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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V.,
Gwilliam R.,
Rajandream M.A.,
Lyne M.H.,
Lyne R.,
Stewart A.,
Sgouros J.G.,
Peat N.,
Hayles J.,
Baker S.G.,
Basham D.,
Bowman S.,
Brooks K.,
Brown D.,
Brown S.,
Chillingworth T.,
Churcher C.M.,
Collins M.,
Connor R., ![]()
Cronin A.,
Davis P.,
Feltwell T.,
Fraser A.,
Gentles S.,
Goble A.,
Hamlin N.,
Harris D.E.,
Hidalgo J.,
Hodgson G.,
Holroyd S.,
Hornsby T.,
Howarth S.,
Huckle E.J.,
Hunt S.,
Jagels K.,
James K.D.,
Jones L.,
Jones M.,
Leather S.,
McDonald S.,
McLean J.,
Mooney P.,
Moule S.,
Mungall K.L.,
Murphy L.D.,
Niblett D.,
Odell C.,
Oliver K.,
O'Neil S.,
Pearson D.,
Quail M.A.,
Rabbinowitsch E.,
Rutherford K.M.,
Rutter S.,
Saunders D.,
Seeger K.,
Sharp S.,
Skelton J.,
Simmonds M.N.,
Squares R.,
Squares S.,
Stevens K.,
Taylor K.,
Taylor R.G.,
Tivey A.,
Walsh S.V.,
Warren T.,
Whitehead S.,
Woodward J.R.,
Volckaert G.,
Aert R.,
Robben J.,
Grymonprez B.,
Weltjens I.,
Vanstreels E.,
Rieger M.,
Schaefer M.,
Mueller-Auer S.,
Gabel C.,
Fuchs M.,
Duesterhoeft A.,
Fritzc C.,
Holzer E.,
Moestl D.,
Hilbert H.,
Borzym K.,
Langer I.,
Beck A.,
Lehrach H.,
Reinhardt R.,
Pohl T.M.,
Eger P.,
Zimmermann W.,
Wedler H.,
Wambutt R.,
Purnelle B.,
Goffeau A.,
Cadieu E.,
Dreano S.,
Gloux S.,
Lelaure V.,
Mottier S.,
Galibert F.,
Aves S.J.,
Xiang Z.,
Hunt C.,
Moore K.,
Hurst S.M.,
Lucas M.,
Rochet M.,
Gaillardin C.,
Tallada V.A.,
Garzon A.,
Thode G.,
Daga R.R.,
Cruzado L.,
Jimenez J.,
Sanchez M.,
del Rey F.,
Benito J.,
Dominguez A.,
Revuelta J.L.,
Moreno S.,
Armstrong J.,
Forsburg S.L.,
Cerutti L.,
Lowe T.,
McCombie W.R.,
Paulsen I.,
Potashkin J.,
Shpakovski G.V.,
Ussery D.,
Barrell B.G.,
Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
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[2]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; TYR-306; SER-310 AND SER-312, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T.,
Villen J.,
Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
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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: 409 AA [This is the length of the unprocessed precursor] |
Molecular weight: 45138 Da [This is the MW of the unprocessed precursor] |
CRC64: 0FAE33765847C185 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MFRTCTKIGT VPKVLVNQKG LIDGLRRVTT DATTSRANPA HVPEEHDKPF PVKLDDSVFE
70 80 90 100 110 120
GYKIDVPSTE IEVTKGELLG LYEKMVTIRR LELACDALYK AKKIRGFCHL SIGQEAVAAG
130 140 150 160 170 180
IEGAITLDDS IITSYRCHGF AYTRGLSIRS IIGELMGRQC GASKGKGGSM HIFAKNFYGG
190 200 210 220 230 240
NGIVGAQIPL GAGIGFAQKY LEKPTTTFAL YGDGASNQGQ AFEAFNMAKL WGLPVIFACE
250 260 270 280 290 300
NNKYGMGTSA ERSSAMTEFY KRGQYIPGLL VNGMDVLAVL QASKFAKKYT VENSQPLLME
310 320 330 340 350 360
FVTYRYGGHS MSDPGTTYRS REEVQKVRAA RDPIEGLKKH IMEWGVANAN ELKNIEKRIR
370 380 390 400
GMVDEEVRIA EESPFPDPIE ESLFSDVYVA GTEPAYARGR NSLEYHQYK
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Q10489 in FASTA format |
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