Q8K9T9 (ODP1_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component
Short name=PDH E1 component
EC=1.2.4.1

Gene names

Name:	aceE
Ordered Locus Names:	BUsg_199

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	888 AA.
Sequence status	Complete.
Protein existence	Inferred 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 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
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 888	888	Pyruvate dehydrogenase E1 component		PRO_0000162241

Sequences

	Sequence		Length	Mass (Da)
	Q8K9T9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E127C03FB1261177	FASTA	888	101,458
	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

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." 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. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67763.1.
RefSeq	NP_660552.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9T9.
SMR	Q8K9T9. Positions 59-888.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg199.
Proteomic databases
PRIDE	Q8K9T9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67763; AAM67763; BUsg_199.
GeneID	1005396.
KEGG	bas:BUsg199.
PATRIC	21247185. VBIBucAph100086_0206.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2609.
KO	K00163.
OMA	NLIFTIS.
ProtClustDB	PRK09405.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-209-MONOMER.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view]
Pfam	PF00456. Transketolase_N. 2 hits. [Graphical view]
PIRSF	PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
TIGRFAMs	TIGR00759. aceE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODP1_BUCAP

Accession

Primary (citable) accession number: Q8K9T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program