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P35489 (ODP2_ACHLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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
OrganismAcholeplasma laidlawii
Taxonomic identifier2148 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
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 2 lipoyl cofactors covalently Potential.

Subunit structure

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

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
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 – 544544Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162270

Regions

Domain1 – 7575Lipoyl-binding 1
Domain114 – 18774Lipoyl-binding 2

Sites

Active site5161 Potential

Amino acid modifications

Modified residue421N6-lipoyllysine By similarity
Modified residue1541N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P35489 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 81E92D869CFD5424

FASTA54457,261
        10         20         30         40         50         60 
MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP VDGTIVSLGA 

        70         80         90        100        110        120 
KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA APQVAAPAAS GDIYDFKFAD 

       130        140        150        160        170        180 
IGEGIHEGTI LQWNFKVGDK VKEGETLVVV ETDKVNAELP SPVDGTILKL GKAEGEVIHV 

       190        200        210        220        230        240 
GETVVLIGQN GATLEQAQAP KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK 

       250        260        270        280        290        300 
VLASPVARKL ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS 

       310        320        330        340        350        360 
VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD ALVNFRNEAK 

       370        380        390        400        410        420 
GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE VYIKKFINLG MAVDTPDGLI 

       430        440        450        460        470        480 
VPNIKNADRL SVFELASQVR SLADDTIARK ISMDQQTGGT FTITNFGSAG IAFGTPVINY 

       490        500        510        520        530        540 
PELAILGIGK IDRKPWVVGN EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL 


LLLS 

« Hide

References

[1]"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii."
Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.
J. Bacteriol. 174:1388-1396(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81753 Genomic DNA. Translation: AAA21909.1.
PIRC42653.

3D structure databases

ProteinModelPortalP35489.
ModBaseSearch...
MobiDBSearch...

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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_ACHLA
AccessionPrimary (citable) accession number: P35489
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 77 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