Reviewed, UniProtKB/Swiss-Prot P35489 (ODP2_ACHLA)

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

Organism

Acholeplasma laidlawii

Taxonomic identifier

2148 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	544 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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).
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 2 lipoyl cofactors covalently Potential.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
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 protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 544	544	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162270
Regions
	Domain	1 – 75	75	Lipoyl-binding 1
	Domain	114 – 187	74	Lipoyl-binding 2
Sites
	Active site	516	1	Potential
Amino acid modifications
	Modified residue	42	1	N6-lipoyllysine By similarity
	Modified residue	154	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35489-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 81E92D869CFD5424	FASTA	544	57,261
	10 20 30 40 50 60 MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP VDGTIVSLGA 70 80 90 100 110 120 KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA APQVAAPAAS GDIYDFKFAD 130 140 150 160 170 180 IGEGIHEGTI LQWNFKVGDK VKEGETLVVV ETDKVNAELP SPVDGTILKL GKAEGEVIHV 190 200 210 220 230 240 GETVVLIGQN GATLEQAQAP KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK 250 260 270 280 290 300 VLASPVARKL ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAEAQAPVQQ TQAPAQAAAS 310 320 330 340 350 360 VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD ALVNFRNEAK 370 380 390 400 410 420 GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE VYIKKFINLG MAVDTPDGLI 430 440 450 460 470 480 VPNIKNADRL SVFELASQVR SLADDTIARK ISMDQQTGGT FTITNFGSAG IAFGTPVINY 490 500 510 520 530 540 PELAILGIGK IDRKPWVVGN EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL LLLS

References

[1]

"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii." Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A. J. Bacteriol. 174:1388-1396(1992) [PubMed: 1735725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M81753 Genomic DNA. Translation: AAA21909.1.
PIR	C42653.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.12. 96506.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_ACHLA

Accession

Primary (citable) accession number: P35489

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 61 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)