Reviewed, UniProtKB/Swiss-Prot P75392 (ODP2_MYCPN)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene names

Name:	pdhC
Ordered Locus Names:	MPN_391
ORF Names:	MP447

Organism

Mycoplasma pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

2104 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Glycolysis
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 402	402	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162282
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	374	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75392-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: F09314A9E714A1D6	FASTA	402	42,397
	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

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: 8948633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29342 / M129.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00089 Genomic DNA. Translation: AAB96095.1.
PIR	S73773.
RefSeq	NP_110079.1.
3D structure databases
HSSP	HSSP built from PDB template 1LAB based on UniProtKB P11961.
ModBase	Search...
Genome annotation databases
GeneID	877106.
GenomeReviews	Gene locus MPN_391 in contig U00089_GR.
KEGG	mpn:MPN391.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P75392.
OMA	EMCIVAT.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-584. MPNE272634:MPN391-MON.
BRENDA	2.3.1.12. 39500.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_MYCPN

Accession

Primary (citable) accession number: P75392

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)