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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.
- 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: 331 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36385 Da [This is the MW of the unprocessed precursor] |
CRC64: 8F8C892E9684F733 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSKIFMFDAL RAATDEEMAK DPTVCVIGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE
70 80 90 100 110 120
NSFTGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFT LPLVIRGPGG
130 140 150 160 170 180
VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVVF FEHVLLYNLQ
190 200 210 220 230 240
EEIPQEEYFL PLNKVEFVRK GKDITILTYS RMRHHVIQAL PALLKEGYDP EVIDLISLKP
250 260 270 280 290 300
LDIDSISISV KKTHKVLIVE ECMKTAGIGA ELIAQINEYL FDELDAPVVR LSSQDIPTPY
310 320 330
NGSLEQATVI QPSQIVDSVK SIITSVKAII T
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Q1XDM1 in FASTA format |
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