Reviewed, UniProtKB/Swiss-Prot P21874 (ODPB_BACST)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1

Gene names

Name:

pdhB

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	325 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	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Subunit structure	Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	pyruvate dehydrogenase (acetyl-transferring) 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

Initiator methionine

1

1

Removed

Chain

2 – 325

324

Pyruvate dehydrogenase E1 component subunit beta

PRO_0000162221

Sites

Binding site

60

1

Thiamine pyrophosphate By similarity

Secondary structure

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325

Helix Strand Turn

Details...

Helix

6 – 20

15

Beta strand

24 – 28

5

Turn

40 – 43

4

Helix

44 – 48

5

Turn

50 – 52

3

Beta strand

53 – 55

3

Helix

60 – 72

13

Beta strand

76 – 80

5

Helix

84 – 89

6

Helix

91 – 95

5

Helix

98 – 100

3

Helix

101 – 104

4

Turn

105 – 107

3

Beta strand

114 – 119

6

Beta strand

121 – 123

3

Helix

134 – 137

4

Beta strand

144 – 146

3

Helix

151 – 163

13

Beta strand

164 – 166

3

Beta strand

168 – 173

6

Turn

174 – 176

3

Beta strand

177 – 179

3

Beta strand

197 – 200

4

Beta strand

203 – 209

7

Helix

213 – 226

14

Beta strand

231 – 235

5

Beta strand

237 – 241

5

Helix

244 – 254

11

Beta strand

257 – 264

8

Beta strand

267 – 269

3

Helix

270 – 281

12

Helix

282 – 284

3

Beta strand

290 – 294

5

Beta strand

296 – 299

4

Helix

302 – 304

3

Helix

305 – 308

4

Helix

312 – 323

12

Sequences

	Sequence		Length	Mass (Da)
	P21874-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: AD1F2D4F82D652AC	FASTA	325	35,460
	10 20 30 40 50 60 MAQMTMVQAI TDALRIELKN DPNVLIFGED VGVNGGVFRA TEGLQAEFGE DRVFDTPLAE 70 80 90 100 110 120 SGIGGLAIGL ALQGFRPVPE IQFFGFVYEV MDSICGQMAR IRYRTGGRYH MPITIRSPFG 130 140 150 160 170 180 GGVHTPELHS DSLEGLVAQQ PGLKVVIPST PYDAKGLLIS AIRDNDPVIF LEHLKLYRSF 190 200 210 220 230 240 RQEVPEGEYT IPIGKADIKR EGKDITIIAY GAMVHESLKA AAELEKEGIS AEVVDLRTVQ 250 260 270 280 290 300 PLDIETIIGS VEKTGRAIVV QEAQRQAGIA ANVVAEINER AILSLEAPVL RVAAPDTVYP 310 320 FAQAESVWLP NFKDVIETAK KVMNF

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], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus." Borges A., Hawkins C.F., Packman L.C., Perham R.N. Eur. J. Biochem. 194:95-102(1990) [PubMed: 2253629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X53560 Genomic DNA. Translation: CAA37629.1.

PIR

S14230.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W85	X-ray	2.00	B/D/F/H	2-324	[»]
1W88	X-ray	2.30	B/D/F/H	2-324	[»]
3DUF	X-ray	2.50	B/D/F/H	1-325	[»]
3DV0	X-ray	2.50	B/D/F/H	1-325	[»]
3DVA	X-ray	2.35	B/D/F/H	1-325	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.4.1. 266715.

Family and domain databases

InterPro

IPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]

Gene3D

G3DSA:3.40.50.920. Transketo_C_like. 1 hit.

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ODPB_BACST

Accession

Primary (citable) accession number: P21874

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 26, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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