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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC MYA-539 / JBD100;
PubMed=9884236 [NCBI, ExPASy, EBI, Israel, Japan]
Zeeman A.-M.,
Luttik M.A.H.,
Thiele C.,
van Dijken J.P.,
Pronk J.T.,
Steensma H.Y.;
"Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of pyruvate dehydrogenase activity, impairs growth on glucose and triggers aerobic alcoholic fermentation.";
Microbiology 144:3437-3446(1998).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B.,
Sherman D.,
Fischer G.,
Durrens P.,
Casaregola S.,
Lafontaine I.,
de Montigny J.,
Marck C.,
Neuveglise C.,
Talla E.,
Goffard N.,
Frangeul L.,
Aigle M.,
Anthouard V.,
Babour A.,
Barbe V.,
Barnay S.,
Blanchin S.,
Beckerich J.-M., ![]()
Beyne E.,
Bleykasten C.,
Boisrame A.,
Boyer J.,
Cattolico L.,
Confanioleri F.,
de Daruvar A.,
Despons L.,
Fabre E.,
Fairhead C.,
Ferry-Dumazet H.,
Groppi A.,
Hantraye F.,
Hennequin C.,
Jauniaux N.,
Joyet P.,
Kachouri R.,
Kerrest A.,
Koszul R.,
Lemaire M.,
Lesur I.,
Ma L.,
Muller H.,
Nicaud J.-M.,
Nikolski M.,
Oztas S.,
Ozier-Kalogeropoulos O.,
Pellenz S.,
Potier S.,
Richard G.-F.,
Straub M.-L.,
Suleau A.,
Swennen D.,
Tekaia F.,
Wesolowski-Louvel M.,
Westhof E.,
Wirth B.,
Zeniou-Meyer M.,
Zivanovic Y.,
Bolotin-Fukuhara M.,
Thierry A.,
Bouchier C.,
Caudron B.,
Scarpelli C.,
Gaillardin C.,
Weissenbach J.,
Wincker P.,
Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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- 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 (By similarity).
- ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit (By similarity).
- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 412 AA [This is the length of the unprocessed precursor] |
Molecular weight: 45453 Da [This is the MW of the unprocessed precursor] |
CRC64: CBCC8AB3DC4C7E96 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP ETSFEGYLLD
70 80 90 100 110 120
VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR GFCHSSVGQE AIAVGIENAI
130 140 150 160 170 180
TKRDTVITSY RCHGFTYMRG AAVQAVLAEL MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG
190 200 210 220 230 240
AQVPLGAGLA FAHQYKHEDA CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG
250 260 270 280 290 300
MGTAAARSSA MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR
310 320 330 340 350 360
YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY DKAARKYVDE
370 380 390 400 410
QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT WDFAKKSFAF RD
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O13366 in FASTA format |
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