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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-613 / Malish 7;
DOI=10.1126/science.1061471; PubMed=11557893 [NCBI, ExPASy, EBI, Israel, Japan]
Ogata H.,
Audic S.,
Renesto-Audiffren P.,
Fournier P.-E.,
Barbe V.,
Samson D.,
Roux V.,
Cossart P.,
Weissenbach J.,
Claverie J.-M.,
Raoult D.;
"Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
Science 293:2093-2098(2001).
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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: 36736 Da [This is the MW of the unprocessed precursor] |
CRC64: BC588D2C9EFFABD9 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MDIKLGKYKP TKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAIDM
70 80 90 100 110 120
VKQKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF NVPNKFYGGH
130 140 150 160 170 180
GIVGAQVPIG TGLAFVEKYN DTHNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN
190 200 210 220 230 240
NEYSMGTSVA RSTFMRDLYK KGASFGIKGF QLDGMDFEEM YDGSKQAAEY VRENSFPLIL
250 260 270 280 290 300
EVKTYRYRGH SMSDPAKYRS KEEVEQYKER DPLVIIRKTI LDNKYVTEAD LKAIEQSVKE
310 320
IVKEAVEFSE NSPLPDEGEL YTQVYC
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Q92IS3 in FASTA format |
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