Sequence of MABA_MYCTU
EC Number:1.1.1.36
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
acetoacetyl-CoA reductase
P9WGT3
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
247
25697
Reaction
(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
Other sequences found for EC No. 1.1.1.36
EC Number:1.1.1.100
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-oxoacyl-[acyl-carrier-protein] reductase
P9WGT3
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
247
25697
Reaction
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
Other sequences found for EC No. 1.1.1.100
General information:
Sequence
0 MTATATEGAK PPFVSRSVLV TGGNRGIGLA IAQRLAADGH KVAVTHRGSG APKGLFGVEC
60 DVTDSDAVDR AFTAVEEHQG PVEVLVSNAG LSADAFLMRM TEEKFEKVIN ANLTGAFRVA
120 QRASRSMQRN KFGRMIFIGS VSGSWGIGNQ ANYAASKAGV IGMARSIARE LSKANVTANV
180 VAPGYIDTDM TRALDERIQQ GALQFIPAKR VGTPAEVAGV VSFLASEDAS YISGAVIPVD
240 GGMGMGH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
694007
Banerjee A.,Sugantino M.,Sacchettini J.C.,Jacobs W.R. Jr.
The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance.
Microbiology
144
2697-2704
1998
694008
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
694009
Marrakchi H.,Ducasse S.,Labesse G.,Montrozier H.,Margeat E.,Emorine L.,Charpentier X.,Daffe M.,Quemard A.
MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II.
Microbiology
148
951-960
2002
694010
Ducasse-Cabanot S.,Cohen-Gonsaud M.,Marrakchi H.,Nguyen M.,Zerbib D.,Bernadou J.,Daffe M.,Labesse G.,Quemard A.
In vitro inhibition of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA by isoniazid.
Antimicrob. Agents Chemother.
48
242-249
2004
694011
Silva R.G.,de Carvalho L.P.,Blanchard J.S.,Santos D.S.,Basso L.A.
Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein (ACP) reductase: kinetic and chemical mechanisms.
Biochemistry
45
13064-13073
2006
694012
Silva R.G.,Rosado L.A.,Santos D.S.,Basso L.A.
Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding.
Arch. Biochem. Biophys.
471
1-10
2008
694013
Gurvitz A.
The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2.
Mol. Genet. Genomics
282
407-416
2009
694014
Veyron-Churlet R.,Zanella-Cleon I.,Cohen-Gonsaud M.,Molle V.,Kremer L.
Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis.
J. Biol. Chem.
285
12714-12725
2010
694015
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
694016
Rosado L.A.,Caceres R.A.,de Azevedo W.F. Jr.,Basso L.A.,Santos D.S.
Role of Serine140 in the mode of action of Mycobacterium tuberculosis beta-ketoacyl-ACP Reductase (MabA).
BMC Res. Notes
5
526-526
2012
694017
Cohen-Gonsaud M.,Ducasse S.,Hoh F.,Zerbib D.,Labesse G.,Quemard A.
Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.
J. Mol. Biol.
320
249-261
2002
694018
Cohen-Gonsaud M.,Ducasse-Cabanot S.,Quemard A.,Labesse G.
Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change.
Proteins
60
392-400
2005
694019
Poncet-Montange G.,Ducasse-Cabanot S.,Quemard A.,Labesse G.,Cohen-Gonsaud M.
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
Acta Crystallogr. D
63
923-925
2007
