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P11961 (ODP2_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subunit structure

Forms a 60-polypeptide structural core with icosahedral symmetry.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglycolysis

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

Initiator methionine11Removed Ref.2
Chain2 – 428427Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162273

Regions

Domain2 – 7675Lipoyl-binding
Region129 – 17143E1/E3 binding

Sites

Active site3991 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine

Secondary structure

....................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11961 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2600CD150261ACB0

FASTA42846,326
        10         20         30         40         50         60 
MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS PVKGKVLEIL 

        70         80         90        100        110        120 
VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT ETVSKEEKVD AVAPNAPAAE 

       130        140        150        160        170        180 
AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE 

       190        200        210        220        230        240 
KAAPAAAKPA TTEGEFPETR EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK 

       250        260        270        280        290        300 
KFKAIAAEKG IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR 

       310        320        330        340        350        360 
GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG SAGGQWFTPV 

       370        380        390        400        410        420 
INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR MIDGATAQKA LNHIKRLLSD 


PELLLMEA 

« Hide

References

[1]"Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
Hawkins C.F., Borges A., Perham R.N.
Eur. J. Biochem. 191:337-346(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]"Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus."
Packman L.C., Borges A., Perham R.N.
Biochem. J. 252:79-86(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-201.
[3]"Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
Dardel F., Laue E.D., Perham R.N.
Eur. J. Biochem. 201:203-209(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-86.
[4]"Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
Dardel F., Davis A.L., Laue E.D., Perham R.N.
J. Mol. Biol. 229:1037-1048(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-86.
[5]"The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
Kalia Y.N., Brocklehurst S.M., Hipps D.S., Appella E., Sakaguchi K., Perham R.N.
J. Mol. Biol. 230:323-341(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 129-171.
[6]"Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase."
Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.
Structure 4:277-286(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 129-171.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53560 Genomic DNA. Translation: CAA37630.1.
PIRS14426. S10799.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B5SX-ray4.40A/B/C/D/E185-425[»]
1EBDX-ray2.60C130-170[»]
1LABNMR-A2-81[»]
1LACNMR-A2-81[»]
1W3DNMR-A119-171[»]
1W4ENMR-A126-169[»]
1W4FNMR-A126-169[»]
1W4GNMR-A126-169[»]
1W85X-ray2.00I/J123-170[»]
1W88X-ray2.30I/J123-170[»]
2PDDNMR-A129-171[»]
2PDENMR-A129-171[»]
3DUFX-ray2.50I/J1-428[»]
3DV0X-ray2.50I/J1-428[»]
3DVAX-ray2.35I/J1-428[»]
ProteinModelPortalP11961.
SMRP11961. Positions 2-81, 126-170, 185-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6156N.
IntActP11961. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP11961.

Entry information

Entry nameODP2_GEOSE
AccessionPrimary (citable) accession number: P11961
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 109 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references