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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L.,
Pachebat J.A.,
Gloeckner G.,
Rajandream M.A.,
Sucgang R.,
Berriman M.,
Song J.,
Olsen R.,
Szafranski K.,
Xu Q.,
Tunggal B.,
Kummerfeld S.,
Madera M.,
Konfortov B.A.,
Rivero F.,
Bankier A.T.,
Lehmann R.,
Hamlin N.,
Davies R., ![]()
Gaudet P.,
Fey P.,
Pilcher K.,
Chen G.,
Saunders D.,
Sodergren E.J.,
Davis P.,
Kerhornou A.,
Nie X.,
Hall N.,
Anjard C.,
Hemphill L.,
Bason N.,
Farbrother P.,
Desany B.,
Just E.,
Morio T.,
Rost R.,
Churcher C.M.,
Cooper J.,
Haydock S.,
van Driessche N.,
Cronin A.,
Goodhead I.,
Muzny D.M.,
Mourier T.,
Pain A.,
Lu M.,
Harper D.,
Lindsay R.,
Hauser H.,
James K.D.,
Quiles M.,
Madan Babu M.,
Saito T.,
Buchrieser C.,
Wardroper A.,
Felder M.,
Thangavelu M.,
Johnson D.,
Knights A.,
Loulseged H.,
Mungall K.L.,
Oliver K.,
Price C.,
Quail M.A.,
Urushihara H.,
Hernandez J.,
Rabbinowitsch E.,
Steffen D.,
Sanders M.,
Ma J.,
Kohara Y.,
Sharp S.,
Simmonds M.N.,
Spiegler S.,
Tivey A.,
Sugano S.,
White B.,
Walker D.,
Woodward J.R.,
Winckler T.,
Tanaka Y.,
Shaulsky G.,
Schleicher M.,
Weinstock G.M.,
Rosenthal A.,
Cox E.C.,
Chisholm R.L.,
Gibbs R.A.,
Loomis W.F.,
Platzer M.,
Kay R.R.,
Williams J.G.,
Dear P.H.,
Noegel A.A.,
Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
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[2]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600113-MCP200; PubMed=16926386 [NCBI, ExPASy, EBI, Israel, Japan]
Gotthardt D.,
Blancheteau V.,
Bosserhoff A.,
Ruppert T.,
Delorenzi M.,
Soldati T.;
"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake.";
Mol. Cell. Proteomics 5:2228-2243(2006).
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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) (By similarity).
- 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: 377 AA [This is the length of the unprocessed precursor] |
Molecular weight: 41988 Da [This is the MW of the unprocessed precursor] |
CRC64: BD3481894B7348C3 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLSNFLKVNS KALGHIRTFA SKSGEIKHNF KKADTYLCDG PSDSTVTNKD ELISFFTEMS
70 80 90 100 110 120
RFRRLETVCD GLYKKKLIRG FCHLYTGQEA VCAGLESAIT KDDHIITAYR DHTYMLSRGA
130 140 150 160 170 180
TPEEIFAELL MKETGCSKGK GGSMHMFTKN FYGGNGIVGA QCPLGAGIAF AQKYNKTGNV
190 200 210 220 230 240
CLAMYGDGAA NQGQLFEAFN MASLWKLPVI FICENNKYGM GTSQKRSTAG HDFYTRGHYV
250 260 270 280 290 300
AGLKVDGMDV FAVKEAGKYA AEWCRAGNGP IILEMDTYRY VGHSMSDPGI TYRTREEVNH
310 320 330 340 350 360
VRQTRDPIEN IRQIILDNKI ATEDQLAAIE ETVRDEMEKA SEKAIAAPLP QARELFTNVY
370
LQEVPVRGVE FVNSFKP
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Q54C70 in FASTA format |
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