Reviewed, UniProtKB/Swiss-Prot Q92HK7 (ODP2_RICCN)

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:	RC0764

Organism

Rickettsia conorii [Complete proteome] [HAMAP]

Taxonomic identifier

781 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	412 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 – 412	412	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162285
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	385	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92HK7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 26E645592CB4B933	FASTA	412	45,426
	10 20 30 40 50 60 MPIKILMPAL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA VDEGILAKIV 70 80 90 100 110 120 IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNSVSPS PKTDANLPKP HENIANVEEQ 130 140 150 160 170 180 VTVIKHDVSR IFASPLAKRL AKMRNIRFES VKGSGPHGRI VKQDILSYTP STAHNKIVSR 190 200 210 220 230 240 NPEEYRLVPN NNIRKIIAKR LLESKQTVPH FYLSIECNVD KLLDIREDIN KFFSEDKSTR 250 260 270 280 290 300 ISVNDFIILA VAKALQEVPN ANASWGEDAI RYYNNVDISV AVAIENGLVT PIVKNANQKN 310 320 330 340 350 360 ILELSREMKA LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP QSCIMGVGAS 370 380 390 400 410 AKRAIVKNDQ ITIATIMDVT LSADHRVVDG AVGAEFLVAF KKFIESPVLM LI

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006914 Genomic DNA. Translation: AAL03302.1.
PIR	D97795.
RefSeq	NP_360401.1.
3D structure databases
HSSP	HSSP built from PDB template 1E2O based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	927481.
GenomeReviews	Gene locus RC0764 in contig AE006914_GR.
KEGG	rco:RC0764.
NMPDR	fig|272944.1.peg.764.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q92HK7.
OMA	HENIANV.
Enzyme and pathway databases
BioCyc	RCON272944:RC0764-MON.
BRENDA	2.3.1.12. 267518.
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]
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_RICCN

Accession

Primary (citable) accession number: Q92HK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 51 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)