Reviewed, UniProtKB/Swiss-Prot Q8K9T8 (ODP2_BUCAP)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene names

Name:	aceF
Ordered Locus Names:	BUsg_200

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	402 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 CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding 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 – 402	402	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162276
Regions
	Domain	1 – 68	68	Lipoyl-binding
Sites
	Active site	375	1	Potential
Amino acid modifications
	Modified residue	35	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9T8-1 [UniParc]. Last modified November 8, 2002. Version 2. Checksum: 1F784349E26E5643	FASTA	402	45,421
	10 20 30 40 50 60 MPDIGLEEVE VTEILVKIGE EIKLDQGLIT VEGDKASMEI PSPISGIVKD ITIKIGEKVK 70 80 90 100 110 120 TSSIIMIFKV NNLNSIKNEK DLNYIKTEKK LNENFLEEKK DIKKIVLVHA TPVVRRLARH 130 140 150 160 170 180 LNVDLKNITP SGPKNRILKE DIELYIRNNT SNKSSFNIEK NNTTNFHKDL FNEIPITNIQ 190 200 210 220 230 240 QIIGKNLHQN WVNIPHVTQF DEVNITLLEE FRHKYNTEKK QKNNMCSKIT ILPFIIKSVA 250 260 270 280 290 300 YGLLEFPIFN SSLSVNKKTI FLKKYVNVGI AVDVQNALFV PVLKNVDKKN IANLSSELIF 310 320 330 340 350 360 LSKKAHENKL DASDMKDGCF TISNLGGIGG SWFSPIINSP EVAILGVSKA LIKPLWNGKE 370 380 390 400 FIPSLMLPLS LSYDHRVING ADAARFLTFI GKMLSDIRFL IM

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: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67764.1. Different initiation.
RefSeq	NP_660553.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJO based on UniProtKB P06959.
ModBase	Search...
Genome annotation databases
GeneID	1005397.
GenomeReviews	Gene locus BUsg_200 in contig AE013218_GR.
KEGG	bas:BUsg200.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8K9T8.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG200-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_BUCAP

Accession

Primary (citable) accession number: Q8K9T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	November 8, 2002
Last modified:	June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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