Pyruvate dehydrogenase E1 component subunit alpha - Bacillus stearothermophilus

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Reviewed, UniProtKB/Swiss-Prot P21873 (ODPA_BACST)

Last modified June 16, 2009. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

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

Gene names

Name:

pdhA

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › 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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC thiamin 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

Removed Ref.1

Chain

368

Pyruvate dehydrogenase E1 component subunit alpha

PRO_0000162198

Secondary structure

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369

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P21873-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DBF43982C0E1926D
Show »

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: 2200674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35; 54-111 AND 269-331.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.

+

Additional computationally mapped references.

Cross-references

Sequence databases

X53560 Genomic DNA. Translation: CAA37628.1.

PIR

DEBSPF. S10798.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W85	X-ray	2.00	A/C/E/G	2-368	[»]
1W88	X-ray	2.30	A/C/E/G	2-368	[»]
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	[»]

ModBase

Enzyme and pathway databases

BRENDA

1.2.4.1. 266715.

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

Entry information

Entry name

ODPA_BACST

Accession

Primary (citable) accession number: P21873

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 67 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)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents