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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature00847; PubMed=12097910 [NCBI, ExPASy, EBI, Israel, Japan]
Gloeckner G.,
Eichinger L.,
Szafranski K.,
Pachebat J.A.,
Bankier A.T.,
Dear P.H.,
Lehmann R.,
Baumgart C.,
Parra G.,
Abril J.F.,
Guigo R.,
Kumpf K.,
Tunggal B.,
Cox E.C.,
Quail M.A.,
Platzer M.,
Rosenthal A.,
Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
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[2]
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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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- 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: Tetramer of 2 alpha and 2 beta subunits (By similarity).
- SUBCELLULAR LOCATION: Mitochondrion matrix.
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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: 356 AA [This is the length of the unprocessed precursor] |
Molecular weight: 39068 Da [This is the MW of the unprocessed precursor] |
CRC64: A259CB6753D1FF3C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLSSILKKIQ PSLLVNFRII TRTYATKEVT VRDAINSALD EELARDEKVF IMGEEVAQYN
70 80 90 100 110 120
GAYKITKGLF DKYGGDRIID TPITEAGFAG IGVGAAMAGT RPIIEFMTFN FAMQAIDHII
130 140 150 160 170 180
NSSAKTHYMS GGKVFNPIVW RGPNGPPTAV GAQHSQCFAA WYGSVPGLKV VAPWSAADHR
190 200 210 220 230 240
GLLKSAIRDD NPVVYLESEL LYNYKFDLSD QEQDKEYLVP IGKAKVEREG KDVTIVGFSR
250 260 270 280 290 300
IVSNCMEAAE ILAKEGISAE VINLRTIRPI DAETIVNSLK KTNKLVTVEE GWAQSGIGAE
310 320 330 340 350
ISALMMEHAF DYLDAPIERI CGADVPMPYA SNLENAAMVQ TQNIVNAAKR VTQRNK
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Q86HX0 in FASTA format |
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