MTG0-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 884A8A94D6084451	FASTA	371	41,441
	10 20 30 40 50 60 MGTKTKKTLF NVDEQMKAIA AQFETLQILN EKGEVVNEAA MPELSDDQLK ELMRRMVYTR 70 80 90 100 110 120 VLDQRSISLN RQGRLGFYAP TAGQEASQLA SHFALEAEDF ILPGYRDVPQ LVWHGLPLYQ 130 140 150 160 170 180 AFLFSRGHFM GNQMPENVNA LAPQIIIGAQ IIQTAGVALG MKLRGKKSVA ITYTGDGGAS 190 200 210 220 230 240 QGDFYEGMNF AGAFKAPAIF VVQNNRYAIS TPVEKQSAAK TVAQKAVAAG IYGIQVDGMD 250 260 270 280 290 300 PLAVYAATAF ARERAVNGEG PTLIETLTFR YGPHTMAGDD PTRYRTKDIE NEWEQKDPIV 310 320 330 340 350 360 RFRAFLENKG LWSQEVEEKV IEEAKEDIKQ AIAKADQAPK QKVTDLMEIM YEKMPYNLAE 370 QYEIYKEKES K

References

[1]

"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax." Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. , Galloway D.R., Read T.D., Popovic T., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed: 15155910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G9241.

[2]

"Acid stress in the food pathogen Bacillus cereus." Browne N., Dowds B.C.A. J. Appl. Microbiol. 92:404-414(2002) [PubMed: 11872115] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, INDUCTION. Strain: NCIMB 11796 / DSM 626.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAEK01000007 Genomic DNA. Translation: EAL15457.1.
3D structure databases
HSSP	HSSP built from PDB template 1W88 based on UniProtKB P21873.
SMR	Q4MTG0. Positions 10-371.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.4.1. 604.
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_BACCE

Accession

Primary (citable) accession number: Q4MTG0
Secondary accession number(s): P83068, P83070

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 23 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)