P47514 (ODP2_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pdhC
Ordered Locus Names:	MG272

Organism

Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]

Taxonomic identifier

243273 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Mycoplasmatales › Mycoplasmataceae › Mycoplasma › Mycoplasma genitalium

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162281
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	356	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47514 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: BF5585A82425E3A8	FASTA	384	41,453
	10 20 30 40 50 60 MANEFKFTDV GEGLHEGKVT EILKQVGDQI KIDEALFVVE TDKVTTELPS PFAGTISAIN 70 80 90 100 110 120 VKVGDVVSIG QVMAVIGEKT STPLVEPKPQ PTEEVAKVKE AGASVVGEIK VSDNLFPIFG 130 140 150 160 170 180 VKPHATPAVK DTKVASSTNI TVETTQKPES KTEQKTIAIS TMRKAIAEAM TKSHAIIPTT 190 200 210 220 230 240 VLTFYVNATK LKQYRESVNG YALSKYSMKI SYFAFFVKAI VNALKKFPVF NASYDPDQNE 250 260 270 280 290 300 IVLNDDINVG IAVDTEEGLI VPNIKQAQTK SVVEIAQAIV DLANKARTKK IKLTDLNKGT 310 320 330 340 350 360 ISVTNFGSLG AAVGTPIIKY PEMCIVATGN LEERIVKVEN GIAVHTILPL TIAADHRWVD 370 380 GADVGRFGKE IAKQIEELID LTVA

References

[1]

"The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. , Phillips C.A., Merrick J.M., Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C. Science 270:397-403(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43967 Genomic DNA. Translation: AAC71494.1.
PIR	A64230.
RefSeq	NP_072939.1. NC_000908.2.
3D structure databases
ProteinModelPortal	P47514.
ModBase	Search...
Protein-protein interaction databases
STRING	243273.MG_272.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC71494; AAC71494; MG_272.
GeneID	875388.
KEGG	mge:MG_272.
PATRIC	20010044. VBIMycGen98045_0314.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
KO	K00627.
OMA	EMCIVAT.
ProtClustDB	PRK11856.
Enzyme and pathway databases
BioCyc	MGEN243273:GH2R-300-MONOMER.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_MYCGE

Accession

Primary (citable) accession number: P47514

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program