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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 sitei401Sequence 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:SA0945
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622891 – 430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST430

Amino acid modifications

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

2D gel databases

SWISS-2DPAGEP99131

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP65636
SMRiP65636
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini125 – 162Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

HOGENOMiHOG000281564
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.

P65636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS
60 70 80 90 100
PVSGTVEEVM VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA
110 120 130 140 150
KEEAPAEQAP VATQTEEVDE NRTVKAMPSV RKYAREKGVN IKAVSGSGKN
160 170 180 190 200
GRITKEDVDA YLNGGAPTAS NESAASATSE EVAETPAAPA AVSLEGDFPE
210 220 230 240 250
TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH RKKFKEIAAE
260 270 280 290 300
QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT
310 320 330 340 350
DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN
360 370 380 390 400
IGSAGGQWFT PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD
410 420 430
HRQIDGATGQ NAMNHIKRLL NNPELLLMEG
Length:430
Mass (Da):46,368
Last modified:October 11, 2004 - v1
Checksum:i4050074CAE5ACDA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB42191.1
PIRiD89879
RefSeqiWP_000863439.1, NC_002745.2

Genome annotation databases

EnsemblBacteriaiBAB42191; BAB42191; BAB42191
KEGGisau:SA0945

Similar proteinsi

Entry informationi

Entry nameiODP2_STAAN
AccessioniPrimary (citable) accession number: P65636
Secondary accession number(s): Q99V06
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 28, 2018
This is version 89 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
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Main funding by: National Institutes of Health