Reviewed, UniProtKB/Swiss-Prot P11961 (ODP2_BACST)

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

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 1 lipoyl cofactor covalently.
Subunit structure	Forms a 60-polypeptide structural core with icosahedral symmetry.
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	3D-structure 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 428

427

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

PRO_0000162273

Regions

Domain

2 – 76

75

Lipoyl-binding

Region

129 – 171

43

E1/E3 binding

Sites

Active site

399

1

Potential

Amino acid modifications

Modified residue

43

1

N6-lipoyllysine

Secondary structure

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428

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Beta strand

16 – 21

6

Beta strand

37 – 40

4

Beta strand

45 – 48

4

Beta strand

59 – 61

3

Beta strand

63 – 67

5

Beta strand

69 – 71

3

Helix

133 – 141

9

Turn

146 – 148

3

Helix

154 – 156

3

Helix

160 – 167

8

Beta strand

195 – 197

3

Helix

205 – 217

13

Beta strand

225 – 231

7

Helix

233 – 241

9

Helix

243 – 248

6

Helix

256 – 269

14

Helix

271 – 273

3

Beta strand

292 – 294

3

Helix

310 – 312

3

Helix

315 – 330

16

Helix

336 – 339

4

Beta strand

345 – 348

4

Turn

350 – 352

3

Beta strand

355 – 357

3

Beta strand

367 – 371

5

Beta strand

375 – 380

6

Beta strand

382 – 397

16

Turn

399 – 401

3

Helix

405 – 419

15

Helix

421 – 423

3

Sequences

	Sequence		Length	Mass (Da)
	P11961-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2600CD150261ACB0	FASTA	428	46,326
	10 20 30 40 50 60 MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS PVKGKVLEIL 70 80 90 100 110 120 VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT ETVSKEEKVD AVAPNAPAAE 130 140 150 160 170 180 AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE 190 200 210 220 230 240 KAAPAAAKPA TTEGEFPETR EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK 250 260 270 280 290 300 KFKAIAAEKG IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR 310 320 330 340 350 360 GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG SAGGQWFTPV 370 380 390 400 410 420 INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR MIDGATAQKA LNHIKRLLSD PELLLMEA

References

[1]	"Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus." Hawkins C.F., Borges A., Perham R.N. Eur. J. Biochem. 191:337-346(1990) [PubMed: 2200674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus." Packman L.C., Borges A., Perham R.N. Biochem. J. 252:79-86(1988) [PubMed: 3421911] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-201.
[3]	"Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex." Dardel F., Laue E.D., Perham R.N. Eur. J. Biochem. 201:203-209(1991) [PubMed: 1915365] [Abstract] Cited for: STRUCTURE BY NMR OF 1-86.
[4]	"Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex." Dardel F., Davis A.L., Laue E.D., Perham R.N. J. Mol. Biol. 229:1037-1048(1993) [PubMed: 8445635] [Abstract] Cited for: STRUCTURE BY NMR OF 1-86.
[5]	"The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus." Kalia Y.N., Brocklehurst S.M., Hipps D.S., Appella E., Sakaguchi K., Perham R.N. J. Mol. Biol. 230:323-341(1993) [PubMed: 8450544] [Abstract] Cited for: STRUCTURE BY NMR OF 129-171.
[6]	"Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase." Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J. Structure 4:277-286(1996) [PubMed: 8805537] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 129-171.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X53560 Genomic DNA. Translation: CAA37630.1.

PIR

S14426. S10799.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B5S	X-ray	4.40	A/B/C/D/E	185-425	[»]
1EBD	X-ray	2.60	C	130-170	[»]
1LAB	NMR	-	A	2-81	[»]
1LAC	NMR	-	A	2-81	[»]
1W3D	NMR	-	A	119-171	[»]
1W4E	NMR	-	A	126-169	[»]
1W4F	NMR	-	A	126-169	[»]
1W4G	NMR	-	A	126-169	[»]
1W85	X-ray	2.00	I/J	123-170	[»]
1W88	X-ray	2.30	I/J	123-170	[»]
2PDD	NMR	-	A	129-171	[»]
2PDE	NMR	-	A	129-171	[»]
3DUF	X-ray	2.50	I/J	1-428	[»]
3DV0	X-ray	2.50	I/J	1-428	[»]
3DVA	X-ray	2.35	I/J	1-428	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6156N.

Enzyme and pathway databases

BRENDA

2.3.1.12. 266715.

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. 1 hit.
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. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ODP2_BACST

Accession

Primary (citable) accession number: P11961

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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