NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-42.
DOI=10.1016/0166-6851(91)90022-X; PubMed=2052042 [NCBI, ExPASy, EBI, Israel, Japan]
Wheelock M.J., Komuniecki R., Duran E., Johnson K.R.;
"Characterization of cDNA clones for the beta subunit of pyruvate dehydrogenase from Ascaris suum.";
Mol. Biochem. Parasitol. 45:9-17(1991).

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: Tetramer of 2 alpha and 2 beta subunits.
SUBCELLULAR LOCATION: Mitochondrion matrix.

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

M38017; AAA29379.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11177; 1NI4. [HSSP ENTRY / PDB]

ModBase

P26269.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
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.

Other

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

Keywords

Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 27`	`27`	`Mitochondrion.`
`CHAIN`	`28 361`	`334`	`Pyruvate dehydrogenase E1 component subunit beta, mitochondrial.`	`PRO_0000020456`
`BINDING`	`90 90`		`Thiamine pyrophosphate (By similarity).`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 39136 Da [This is the MW of the unprocessed precursor]

CRC64: F04D1C379C28196B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVNGCMRLL RNGLTSACAL EQSVRRLASG TLNVTVRDAL NAALDEEIKR DDRVFLIGEE 

        70         80         90        100        110        120 
VAQYDGAYKI SKGLWKKYGD GRIWDTPITE MAIAGLSVGA AMNGLRPICE FMSMNFSMQG 

       130        140        150        160        170        180 
IDHIINSAAK AHYMSAGRFH VPIVFRGANG AAVGVAQQHS QDFTAWFMHC PGVKVVVPYD 

       190        200        210        220        230        240 
CEDARGLLKA AVRDDNPVIC LENEILYGMK FPVSPEAQSP DFVLPFGQAK IQRPGKDITI 

       250        260        270        280        290        300 
VSLSIGVDVS LHAADELAKS GIDCEVINLR CVRPLDFQTV KDSVIKTKHL VTVESGWPNC 

       310        320        330        340        350        360 
GVGAEISARV TESDAFGYLD GPILRVTGVD VPMPYAQPLE TAALPQPADV VKMVKKCLNV 


Q

P26269 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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