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UniProtKB/Swiss-Prot entry Q4MTG0


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

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Entry information
Entry name ODPA_BACCE
Primary accession number Q4MTG0
Secondary accession numbers P83068 P83070
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 16)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonym EC 1.2.4.1
Gene name
Name: pdhA
ORFNames: BCE_G9241_3962
From
Bacillus cereus [TaxID: 1396] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G9241;
DOI=10.1073/pnas.0402414101; PubMed=15155910 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax.";
Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
[2]
PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
STRAIN=NCIMB 11796 / DSM 626;
DOI=10.1046/j.1365-2672.2002.01541.x; PubMed=11872115 [NCBI, ExPASy, EBI, Israel, Japan]
Browne N., Dowds B.C.A.;
"Acid stress in the food pathogen Bacillus cereus.";
J. Appl. Microbiol. 92:404-414(2002).
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) (By similarity).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: 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.
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
AAEK01000007; EAL15457.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
SMR Q4MTG0; 10-371.
ModBase Q4MTG0.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS Q4MTG0.
Other
ProtoNet Q4MTG0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate; Stress response; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   371  370     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000271255
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 41441 Da [This is the MW of the unprocessed precursor] CRC64: 884A8A94D6084451 [This is a checksum on the sequence]
        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 

Q4MTG0 in FASTA format

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