Reviewed, UniProtKB/Swiss-Prot Q1RJT3 (ODP2_RICBR)

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:	pdhC
Ordered Locus Names:	RBE_0300

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

Protein attributes

Sequence length	418 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 pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
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 – 418	418	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000288763
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	388	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RJT3-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: E0ECE5B73C92EC31	FASTA	418	45,750
	10 20 30 40 50 60 MPIKLLMPAL SPTMTEGNLA RWLKKEGDKI NPGEVIAEIE TDKATMEVEA VDEGTLAKII 70 80 90 100 110 120 IPQGSQNVPV NSLIAVLIEE GEELSGIEEF IAKNNSNSPK KEEISKPAET IAPQNVKEEN 130 140 150 160 170 180 ITTASDQNNI KVFASPLAKR LAKIQNVRIE EIKGSGPHGR IIKQDVLSHK GGSKALSNKI 190 200 210 220 230 240 VSRNPEEYRL APNNNIRKII AKRLLESKQT VPHFYLSIEC NVDKLLDIRE DINKSFGDDK 250 260 270 280 290 300 SAKISVNDFI ILAVAKALQE VPNANASWGD DAIRYYNNVD ISVAVAIENG LVTPIIRNAD 310 320 330 340 350 360 QKNIVDLSSE MKGLIKKARE NKLTPEEFQG GGFTISNLGM YGIKNFNAII NPPQSCIMGV 370 380 390 400 410 GSSSKRAIVK NDQISIATIM DVTLSADHRV VDGAVGAEFL AAFKRFIESP ALMLLYTR

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000087 Genomic DNA. Translation: ABE04381.1.
RefSeq	YP_537470.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RJT3.
Genome annotation databases
GeneID	3996210.
GenomeReviews	Gene locus RBE_0300 in contig CP000087_GR.
KEGG	rbe:RBE_0300.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1RJT3.
OMA	ISIATIM.
Enzyme and pathway databases
BioCyc	RBEL336407:RBE_0300-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. 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]
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_RICBR

Accession

Primary (citable) accession number: Q1RJT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 16, 2006
Last modified:	November 3, 2009
This is version 27 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)