Q49110 (ODP2_MYCCT) 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
Synonyms:	odp2
Ordered Locus Names:	MCAP_0227

Organism

Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) [Complete proteome] [HAMAP]

Taxonomic identifier

340047 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Mycoplasmatales › Mycoplasmataceae › Mycoplasma › Mycoplasma mycoides group › Mycoplasma capricolum › Mycoplasma capricolum subsp. capricolum

Protein attributes

Sequence length	438 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 – 438	438	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162280
Regions
	Domain	1 – 75	75	Lipoyl-binding
Sites
	Active site	411	1	Potential
Amino acid modifications
	Modified residue	42	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49110 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4BF83B697480B4AB	FASTA	438	46,927
	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

References

	« Hide 'large scale' referencesShow '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.
RefSeq	YP_424214.1. NC_007633.1.
3D structure databases
ProteinModelPortal	Q49110.
ModBase	Search...
Protein-protein interaction databases
STRING	340047.MCAP_0227.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABC01559; ABC01559; MCAP_0227.
GeneID	3828394.
KEGG	mcp:MCAP_0227.
PATRIC	20004919. VBIMycCap130493_0230.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281564.
KO	K00627.
OMA	DITETHK.
ProtClustDB	PRK11856.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_MYCCT

Accession

Primary (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:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program