Reviewed, UniProtKB/Swiss-Prot Q8CT13 (ODP2_STAES)

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:	SE_0793

Organism

Staphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]

Taxonomic identifier

176280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	433 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).
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
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 – 433	433	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162294
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	404	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CT13-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: EF82B61024832B27	FASTA	433	46,991
	10 20 30 40 50 60 MAFEFRLPDI GEGIHEGEIV KWFIKAGDTI EEDDVLAEVQ NDKSVVEIPS PVSGTVEEVL 70 80 90 100 110 120 VDEGTVAVVG DVIVKIDAPD AEEMQFKGHG DDEDSKKEEK EQESPVQEEA SSTQSQEKTE 130 140 150 160 170 180 VDESKTVKAM PSVRKYAREN GVNIKAVNGS GKNGRITKED IDAYLNGGSS EEGSNTSVAS 190 200 210 220 230 240 ESTSSDVVNA SATQALPEGD FPETTEKIPA MRKAIAKAMV NSKHTAPHVT LMDEIDVQEL 250 260 270 280 290 300 WDHRKKFKEI AAEQGTKLTF LPYVVKALVS ALKKYPALNT SFNEEAGEVV HKHYWNIGIA 310 320 330 340 350 360 ADTDKGLLVP VVKHADRKSI FEISDEINEL AVKARDGKLT SEEMKGATCT ISNIGSAGGQ 370 380 390 400 410 420 WFTPVINHPE VAILGIGRIA QKPIVKDGEI VAAPVLALSL SFDHRQIDGA TGQNAMNHIK 430 RLLNNPELLL MEG

References

[1]

"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015929 Genomic DNA. Translation: AAO04390.1.
RefSeq	NP_764348.1.
3D structure databases
HSSP	HSSP built from PDB template 2PDE based on UniProtKB P11961.
SMR	Q8CT13. Positions 2-79.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CT13.
Genome annotation databases
GeneID	1056530.
GenomeReviews	Gene locus SE_0793 in contig AE015929_GR.
KEGG	sep:SE0793.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8CT13.
OMA	KEDIDAY.
Enzyme and pathway databases
BioCyc	SEPI176280:SE_0793-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. 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]
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_STAES

Accession

Primary (citable) accession number: Q8CT13

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 52 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)