Q68WK6 (ODP2_RICTY) 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:	pdhC
Ordered Locus Names:	RT0517

Organism

Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]

Taxonomic identifier

257363 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia typhi

Protein attributes

Sequence length	404 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.

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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 404	404	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000288765
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	377	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68WK6 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: C868563403885ADC	FASTA	404	44,546
	10 20 30 40 50 60 MPIKILMPAL SPTMKDGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVES VDEGILAKII 70 80 90 100 110 120 IPQNSQNVPV NSLIAVLSEE GESTADIDAF IAKNNSVSLS LKTDTTLKKA NESITNVEVV 130 140 150 160 170 180 KHDLSKIFAS PLAKRLAKIR NIRLESVQGS GPHGRIVKQD ILSYSPSTAY NRDTEEYRSV 190 200 210 220 230 240 PNNNIRQIIA KRLLESKQTV PHFYLSIECN VDKLLDIRED INKSFSEDKL TKISVNDFII 250 260 270 280 290 300 LAVAKALQEV PNANASWAED AIRYYNNVDI SVAVAIENGI VTPIIKDANK KNIIELSHEM 310 320 330 340 350 360 KILIKKAKDN KLTPVEFQGG GFTISNLGMY GIKNFNAIIN TPQSCIMGVG ASTKRAIVKN 370 380 390 400 DQIIIATIMD VTLSADHRVI DGAVSAEFLA SFKRFIEHPV LMLI

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU03986.1.
RefSeq	YP_067468.1. NC_006142.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZWV based on UniProtKB P11182.
ProteinModelPortal	Q68WK6.
ModBase	Search...
Protein-protein interaction databases
STRING	257363.RT0517.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU03986; AAU03986; RT0517.
GeneID	2959197.
KEGG	rty:RT0517.
PATRIC	17910274. VBIRicTyp34752_0542.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281566.
KO	K00627.
OMA	ETIAPQN.
ProtClustDB	PRK11856.
Enzyme and pathway databases
BioCyc	RTYP257363:GJEQ-543-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. IPR006257. LAT1. 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.
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_RICTY

Accession

Primary (citable) accession number: Q68WK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program