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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
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) (By similarity).By similarity

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 sitei425Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciLXYL281090:G1G06-2526-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:Lxx25050
OrganismiLeifsonia xyli subsp. xyli (strain CTCB07)
Taxonomic identifieri281090 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeLeifsonia
Proteomesi
  • UP000001306 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002324581 – 452Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi281090.Lxx25050

Structurei

3D structure databases

ProteinModelPortaliQ6ABX9
SMRiQ6ABX9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 78Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini170 – 207Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4107RN0 Bacteria
COG0508 LUCA
HOGENOMiHOG000281564
KOiK00627
OMAiDNLCEVQ
OrthoDBiPOG091H05OF

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
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
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

Q6ABX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRESQFLLPD VGEGLTEAEI VSWKVAPGDS VAVNQVIVEI ETAKSLVELP
60 70 80 90 100
SPFEGTVGEL LVVEGQTVEV GTPIFTVNGG EADHGVTEPA GEAEQAAVDA
110 120 130 140 150
AASVTHESEE PKAGAVIVGY GSAGHGTSRR RVTHPGAAAR PAAFPPAESA
160 170 180 190 200
AEPGRAPSTP VPPSGGGPVI AKPPIRKLAK DLGVDLSTVT ATGAIGEVTR
210 220 230 240 250
EDVLREGTQA SVFRNIQTPE WPDDREERIL VKGVRKAIAN AMVTSAFSAP
260 270 280 290 300
HVSVFVDVDA TRTMEFVKRL KSAPDFVGVK VSPLLIMAKA IVWAVRRNPT
310 320 330 340 350
VNSTWTDEEI IVRHYVNLGI AAATPRGLIV PNVKEAQGMS LLELAGALEE
360 370 380 390 400
LTLTAREGKT QPADMANGTI TITNIGVFGM DTGTPILNPG EVGIVALGTI
410 420 430 440 450
KQKPWVVDGE VRPRFVTTLG GSFDHRVVDG DVASRFLADV ASIIEEPALL

LD
Length:452
Mass (Da):47,427
Last modified:September 13, 2004 - v1
Checksum:iE82E69643536926A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016822 Genomic DNA Translation: AAT90113.1
RefSeqiWP_011187092.1, NC_006087.1

Genome annotation databases

EnsemblBacteriaiAAT90113; AAT90113; Lxx25050
KEGGilxx:Lxx25050

Similar proteinsi

Entry informationi

Entry nameiODP2_LEIXX
AccessioniPrimary (citable) accession number: Q6ABX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: September 13, 2004
Last modified: March 28, 2018
This is version 83 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
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Main funding by: National Institutes of Health