Sequence of ACEA_MYCTU
EC Number:4.1.3.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
isocitrate = succinate + glyoxylate
Other sequences found for EC No. 4.1.3.1
EC Number:4.1.3.30
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Methylisocitrate lyase
P9WKK7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
428
47087
Reaction
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = succinate + pyruvate
Other sequences found for EC No. 4.1.3.30
General information:
Sequence
0 MSVVGTPKSA EQIQQEWDTN PRWKDVTRTY SAEDVVALQG SVVEEHTLAR RGAEVLWEQL
60 HDLEWVNALG ALTGNMAVQQ VRAGLKAIYL SGWQVAGDAN LSGHTYPDQS LYPANSVPQV
120 VRRINNALQR ADQIAKIEGD TSVENWLAPI VADGEAGFGG ALNVYELQKA LIAAGVAGSH
180 WEDQLASEKK CGHLGGKVLI PTQQHIRTLT SARLAADVAD VPTVVIARTD AEAATLITSD
240 VDERDQPFIT GERTREGFYR TKNGIEPCIA RAKAYAPFAD LIWMETGTPD LEAARQFSEA
300 VKAEYPDQML AYNCSPSFNW KKHLDDATIA KFQKELAAMG FKFQFITLAG FHALNYSMFD
360 LAYGYAQNQM SAYVELQERE FAAEERGYTA TKHQREVGAG YFDRIATTVD PNSSTTALTG
420 STEEGQFH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
386157
Cole S.T.,Brosch R.,Parkhill J.,Garnier T.,Churcher C.M.,Harris D.E.,Gordon S.V.,Eiglmeier K.,Gas S.,Barry C.E. III,Tekaia F.,Badcock K.,Basham D.,Brown D.,Chillingworth T.,Connor R.,Davies R.M.,Devlin K.,Feltwell T.,Gentles S.,Hamlin N.,Holroyd S.,Hornsby T.,Jagels K.,Krogh A.,McLean J.,Moule S.,Murphy L.D.,Oliver S.,Osborne J.,Quail M.A.,Rajandream M.A.,Rogers J.,Rutter S.,Seeger K.,Skelton S.,Squares S.,Squares R.,Sulston J.E.,Taylor K.,Whitehead S.,Barrell B.G.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature
393
537-544
1998
386158
McKinney J.D.,Honer zu Bentrup K.,Munoz-Elias E.J.,Miczak A.,Chen B.,Chan W.T.,Swenson D.,Sacchettini J.C.,Jacobs W.R. Jr.,Russell D.G.
Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase.
Nature
406
735-738
2000
386159
Kumar R.,Bhakuni V.
Mycobacterium tuberculosis isocitrate lyase (MtbIcl): role of divalent cations in modulation of functional and structural properties.
Proteins
72
892-900
2008
386160
Festa R.A.,McAllister F.,Pearce M.J.,Mintseris J.,Burns K.E.,Gygi S.P.,Darwin K.H.
Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis.
PLoS ONE
5
0-0
2010
386161
Kelkar D.S.,Kumar D.,Kumar P.,Balakrishnan L.,Muthusamy B.,Yadav A.K.,Shrivastava P.,Marimuthu A.,Anand S.,Sundaram H.,Kingsbury R.,Harsha H.C.,Nair B.,Prasad T.S.,Chauhan D.S.,Katoch K.,Katoch V.M.,Kumar P.,Chaerkady R.,Ramachandran S.,Dash D.,Pandey A.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol. Cell. Proteomics
10
0-0
2011
386162
Moynihan M.M.,Murkin A.S.
Cysteine is the general base that serves in catalysis by isocitrate lyase and in mechanism-based inhibition by 3-nitropropionate.
Biochemistry
53
178-187
2014
386163
Sharma V.,Sharma S.,zu Bentrup K.H.,McKinney J.D.,Russell D.G.,Jacobs W.R. Jr.,Sacchettini J.C.
Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis.
Nat. Struct. Biol.
7
663-668
2000
386164
Micklinghoff J.C.,Breitinger K.J.,Schmidt M.,Geffers R.,Eikmanns B.J.,Bange F.C.
Role of the transcriptional regulator RamB (Rv0465c) in the control of the glyoxylate cycle in Mycobacterium tuberculosis.
J. Bacteriol.
191
7260-7269
2009
386165
Masiewicz P.,Brzostek A.,Wolanski M.,Dziadek J.,Zakrzewska-Czerwinska J.
A novel role of the PrpR as a transcription factor involved in the regulation of methylcitrate pathway in Mycobacterium tuberculosis.
PLoS ONE
7
0-0
2012
