NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8021225 [NCBI, ExPASy, EBI, Israel, Japan]
Hein S., Steinbuechel A.;
"Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase.";
J. Bacteriol. 176:4394-4408(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1244; PubMed=16964242 [NCBI, ExPASy, EBI, Israel, Japan]
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).

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) (By similarity).
CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
SUBUNIT: Homodimer (By similarity).

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

U09865; AAA21598.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM260479; CAJ92510.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55514; A55514.

RefSeq

YP_725878.1; -.

3D structure databases

HSSP

P06958; 1L8A. [HSSP ENTRY / PDB]

ModBase

Q59097.

Family and domain databases

InterPro

IPR004660; 2-oxoA_DHase_E1.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.920; Transketo_C_like; 1.

Pfam

PF00456; Transketolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000156; Pyruvate_dh_E1; 1.

TIGRFAMs

TIGR00759; aceE; 1.

BLOCKS

Q59097.

Genome annotation databases

GeneID

4250135; -.

GenomeReviews

AM260479_GR; H16_A1374.

KEGG

reh:H16_A1374; -.

Phylogenomic databases

HOGENOM

Q59097; -.

Genome annotation databases

CMR

Q59097; H16_A1374.

Other

ProtoNet

Q59097.

UniRef

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

Keywords

Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 895`	`895`		`Pyruvate dehydrogenase E1 component.`	`PRO_0000162238`

Sequence information

Length: 895 AA [This is the length of the unprocessed precursor]

Molecular weight: 100365 Da [This is the MW of the unprocessed precursor]

CRC64: 522A9A3C43454051 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAVPEQILG ASSANDADPQ ETHEWLDALQ GVLAAEGPAR AAFLIDKQIE YARVNGVTQP 

        70         80         90        100        110        120 
FHAETQYINT IPVEQQARIP GDQDIEHRIR SYTRWNAMAM VLRANKHTNV GGHISSFASA 

       130        140        150        160        170        180 
ATLYDVGYNH FWRAPSEAGG GDLVFVQGHS APGVYSRAFL LGRLTQDQLD NFRQEVDGKG 

       190        200        210        220        230        240 
ISSYPHPWLM PDFWQFPTVS MGLGPIMAIY QARFMKYLDS RGLAKAGDRK VWAFLGDGET 

       250        260        270        280        290        300 
DEPESLGAIG MAGREKLDNL VFVINCNLQR LDGPVRGNGK IIQELESEFR GAGWNVIKVV 

       310        320        330        340        350        360 
WGSKWDSLLA RDTKGLLMKR MMECVDGEYQ TMKAKDGAYV REHFFNTPEL KAMVADWSDD 

       370        380        390        400        410        420 
DIWRLNRGGH DPHKIYAAYK AASEHKGQPT LILAKTIKGY GMGDAGQAMN VAHQQKKMPV 

       430        440        450        460        470        480 
DAIRKFRDQF NLPVADDQLE EVPYITFPEG SKELEYMRQA RQNLGGYLPA RRQKAEALPV 

       490        500        510        520        530        540 
PQLSAFDALL KATGEGREVS TTMAFVRILN TLLKDKQIGK HVVPIVPDES RTFGMEGLFR 

       550        560        570        580        590        600 
QVGIWNQEGQ KYVPEDHDQL MFYKESQTGQ VLQEGINEAG AMCDWIAAAT SYSTHGVQMI 

       610        620        630        640        650        660 
PFYIYYSMFG IQRIGDLCWA AADMRSRGFL LGGTAGRTTL NGEGLQHEDG HSHVFHAAIP 

       670        680        690        700        710        720 
NCISYDPTFQ YELAVVMQDG LRRMYAEQED VYYYLTVMNE NYEHPEMPAG VEQDIVKGMY 

       730        740        750        760        770        780 
QFRKGVENSN APRVQLLGSG TIFREVIAAA DLLKKDWGVE SDLWGCPSFT ELAREGHDVE 

       790        800        810        820        830        840 
RFNLLHPTET PRESHVAKSL KSARGPVIAS TDYVRAFAEQ IRPFVPRRYV VLGTDGFGRS 

       850        860        870        880        890 
DTREKLRHFF EVDRYWVTLA ALKALADEGA IGRDKVAEAI KKYNLDPNKP NPMSV

Q59097 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