P21873 (ODPA_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

pdhA

Organism

Geobacillus stearothermophilus (Bacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	369 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
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate 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.1

Chain

2 – 369

368

Pyruvate dehydrogenase E1 component subunit alpha

PRO_0000162198

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

369

Helix Strand Turn

Details...

Helix

10 – 19

10

Helix

36 – 38

3

Helix

44 – 69

26

Helix

83 – 91

9

Beta strand

98 – 100

3

Beta strand

102 – 104

3

Helix

106 – 111

6

Helix

116 – 124

9

Helix

127 – 130

4

Helix

147 – 161

15

Beta strand

168 – 173

6

Helix

175 – 178

4

Helix

180 – 191

12

Beta strand

196 – 202

7

Beta strand

204 – 206

3

Helix

211 – 213

3

Helix

221 – 226

6

Beta strand

231 – 235

5

Helix

239 – 254

16

Beta strand

260 – 265

6

Beta strand

274 – 277

4

Helix

278 – 280

3

Helix

285 – 292

8

Helix

296 – 306

11

Helix

312 – 334

23

Helix

341 – 346

6

Helix

354 – 366

13

Sequences

	Sequence		Length	Mass (Da)
	P21873 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DBF43982C0E1926D	FASTA	369	41,469
	10 20 30 40 50 60 MGVKTFQFPF AEQLEKVAEQ FPTFQILNEE GEVVNEEAMP ELSDEQLKEL MRRMVYTRIL 70 80 90 100 110 120 DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL PGYRDVPQII WHGLPLYQAF 130 140 150 160 170 180 LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI QAAGVALGLK MRGKKAVAIT YTGDGGTSQG 190 200 210 220 230 240 DFYEGINFAG AFKAPAIFVV QNNRFAISTP VEKQTVAKTL AQKAVAAGIP GIQVDGMDPL 250 260 270 280 290 300 AVYAAVKAAR ERAINGEGPT LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF 310 320 330 340 350 360 RKFLEAKGLW SEEEENNVIE QAKEEIKEAI KKADETPKQK VTDLISIMFE ELPFNLKEQY EIYKEKESK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35; 54-111 AND 269-331. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53560 Genomic DNA. Translation: CAA37628.1.

PIR

DEBSPF. S10798.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W85	X-ray	2.00	A/C/E/G	2-369	[»]
1W88	X-ray	2.30	A/C/E/G	2-369	[»]
3DUF	X-ray	2.50	A/C/E/G	1-369	[»]
3DV0	X-ray	2.50	A/C/E/G	1-369	[»]
3DVA	X-ray	2.35	A/C/E/G	1-369	[»]

ProteinModelPortal

P21873.

SMR

P21873. Positions 5-369.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29596N.

IntAct

P21873. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P21873.

Family and domain databases

InterPro

IPR001017. DH_E1.
IPR017596. Pyrv_DH_E1_asu_subgrp-x.
[Graphical view]

Pfam

PF00676. E1_dh. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03181. PDH_E1_alph_x. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P21873.

Entry information

Entry name

ODPA_GEOSE

Accession

Primary (citable) accession number: P21873

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program