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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

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:SERP0682
OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Taxonomic identifieri176279 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000531 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622951 – 433Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST433

Amino acid modifications

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

Proteomic databases

PRIDEiQ5HQ74.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi176279.SERP0682.

Structurei

3D structure databases

ProteinModelPortaliQ5HQ74.
SMRiQ5HQ74.
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.
HOGENOMiHOG000281564.
KOiK00627.
OMAiTMEFESF.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR036625. E3-bd_dom_sf.
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.

Q5HQ74-1 [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 EEGSNTSAAS 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):46,963
Last modified:February 15, 2005 - v1
Checksum:i38D2B61DBF832B22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000029 Genomic DNA. Translation: AAW54054.1.
RefSeqiWP_001831683.1. NC_002976.3.

Genome annotation databases

EnsemblBacteriaiAAW54054; AAW54054; SERP0682.
KEGGiser:SERP0682.

Similar proteinsi

Entry informationi

Entry nameiODP2_STAEQ
AccessioniPrimary (citable) accession number: Q5HQ74
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: October 25, 2017
This is version 87 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families