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Q89AR0 (ODP1_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component
Short name=PDH E1 component
EC=1.2.4.1
Gene names
Name:aceE
Ordered Locus Names:bbp_189
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Homodimer By similarity. Makes part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887Pyruvate dehydrogenase E1 component
PRO_0000162242

Sequences

Sequence LengthMass (Da)Tools
Q89AR0 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 89A9A18649A6A78A

FASTA887100,906
        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

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
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.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO26921.1.
RefSeqNP_777816.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AR0.
SMRQ89AR0. Positions 57-887.
ModBaseSearch...

Protein-protein interaction databases

STRING224915.bbp189.

Proteomic databases

PRIDEQ89AR0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26921; AAO26921; bbp_189.
GeneID1058233.
KEGGbab:bbp189.
PATRIC21245153. VBIBucAph80364_0183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
KOK00163.
OMANLIFTIS.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-189-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF00456. Transketolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODP1_BUCBP
AccessionPrimary (citable) accession number: Q89AR0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
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