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Q6ABX9 (ODP2_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:pdhC
Ordered Locus Names:Lxx25050
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

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

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000232458

Regions

Domain4 – 7774Lipoyl-binding

Sites

Active site4251 Potential

Amino acid modifications

Modified residue441N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ABX9 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: E82E69643536926A

FASTA45247,427
        10         20         30         40         50         60 
MRESQFLLPD VGEGLTEAEI VSWKVAPGDS VAVNQVIVEI ETAKSLVELP SPFEGTVGEL 

        70         80         90        100        110        120 
LVVEGQTVEV GTPIFTVNGG EADHGVTEPA GEAEQAAVDA AASVTHESEE PKAGAVIVGY 

       130        140        150        160        170        180 
GSAGHGTSRR RVTHPGAAAR PAAFPPAESA AEPGRAPSTP VPPSGGGPVI AKPPIRKLAK 

       190        200        210        220        230        240 
DLGVDLSTVT ATGAIGEVTR EDVLREGTQA SVFRNIQTPE WPDDREERIL VKGVRKAIAN 

       250        260        270        280        290        300 
AMVTSAFSAP HVSVFVDVDA TRTMEFVKRL KSAPDFVGVK VSPLLIMAKA IVWAVRRNPT 

       310        320        330        340        350        360 
VNSTWTDEEI IVRHYVNLGI AAATPRGLIV PNVKEAQGMS LLELAGALEE LTLTAREGKT 

       370        380        390        400        410        420 
QPADMANGTI TITNIGVFGM DTGTPILNPG EVGIVALGTI KQKPWVVDGE VRPRFVTTLG 

       430        440        450 
GSFDHRVVDG DVASRFLADV ASIIEEPALL LD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT90113.1.
RefSeqYP_063218.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6ABX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx25050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT90113; AAT90113; Lxx25050.
GeneID2940497.
KEGGlxx:Lxx25050.
PATRIC22338780. VBILeiXyl11655_2622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281564.
KOK00627.
OMATIKQKPW.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-2349-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_LEIXX
AccessionPrimary (citable) accession number: Q6ABX9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families