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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei374 – 3741Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pdhC
Ordered Locus Names:MPN_391
ORF Names:MP447
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000808: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysineBy similarityPROSITE-ProRule annotation

Proteomic databases

PaxDbiP75392.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP75392. 1 interaction.
STRINGi272634.MPN391.

Structurei

3D structure databases

ProteinModelPortaliP75392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
KOiK00627.
OMAiSPYQVWS.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P75392-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANEFKFTDV GEGLHEGKVT EILKKVGDTI KVDEALFVVE TDKVTTELPS
60 70 80 90 100
PYAGVITAIT TNVGDVVHIG QVMAVIDDGA GAAAPAAPQP VSAPAPAPTP
110 120 130 140 150
TFTPTPAPVT TEPVVEEAGA SVVGEIKVSN SVFPIFGVQP SAPQPTPAPV
160 170 180 190 200
VQPTSAPTPT PAPASAAAPS GEETIAITTM RKAIAEAMVK SHENIPATIL
210 220 230 240 250
TFYVNATKLK QYRESVNGLA LSKYNMKISF FAFFVKAIVN ALKKFPVFNG
260 270 280 290 300
RYDKERNLIV LNKDVNVGIA VDTPDGLIVP NIKQAQTKSV VDIAKDIVDL
310 320 330 340 350
ANRARSKQIK LPDLSKGTIS VTNFGSLGAA FGTPIIKHPE MCIVATGNME
360 370 380 390 400
ERVVRAEGGV AVHTILPLTI AADHRWVDGA DVGRFGKEIA KQIEELIDLE

VA
Length:402
Mass (Da):42,397
Last modified:February 1, 1997 - v1
Checksum:iF09314A9E714A1D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96095.1.
PIRiS73773.
RefSeqiNP_110079.1. NC_000912.1.

Genome annotation databases

EnsemblBacteriaiAAB96095; AAB96095; MPN_391.
GeneIDi877106.
KEGGimpn:MPN391.
PATRICi20022158. VBIMycPne110_0422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96095.1.
PIRiS73773.
RefSeqiNP_110079.1. NC_000912.1.

3D structure databases

ProteinModelPortaliP75392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP75392. 1 interaction.
STRINGi272634.MPN391.

Proteomic databases

PaxDbiP75392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB96095; AAB96095; MPN_391.
GeneIDi877106.
KEGGimpn:MPN391.
PATRICi20022158. VBIMycPne110_0422.

Phylogenomic databases

eggNOGiCOG0508.
KOiK00627.
OMAiSPYQVWS.
OrthoDBiEOG610413.

Enzyme and pathway databases

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

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiODP2_MYCPN
AccessioniPrimary (citable) accession number: P75392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycoplasma pneumoniae
    Mycoplasma pneumoniae (strain M129): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.