NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924;
PubMed=2200674 [NCBI, ExPASy, EBI, Israel, Japan]
Hawkins C.F., Borges A., Perham R.N.;
"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.";
Eur. J. Biochem. 191:337-346(1990).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2253629 [NCBI, ExPASy, EBI, Israel, Japan]
Borges A., Hawkins C.F., Packman L.C., Perham R.N.;
"Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.";
Eur. J. Biochem. 194:95-102(1990).

Comments

FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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: Heterodimer of an alpha and a beta chain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X53560; CAA37629.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S14230; S14230.

3D structure databases

PDB

1W85; X-ray; 2.00 A; B/D/F/H=1-325.	[ExPASy / RCSB / EBI]
1W88; X-ray; 2.30 A; B/D/F/H=1-325.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1W85; -.
1W88; -.

ModBase

P21874.

Ontologies

GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.920; Transketo_C_like; 1.

Pfam

PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.

ProtoNet

P21874.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 325`	`324`	`Pyruvate dehydrogenase E1 component subunit beta.`	`PRO_0000162221`
`BINDING`	`60 60`		`Thiamine pyrophosphate (By similarity).`
`HELIX`	`6 20`	`15`
`STRAND`	`24 28`	`5`
`TURN`	`40 43`	`4`
`HELIX`	`44 48`	`5`
`TURN`	`50 52`	`3`
`STRAND`	`53 55`	`3`
`HELIX`	`60 72`	`13`
`STRAND`	`76 80`	`5`
`HELIX`	`84 89`	`6`
`HELIX`	`91 95`	`5`
`HELIX`	`98 100`	`3`
`HELIX`	`101 104`	`4`
`TURN`	`105 107`	`3`
`STRAND`	`114 119`	`6`
`STRAND`	`121 123`	`3`
`HELIX`	`134 137`	`4`
`STRAND`	`144 146`	`3`
`HELIX`	`151 163`	`13`
`STRAND`	`164 166`	`3`
`STRAND`	`168 173`	`6`
`TURN`	`174 176`	`3`
`STRAND`	`177 179`	`3`
`STRAND`	`197 200`	`4`
`STRAND`	`203 209`	`7`
`HELIX`	`213 226`	`14`
`STRAND`	`231 235`	`5`
`STRAND`	`237 241`	`5`
`HELIX`	`244 254`	`11`
`STRAND`	`257 264`	`8`
`STRAND`	`267 269`	`3`
`HELIX`	`270 281`	`12`
`HELIX`	`282 284`	`3`
`STRAND`	`290 294`	`5`
`STRAND`	`296 299`	`4`
`HELIX`	`302 304`	`3`
`HELIX`	`305 308`	`4`
`HELIX`	`312 323`	`12`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 35460 Da [This is the MW of the unprocessed precursor]

CRC64: AD1F2D4F82D652AC [This is a checksum on the sequence]

        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

P21874 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools