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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Staphylococcus epidermidis (strain ATCC 12228)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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 activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei404Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciSEPI176280:G1G05-798-MONOMER

Names & Taxonomyi

Protein namesi
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 namesi
Name:pdhC
Ordered Locus Names:SE_0793
OrganismiStaphylococcus epidermidis (strain ATCC 12228)
Taxonomic identifieri176280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000001411 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622941 – 433Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

STRINGi176280.SE0793

Structurei

3D structure databases

ProteinModelPortaliQ8CT13
SMRiQ8CT13
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini128 – 165Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA
KOiK00627
OMAiTMEFESF

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

Q8CT13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFEFRLPDI GEGIHEGEIV KWFIKAGDTI EEDDVLAEVQ NDKSVVEIPS
60 70 80 90 100
PVSGTVEEVL VDEGTVAVVG DVIVKIDAPD AEEMQFKGHG DDEDSKKEEK
110 120 130 140 150
EQESPVQEEA SSTQSQEKTE VDESKTVKAM PSVRKYAREN GVNIKAVNGS
160 170 180 190 200
GKNGRITKED IDAYLNGGSS EEGSNTSVAS ESTSSDVVNA SATQALPEGD
210 220 230 240 250
FPETTEKIPA MRKAIAKAMV NSKHTAPHVT LMDEIDVQEL WDHRKKFKEI
260 270 280 290 300
AAEQGTKLTF LPYVVKALVS ALKKYPALNT SFNEEAGEVV HKHYWNIGIA
310 320 330 340 350
ADTDKGLLVP VVKHADRKSI FEISDEINEL AVKARDGKLT SEEMKGATCT
360 370 380 390 400
ISNIGSAGGQ WFTPVINHPE VAILGIGRIA QKPIVKDGEI VAAPVLALSL
410 420 430
SFDHRQIDGA TGQNAMNHIK RLLNNPELLL MEG
Length:433
Mass (Da):46,991
Last modified:March 1, 2003 - v1
Checksum:iEF82B61024832B27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015929 Genomic DNA Translation: AAO04390.1
RefSeqiNP_764348.1, NC_004461.1
WP_002467591.1, NC_004461.1

Genome annotation databases

EnsemblBacteriaiAAO04390; AAO04390; SE_0793
GeneIDi1056530
KEGGisep:SE0793
PATRICifig|176280.10.peg.766

Similar proteinsi

Entry informationi

Entry nameiODP2_STAES
AccessioniPrimary (citable) accession number: Q8CT13
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: May 23, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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