Reviewed, UniProtKB/Swiss-Prot Q89AR0 (ODP1_BUCBP)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1

Gene names

Name:	aceE
Ordered Locus Names:	bbp_189

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 + CO(2).
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Homodimer By similarity.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC transketolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 887	887	Pyruvate dehydrogenase E1 component		PRO_0000162242

Sequences

	Sequence		Length	Mass (Da)
	Q89AR0-1 [UniParc]. Last modified June 16, 2003. Version 1. Checksum: 89A9A18649A6A78A	FASTA	887	100,906
	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

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: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26921.1.
RefSeq	NP_777816.1.
3D structure databases
HSSP	HSSP built from PDB template 1L8A based on UniProtKB P06958.
ModBase	Search...
Genome annotation databases
GeneID	1058233.
GenomeReviews	Gene locus bbp_189 in contig AE016826_GR.
KEGG	bab:bbp189.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AR0.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_189-MON.
Family and domain databases
InterPro	IPR004660. 2-oxoA_DHase_E1. IPR005478. BacTransketolase. IPR005474. Transketo_N. IPR015941. Transketolase_C-like. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PANTHER	PTHR11624:SF1. BacTransketolase. 1 hit.
Pfam	PF00456. Transketolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000156. Pyruvate_dh_E1. 1 hit.
TIGRFAMs	TIGR00759. aceE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODP1_BUCBP

Accession

Primary (citable) accession number: Q89AR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	June 16, 2003
Last modified:	November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)