Q5HQ74 (ODP2_STAEQ) 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:	SERP0682

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	433 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).
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
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_0000162295
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)
	Q5HQ74 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 38D2B61DBF832B22	FASTA	433	46,963
	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 EEGSNTSAAS 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]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35984 / RP62A.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000029 Genomic DNA. Translation: AAW54054.1.
RefSeq	YP_188266.1. NC_002976.3.
3D structure databases
ProteinModelPortal	Q5HQ74.
SMR	Q5HQ74. Positions 2-79, 124-168, 190-431.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HQ74.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000043164; EBSTAP00000041707; EBSTAG00000043162.
GeneID	3240397.
GenomeReviews	Gene locus SERP0682 in contig CP000029_GR.
KEGG	ser:SERP0682.
NMPDR	fig|176279.3.peg.596.
PATRIC	19612233. VBIStaEpi130894_0660.
TIGR	SERP0682.
Phylogenomic databases
eggNOG	COG0508.
GeneTree	EBGT00050000024152.
HOGENOM	HBG630916.
OMA	KEDIDAY.
PhylomeDB	Q5HQ74.
ProtClustDB	PRK11856.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP0682-MONOMER.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.559.10. CAT-like_dom. 1 hit. G3DSA:4.10.320.10. E3_bd. 1 hit.
KO	K00627.
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.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_STAEQ

Accession

Primary (citable) accession number: Q5HQ74

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program