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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-1525 / URRWXCal2;
DOI=10.1371/journal.pbio.0030248; PubMed=15984913 [NCBI, ExPASy, EBI, Israel, Japan]
Ogata H.,
Renesto P.,
Audic S.,
Robert C.,
Blanc G.,
Fournier P.-E.,
Parinello H.,
Claverie J.-M.,
Raoult D.;
"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite.";
PLoS Biol. 3:1-12(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: 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: 36724 Da [This is the MW of the unprocessed precursor] |
CRC64: DFD9E71813DC1E81 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MDIKPKKYKP TKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVDT
70 80 90 100 110 120
VKQKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DIPNKFYGGH
130 140 150 160 170 180
GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN
190 200 210 220 230 240
NEYSMGTSVA RSTFMRDLYK KGESFGIKGF QLDGMDFEEM YNGAKQAAEY VRENSFPLIL
250 260 270 280 290 300
EVKTYRYRGH SMSDPAKYRS KEEVEQYKER DPLVIIRKTI LDNKYATEAD LKEIEQSVKE
310 320
IVKEAVKFSE NSPLPDEGEL YTEVYC
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Q4UKQ6 in FASTA format |
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