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Q59821 (ODP2_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length430 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).

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
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 – 430430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162292

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site4011 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59821 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AFE00748A65ACDA9

FASTA43046,439
        10         20         30         40         50         60 
MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS PVSGTVEEVM 

        70         80         90        100        110        120 
VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA KEEAPAEQAP VATQTEEVDE 

       130        140        150        160        170        180 
NRTVKAMPSV RKYAREKGVN IKAVSGSGKN GRITKEDVDA YLNGGAPTAS NESADSATNE 

       190        200        210        220        230        240 
EVAETPAAPA AVSLEGDFPE TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH 

       250        260        270        280        290        300 
RKKFKEIAAE QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT 

       310        320        330        340        350        360 
DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN IGSAGGQWFT 

       370        380        390        400        410        420 
PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD HRQIDGATGQ NAMNHIKRLL 

       430 
NNPELLLMEG 

« Hide

References

[1]"Lipoamide dehydrogenase of Staphylococcus aureus: nucleotide sequence and sequence analysis."
Hemila H.
Biochim. Biophys. Acta 1129:119-123(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27733 / V8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58434 Genomic DNA. Translation: CAA41339.1.
PIRS19722.

3D structure databases

ProteinModelPortalQ59821.
SMRQ59821. Positions 2-79, 121-165, 187-428.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ59821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0508.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 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]
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.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_STAAU
AccessionPrimary (citable) accession number: Q59821
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 76 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