Sequence of ODP2_ECOLI
EC Number:1.2.1.104
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH
Other sequences found for EC No. 1.2.1.104
EC Number:1.3.1.12
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+
Other sequences found for EC No. 1.3.1.12
EC Number:2.3.1.12
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
dihydrolipoyllysine-residue acetyltransferase
P06959
Escherichia coli (strain K12)
630
66096
Reaction
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
Other sequences found for EC No. 2.3.1.12
General information:
Sequence
0 MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
60 VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV
120 TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA
180 GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT
240 VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
300 AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED
360 VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
420 VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS
480 LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA
540 GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
600 FDHRVIDGAD GARFITIINN TLSDIRRLVM
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1094434
Stephens P.E.,Darlison M.G.,Lewis H.M.,Guest J.R.
The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component.
Eur. J. Biochem.
133
481-489
1983
1094435
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
1094436
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
1094437
Link A.J.,Robison K.,Church G.M.
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Electrophoresis
18
1259-1313
1997
1094438
Hale G.,Perham R.N.
Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
Biochem. J.
187
905-908
1980
1094439
Russel G.C.,Guest J.R.
Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue.
Biochem. J.
269
443-450
1990
1094440
Ali S.T.,Guest J.R.
Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli.
Biochem. J.
271
139-145
1990
1094441
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
1094442
Zhang J.,Sprung R.,Pei J.,Tan X.,Kim S.,Zhu H.,Liu C.F.,Grishin N.V.,Zhao Y.
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Mol. Cell. Proteomics
8
215-225
2009
