Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P75392 (ODP2_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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
Ordered Locus Names:MPN_391
ORF Names:MP447
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129) [Reference proteome] [HAMAP]
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length402 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
Reference 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 – 402402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162282

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3741 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P75392 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F09314A9E714A1D6

FASTA40242,397
        10         20         30         40         50         60 
MANEFKFTDV GEGLHEGKVT EILKKVGDTI KVDEALFVVE TDKVTTELPS PYAGVITAIT 

        70         80         90        100        110        120 
TNVGDVVHIG QVMAVIDDGA GAAAPAAPQP VSAPAPAPTP TFTPTPAPVT TEPVVEEAGA 

       130        140        150        160        170        180 
SVVGEIKVSN SVFPIFGVQP SAPQPTPAPV VQPTSAPTPT PAPASAAAPS GEETIAITTM 

       190        200        210        220        230        240 
RKAIAEAMVK SHENIPATIL TFYVNATKLK QYRESVNGLA LSKYNMKISF FAFFVKAIVN 

       250        260        270        280        290        300 
ALKKFPVFNG RYDKERNLIV LNKDVNVGIA VDTPDGLIVP NIKQAQTKSV VDIAKDIVDL 

       310        320        330        340        350        360 
ANRARSKQIK LPDLSKGTIS VTNFGSLGAA FGTPIIKHPE MCIVATGNME ERVVRAEGGV 

       370        380        390        400 
AVHTILPLTI AADHRWVDGA DVGRFGKEIA KQIEELIDLE VA 

« Hide

References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB96095.1.
PIRS73773.
RefSeqNP_110079.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP75392. 1 interaction.
STRING272634.MPN391.

Proteomic databases

PaxDbP75392.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB96095; AAB96095; MPN_391.
GeneID877106.
KEGGmpn:MPN391.
PATRIC20022158. VBIMycPne110_0422.

Phylogenomic databases

eggNOGCOG0508.
KOK00627.
OMAFWHVSEG.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-584.
MPNE272634:GJ6Z-413-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_MYCPN
AccessionPrimary (citable) accession number: P75392
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 85 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

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names