Q89AQ9 (ODP2_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
EC=2.3.1.12

Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2

Gene names

Name:	aceF
Ordered Locus Names:	bbp_190

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence AAO26922.1 differs from that shown. Reason: Erroneous initiation.

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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 410	410	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162277
Regions
	Domain	1 – 68	68	Lipoyl-binding
Sites
	Active site	383	1	Potential
Amino acid modifications
	Modified residue	35	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AQ9 [UniParc]. Last modified June 16, 2003. Version 1. Checksum: 69EF982E6C212730	FASTA	410	46,119
	10 20 30 40 50 60 MPDIGTDLVE VIEILVKIGD QVKKDDSLIT VEGQKASIEI PASHTGTIKN IIVHIGEKIT 70 80 90 100 110 120 TGSLIAILNG IDDNVKSKND SSSYSFKNSK NTSTNSNLGN VNNNINNRTI LVHATPTVRR 130 140 150 160 170 180 LARKFDIKLE NITGTGRKGR ILKEDVISYK NISLFNDIKK SLKKTNVNYY KDNVTCDDFK 190 200 210 220 230 240 SIELTRTQIR SSKNLLKSWL TIPHVTQFDE SDITELENFR QKYNSDLKDK SKKLTILIFV 250 260 270 280 290 300 IKAVSKALEM FPKFNGRLIN KDNRIAIVLN EHINIGIVVD TDDGLLVPVI NRVNKKNISS 310 320 330 340 350 360 ISNDLRIISE RARSRKLNFS DIKEYGSFTI SNLGGIGGTN FTPIIKYPEL AILGISRALI 370 380 390 400 410 KPYWNSHAFI PKLMLPLSLS YDHRAIDGVA AVRFITFVKK MLTDIRFLMI

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: AAO26922.1. Different initiation.
RefSeq	NP_777817.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AQ9.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp190.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO26922; AAO26922; bbp_190.
GeneID	1058122.
KEGG	bab:bbp190.
PATRIC	21245155. VBIBucAph80364_0184.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
KO	K00627.
OMA	DIGGATQ.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-190-MONOMER.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_BUCBP

Accession

Primary (citable) accession number: Q89AQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	June 16, 2003
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program