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Sequence of ACNB_ECOLI

EC Number:4.2.1.3

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
aconitate hydratase
P36683
Escherichia coli (strain K12)
865
93498
Reaction
citrate = cis-aconitate + H2O
Other sequences found for EC No. 4.2.1.3

EC Number:4.2.1.99

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2-methylisocitrate dehydratase
P36683
Escherichia coli (strain K12)
865
93498
Reaction
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
Other sequences found for EC No. 4.2.1.99

General information:

Sequence
show sequence in fasta format
  0 MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA
 60 AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS
120 HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD
180 DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV
240 GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
300 LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA
360 LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM
420 TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH
480 SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM
540 QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
600 ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA
660 DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA
720 GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA
780 DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT
840 YRYLNFNQLS QYTEKADGVI FQTAV
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1025726
Fujita N.,Mori H.,Yura T.,Ishihama A.
Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region.
Nucleic Acids Res.
22
1637-1639
1994
1025727
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
1025728
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
1025729
Bradbury A.J.,Gruer M.J.,Rudd K.E.,Guest J.R.
The second aconitase (AcnB) of Escherichia coli.
Microbiology
142
389-400
1996
1025730
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
1025731
Brock M.,Maerker C.,Schuetz A.,Voelker U.,Buckel W.
Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase.
Eur. J. Biochem.
269
6184-6194
2002
1025732
Jordan P.A.,Tang Y.,Bradbury A.J.,Thomson A.J.,Guest J.R.
Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB).
Biochem. J.
344
739-746
1999
1025733
Gruer M.J.,Guest J.R.
Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli.
Microbiology
140
2531-2541
1994
1025734
Gruer M.J.,Bradbury A.J.,Guest J.R.
Construction and properties of aconitase mutants of Escherichia coli.
Microbiology
143
1837-1846
1997
1025735
Tang Y.,Guest J.R.
Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases.
Microbiology
145
3069-3079
1999
1025736
Tang Y.,Quail M.A.,Artymiuk P.J.,Guest J.R.,Green J.
Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression.
Microbiology
148
1027-1037
2002
1025737
Tang Y.,Guest J.R.,Artymiuk P.J.,Green J.
Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation.
Mol. Microbiol.
56
1149-1158
2005
1025738
Williams C.H. Jr.,Stillman T.J.,Barynin V.V.,Sedelnikova S.E.,Tang Y.,Green J.,Guest J.R.,Artymiuk P.J.
E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition.
Nat. Struct. Biol.
9
447-452
2002