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UniProtKB/Swiss-Prot entry P57301


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

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Entry information
Entry name ODP1_BUCAI
Primary accession number P57301
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on December 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 48)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
OrderedLocusNames: BU205
From
Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [TaxID: 118099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).
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
BA000003; BAB12922.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_240036.1; -.
3D structure databases
HSSP P06958; 1L8A. [HSSP ENTRY / PDB]
SMR P57301; 58-887.
ModBase P57301.
Enzyme and pathway databases
BioCyc BSP107806:BU205-MON; -.
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.
BLOCKS P57301.
Genome annotation databases
GeneID 1109648; -.
GenomeReviews BA000003_GR; BU205.
KEGG buc:BU205; -.
Phylogenomic databases
HOGENOM P57301; -.
Genome annotation databases
CMR P57301; BU205.
Other
ProtoNet P57301.
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   887  887     Pyruvate dehydrogenase E1 component. PRO_0000162240
Sequence information
Length: 887 AA [This is the length of the unprocessed precursor] Molecular weight: 101396 Da [This is the MW of the unprocessed precursor] CRC64: B6AB82C012826105 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSENLYNDVD PIETRDWVQA IESVIRREGH KRAHFLIEQV LKTAKINRKE FFRSSFTSDY 

        70         80         90        100        110        120 
INTISREDEY EYPGNLILEK RIRSAIRWNA IMMVLRASKK NLELGGHLSS FQSSATIYEV 

       130        140        150        160        170        180 
CFNHFFQAKN HKDGGDLVYF QGHISPGIYA RSFLEGRLSE EQIDNFRQEV DGIGLSSYPH 

       190        200        210        220        230        240 
PKLMPNFWQF PTVSMGLGPL CAIYQAKFLK YLHNRELKNT SKQIVYAFLG DGEMDEPESK 

       250        260        270        280        290        300 
GAISIAVREK LDNLIFIINC NLQRLDGPVV GNGKIVNELE SFFYGAGWKV IKVIWGSRWD 

       310        320        330        340        350        360 
CLLKKDTSGK LIQLMNETVD GDYQTFKSKD GAYVRKYFFG KYKETYDLVK DMTDEEIWKL 

       370        380        390        400        410        420 
NRGGHDPKKM FNALKKAKET KYKPTVILAH TVKGYGMGVI AEGKNIAHQI KKININGIIH 

       430        440        450        460        470        480 
IRDRFNIPVS NDEINKLPYV TFKKNSEEYC YIHSQRKKLG GYIPFRLSSF TGKLILPKLI 

       490        500        510        520        530        540 
DFQSLLEEQK KDISTTVAFI RVLNIILKNN SIKHLIVPII ADEARTFGME GLFRKIGIYS 

       550        560        570        580        590        600 
SSGQKYTPQD REQLAYYKEE KKGQILQEGI NELGAASSWL AAATSYSTND FPMILFYIYY 

       610        620        630        640        650        660 
SIFGFQRIGD LFWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD 

       670        680        690        700        710        720 
PAFAYEVAVI IQDGLRRMYG PSQENIYYYI TTINENYYMP AMPIGVEEGI CKGIYKLKTL 

       730        740        750        760        770        780 
HGTTSKVQLI GSGAILRSVC EAAEILLKDY SITTDIYSVT SFTELARNGE DCERWNMLHP 

       790        800        810        820        830        840 
NEKNKIAYVK QIMNKNPTVA ATDYMKLFAE QIRHYIPSQE YHVLGTDGFG RSDSRDKLRD 

       850        860        870        880 
HFEVNAYYIV IAALNLLANI NDIKKKVVED AIMKFNIDAN KINPRLS 

P57301 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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