Q4ULG1 (ODP2_RICFE) 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:	RF_0761

Organism

Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP]

Taxonomic identifier

315456 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › Rickettsia felis

Protein attributes

Sequence length	412 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 – 412	412	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000288764
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)
	Q4ULG1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: CF7CE592B67A8DFB	FASTA	412	45,220
	10 20 30 40 50 60 MPIKILMPVL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA VDEGILAKIV 70 80 90 100 110 120 IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNNVSPS PKTDANLPKP HENIAKVEEQ 130 140 150 160 170 180 VAVIKHDASK IFASPLAKRL AKMGNIRLES VKGSGPHGRI VKQDILSYTP STVHNKIVSR 190 200 210 220 230 240 NPEEYRLVPN NNIRKIIAKR LLESKQTVPH FYLSIECNVD KLLDIREDIN KSFSEDKSTR 250 260 270 280 290 300 ISVNDFIILA VAKALQELPN ANASWGEDAI RYHNNVDISV AVAIENGLVT PIVKNANQKN 310 320 330 340 350 360 IIELSREMKE LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP QSCIMGVGAS 370 380 390 400 410 AKRAIVKNDQ VTIATIMDVT LSADHRVVDG AVGAEFLAAF KKFIESPALM LI

References

[1]

"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite." Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D. PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-1525 / URRWXCal2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000053 Genomic DNA. Translation: AAY61612.1.
RefSeq	YP_246777.1. NC_007109.1.
3D structure databases
HSSP	HSSP built from PDB template 1FYC based on UniProtKB P10515.
ProteinModelPortal	Q4ULG1.
SMR	Q4ULG1. Positions 183-412.
ModBase	Search...
Protein-protein interaction databases
STRING	315456.RF_0761.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAY61612; AAY61612; RF_0761.
GeneID	3400828.
KEGG	rfe:RF_0761.
PATRIC	17892180. VBIRicFel64634_0918.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281566.
KO	K00627.
OMA	ETIAPQN.
ProtClustDB	PRK11856.
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_RICFE

Accession

Primary (citable) accession number: Q4ULG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program