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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SAG 48.80;
DOI=10.1186/1741-7007-5-2; PubMed=17222354 [NCBI, ExPASy, EBI, Israel, Japan]
Lemieux C.,
Otis C.,
Turmel M.;
"A clade uniting the green algae Mesostigma viride and Chlorokybus atmophyticus represents the deepest branch of the Streptophyta in chloroplast genome-based phylogenies.";
BMC Biol. 5:2-2(2007).
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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: Heterodimer of an alpha and a beta chain (By similarity).
- SUBCELLULAR LOCATION: Plastid, chloroplast.
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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: 335 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36680 Da [This is the MW of the unprocessed precursor] |
CRC64: E846941B42AF42AF [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAVRFLFEAL QKAIDEEMER EKRVVLIGED IGHYGGSYKV TQGLYGKYGK HRVIDTPIAE
70 80 90 100 110 120
YSFVGAAVGA AATGLIPVVE GMNMAFILLA YSQISNNMGM LCATSGGHFQ VPMVLRGPGG
130 140 150 160 170 180
IGKQLGAEHS QRLESYFQSV PGLQIVTCST PYNAKGLLKS AIRSKNPILF IEHVLLYNLK
190 200 210 220 230 240
GEVPDNDYLL PLEKAELVRE GSDITVLTYS RQRYNVIQAV KVLVEEGYDP EVIDLISLKP
250 260 270 280 290 300
FDMETIGKSI QKTHKVLIVE ECMMTGGISN VLQSLIIDNF FDALDAAPLI LSSPNVPTPY
310 320 330
TGPLEEATVV QTIDIIESIE YGITGKPPKP RTAKK
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A2CI50 in FASTA format |
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