ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8K9T9

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ODP1_BUCAP
Primary accession number Q8K9T9
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 47)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
OrderedLocusNames: BUsg_199
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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: Homodimer (By similarity).
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
AE013218; AAM67763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660552.1; -.
3D structure databases
HSSP P06958; 1L8A. [HSSP ENTRY / PDB]
SMR Q8K9T9; 59-888.
ModBase Q8K9T9.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG199-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004660; 2-oxoA_DHase_E1.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF00456; Transketolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
ProtoNet Q8K9T9.
Genome annotation databases
GeneID 1005396; -.
GenomeReviews AE013218_GR; BUsg_199.
KEGG bas:BUsg199; -.
Phylogenomic databases
HOGENOM Q8K9T9; -.
Genome annotation databases
CMR Q8K9T9; BUsg_199.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   888  888     Pyruvate dehydrogenase E1 component. PRO_0000162241
Sequence information
Length: 888 AA [This is the length of the unprocessed precursor] Molecular weight: 101458 Da [This is the MW of the unprocessed precursor] CRC64: E127C03FB1261177 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSEKLYNYDV DPVETNDWVQ SIESVIREEG LERAKFLIEK ILKKSKITRA NFFKCFFTSD 

        70         80         90        100        110        120 
YINTISSEEE VEYPGDLILE KRIRSAIRWN AIMMVLRASK KDLELGGHLS SFQSSATIYE 

       130        140        150        160        170        180 
VCFNHFFRSK NDEDGGDLVY FQGHIAPGIY ARSFLEGRLS KKQIDNFRQE VDGKGLSSYP 

       190        200        210        220        230        240 
HPKLMPNFWQ FPTVSMGLGP LCAIYQAKFL KYLQNRELKN TSKQTVYAFL GDGEMDEPES 

       250        260        270        280        290        300 
KGAISIAVRE KLDNLIFVIN CNLQRLDGPV VGNGKIVNEL ESFFYGAGWK VIKVIWGGKW 

       310        320        330        340        350        360 
DSLLKKDKTG KLIQLMNETI DGEYQTLKSK DGAYVRKYFF GKYQETLELV KNMTDEEIWN 

       370        380        390        400        410        420 
LNRGGHDPKK MFNALKKAKE IKDKPTVILA HTVKGYGMGV IAEGKNIAHQ IKKININGII 

       430        440        450        460        470        480 
YIRDRFNIPI SNEDIKELPY VVFEKNSKEY CYMHQQRKKL GGYIPFRLSK FTNALNIPDL 

       490        500        510        520        530        540 
IDFKSLLKEQ NKKMSTTIAF VRVLNLILKN HSIKNLIVPI IADEARTFGM EGLFRMIGIY 

       550        560        570        580        590        600 
SSIGQKYVPQ DREQLAYYKE EKKGQILQEG INELGAASSW LAAATSYSTN DFPMIPFYIY 

       610        620        630        640        650        660 
YSIFGFQRIG DLFWAAGDQQ ARGFLIGGTS GRTTLNGEGL QHEDGHSHIQ SLTIPNCVSY 

       670        680        690        700        710        720 
DPAFAYEVAV IIQDGLRRMY GPLQENIYYY ITTINENYYM PAMPQGVEKG ICKGIYKLKT 

       730        740        750        760        770        780 
FYATELKVQL MGSGAILRCI CKAGEILSND YCITTDIYSV TSFTELARNG EDCERWNMLH 

       790        800        810        820        830        840 
PYEKKRIAYI KTVMNSSPAV AATDYMKLFA EQIRHYIPSN EYHVLGTDGF GRSDSRDKLR 

       850        860        870        880 
DHFEVSAYYI VVAALNLLAK LNNINKKVVE EAIIKFNINA DKINPRLA
Q8K9T9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!