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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0020076; PubMed=16703114 [NCBI, ExPASy, EBI, Israel, Japan]
Ogata H.,
La Scola B.,
Audic S.,
Renesto P.,
Blanc G.,
Robert C.,
Fournier P.-E.,
Claverie J.-M.,
Raoult D.;
"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens.";
PLoS Genet. 2:733-744(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).
- SUBUNIT: Heterodimer of an alpha and a beta chain.
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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: 326 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36853 Da [This is the MW of the unprocessed precursor] |
CRC64: 36F16A727359D2E1 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MDIKLGKYKP VKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVDM
70 80 90 100 110 120
VKQKEDSMVT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DVPNKFYGGH
130 140 150 160 170 180
GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN
190 200 210 220 230 240
NEYSMGTSVA RSTFMRDLYK KGESFGIKGF QLNGMDFEEM YDGVKQAAEY VRENSMPLIL
250 260 270 280 290 300
EVKTYRYRGH SMSDPAKYRS KEEVETYKER DPITEIRKII LENNYASEAD LKEIEQSVKE
310 320
IVKEAVEFSE NSPLPNEEEL YTQIYV
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Q1RJX4 in FASTA format |
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