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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Madrid E;
DOI=10.1038/24094; PubMed=9823893 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson S.G.E.,
Zomorodipour A.,
Andersson J.O.,
Sicheritz-Ponten T.,
Alsmark U.C.M.,
Podowski R.M.,
Naeslund A.K.,
Eriksson A.-S.,
Winkler H.H.,
Kurland C.G.;
"The genome sequence of Rickettsia prowazekii and the origin of mitochondria.";
Nature 396:133-140(1998).
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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: 36824 Da [This is the MW of the unprocessed precursor] |
CRC64: BC9A6F66044B213A [This is a checksum on the sequence] |
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10 20 30 40 50 60
MDIKPEKYKP IKEEYIKSFK DMLLLRRFEE KCGQLYGMGK IGGFCHLYIG QEAVISAVAM
70 80 90 100 110 120
IKKKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DIPNKFYGGH
130 140 150 160 170 180
GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMASLW GLPIVYIIEN
190 200 210 220 230 240
NEYSMGTSVA RSTFMCDLYK KGESFGIRGF QLDGMDFEEM YNGTKQVAEY VRENSFPVIL
250 260 270 280 290 300
EVKTYRYRGH SMSDPAKYRS KEEVEKYKER DTLVRIREII LDNKYATEAD LKAIEQSVRE
310 320
IIKVAVEFSE NSPLPAEDEL YTEIYV
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Q9ZDR4 in FASTA format |
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ExPASy Home page
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