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UniProtKB/Swiss-Prot entry Q89AR0

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

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Entry information
Entry name ODP1_BUCBP
Primary accession number Q89AR0
Secondary accession numbers None
Integrated into Swiss-Prot on June 16, 2003
Sequence was last modified on June 16, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 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: bbp_189
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO26921.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777816.1; -.
3D structure databases
HSSP P06958; 1L8A. [HSSP ENTRY / PDB]
ModBase Q89AR0.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_189-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0004802; Molecular function: transketolase activity (inferred from electronic annotation from InterPro).
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.
IPR005478; BacTransketolase.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
PANTHER PTHR11624:SF1; BacTransketolase; 1.
Pfam PF00456; Transketolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
BLOCKS Q89AR0.
ProtoNet Q89AR0.
Genome annotation databases
GeneID 1058233; -.
GenomeReviews AE016826_GR; bbp_189.
KEGG bab:bbp189; -.
Phylogenomic databases
HOGENOM Q89AR0; -.
Genome annotation databases
CMR Q89AR0; bbp_189.
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   887  887     Pyruvate dehydrogenase E1 component. PRO_0000162242
Sequence information
Length: 887 AA [This is the length of the unprocessed precursor] Molecular weight: 100906 Da [This is the MW of the unprocessed precursor] CRC64: 89A9A18649A6A78A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEFSSNDID PIETEDWIQA IKSVIREDGL ERANFIINTV KKYVPYKNKV VFKKCAISNY 

        70         80         90        100        110        120 
VNTIPVEEEP NYPGDLFIEQ KIRSVIRWNA IMMVLRASKK NLDLGGHLSS FQSAATIYEV 

       130        140        150        160        170        180 
CFNHFFHATN ENNGGDLVYF QGHISPGIYS RAFIEDRLTQ KQLDNFRQEI DGIGLSSYPH 

       190        200        210        220        230        240 
PKLMPNFWQF PTVSMGLGPI CAIYQAKFLK YLEHRNLKCT NNQKVYAFLG DGEMDEPESK 

       250        260        270        280        290        300 
GAISIAAREK LDNLIFIVNC NLQRLDGPVI GNGKVIDELE SVFKGCGWKV IKVIWGSKWD 

       310        320        330        340        350        360 
SLLKKDVSGK LIKLMNETLD GDYQTFKSKN GAYIRKYFFG KYLETQELVK DMSDDQIWNL 

       370        380        390        400        410        420 
DRGGHDPKKI YAALSKANSI VGKPVIILMH TVKGYGMGDI AEGKNIAHQI KKIDIKGITY 

       430        440        450        460        470        480 
IKNRFKVPVE ENELKYLPYV SFDANSIEYK YLHARRKKLG GYLPIRLSNF TNFFTLPKLD 

       490        500        510        520        530        540 
EFSTLLTEQK KEISTTIVFI RILNILLRNS FIKDRIVPII ADEARTFGME GLFRKIGIYN 

       550        560        570        580        590        600 
FIGQKYTPQD KELLAYYKED KKGQILQEGI NELGAAASWL AAATSYSTNN FPMIPFYIFY 

       610        620        630        640        650        660 
SMFGFQRIGD LFWAAGDQQA RGFLIGGTSG KTTLNGEGLQ HGDGHSHIQA LTIPNCISYN 

       670        680        690        700        710        720 
PAYAYELAVI VHDGLQRMYG PSQENIYYYI TTMNENYVMP GISKNMYEGI CKGIYKLKHV 

       730        740        750        760        770        780 
GKKNVKVQIM GSGSILQCVC RAAEILLEEY DIGSDVYSVT SFTELARNGQ DCDRWNLLHP 

       790        800        810        820        830        840 
TQEKKVPFVT KIMNKLPAIA VTDYMKLFSE QVRAYIPAVT YRVLGTDGFG RSDSRKNLRR 

       850        860        870        880 
YFEIDEYHIV IAVLGELEKI GDVDKNTIVN AISKFKIDIN KVNPRLA
Q89AR0 in FASTA format

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