SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CT13

- ODP2_STAES

UniProt

Q8CT13 - ODP2_STAES

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
pdhC, SE_0793
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Status
Reviewed - 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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei404 – 4041 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciSEPI176280:GCDG-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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001411: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysine By similarity

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. Positions 2-79, 124-168, 190-431.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
KOiK00627.
OMAiVAFRTRI.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CT13-1 [UniParc]FASTAAdd to Basket

« Hide

MAFEFRLPDI GEGIHEGEIV KWFIKAGDTI EEDDVLAEVQ NDKSVVEIPS    50
PVSGTVEEVL VDEGTVAVVG DVIVKIDAPD AEEMQFKGHG DDEDSKKEEK 100
EQESPVQEEA SSTQSQEKTE VDESKTVKAM PSVRKYAREN GVNIKAVNGS 150
GKNGRITKED IDAYLNGGSS EEGSNTSVAS ESTSSDVVNA SATQALPEGD 200
FPETTEKIPA MRKAIAKAMV NSKHTAPHVT LMDEIDVQEL WDHRKKFKEI 250
AAEQGTKLTF LPYVVKALVS ALKKYPALNT SFNEEAGEVV HKHYWNIGIA 300
ADTDKGLLVP VVKHADRKSI FEISDEINEL AVKARDGKLT SEEMKGATCT 350
ISNIGSAGGQ WFTPVINHPE VAILGIGRIA QKPIVKDGEI VAAPVLALSL 400
SFDHRQIDGA TGQNAMNHIK RLLNNPELLL MEG 433
Length:433
Mass (Da):46,991
Last modified:March 1, 2003 - v1
Checksum:iEF82B61024832B27
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO04390.1.
RefSeqiNP_764348.1. NC_004461.1.

Genome annotation databases

EnsemblBacteriaiAAO04390; AAO04390; SE_0793.
GeneIDi1056530.
KEGGisep:SE0793.
PATRICi19607383. VBIStaEpi113981_0766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO04390.1 .
RefSeqi NP_764348.1. NC_004461.1.

3D structure databases

ProteinModelPortali Q8CT13.
SMRi Q8CT13. Positions 2-79, 124-168, 190-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176280.SE0793.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO04390 ; AAO04390 ; SE_0793 .
GeneIDi 1056530.
KEGGi sep:SE0793.
PATRICi 19607383. VBIStaEpi113981_0766.

Phylogenomic databases

eggNOGi COG0508.
KOi K00627.
OMAi VAFRTRI.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci SEPI176280:GCDG-798-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12228.

Entry informationi

Entry nameiODP2_STAES
AccessioniPrimary (citable) accession number: Q8CT13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi