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Q49110 (ODP2_MYCCT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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
Synonyms:odp2
Ordered Locus Names:MCAP_0227
OrganismMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) [Complete proteome] [HAMAP]
Taxonomic identifier340047 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length438 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 – 438438Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162280

Regions

Domain1 – 7575Lipoyl-binding

Sites

Active site4111 Potential

Amino acid modifications

Modified residue421N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49110 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4BF83B697480B4AB

FASTA43846,927
        10         20         30         40         50         60 
MFKVKFADIG EGLTEGTVAE VLVKVGDVVK EGQSLYFVET DKVNSEIPAP VAGKIAVINI 

        70         80         90        100        110        120 
KAGQEIKVGD VVMEIEDGSD TSATSEPKAE TKSEAKVEVV EENASVVGAT PVSNDVIVRK 

       130        140        150        160        170        180 
QTTTVNKSST IKATPLARKV AADLNIDLSL VTPTGPNQRI LVADIKNHQA SSTQLASQPI 

       190        200        210        220        230        240 
SQPAPTPSPS AHQTIAPTIK VVEPSAPLSW DEVPMNGVRK ATVKAMTKSH TEIAAFTGMK 

       250        260        270        280        290        300 
NTDITETHKM RTELKDHAAA SGIKLTYLAF IIKAVAKSLR DMPNINVRGD FANNKIQFMH 

       310        320        330        340        350        360 
NINIGIAVDT PNGLMVPVIK GADHLSVFEI AIKISELANK AKDGKLTRAE MTEATFTVSN 

       370        380        390        400        410        420 
FGSVGLDYAT PIINSPESAI LGVGTMSQTP LYINGELQKR FIMPLSMTCD HRIIDGADAG 

       430 
RFLIKVQDYL SKPVLLFM 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in Mycoplasma capricolum."
Zhu P.P., Peterkofsky A.
Protein Sci. 5:1719-1736(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O., Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: California kid / ATCC 27343 / NCTC 10154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62057 Genomic DNA. Translation: AAC44344.1.
CP000123 Genomic DNA. Translation: ABC01559.1.
RefSeqYP_424214.1. NC_007633.1.

3D structure databases

ProteinModelPortalQ49110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340047.MCAP_0227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC01559; ABC01559; MCAP_0227.
GeneID3828394.
KEGGmcp:MCAP_0227.
PATRIC20004919. VBIMycCap130493_0230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281564.
KOK00627.
OMAEGNTQPP.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycMCAP340047:GC0H-225-MONOMER.

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_MYCCT
AccessionPrimary (citable) accession number: Q49110
Secondary accession number(s): Q2SSP9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 96 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