Sequence of MVAA_PSEMV

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
hydroxymethylglutaryl-CoA reductase
P13702
Pseudomonas mevalonii
428
45590
Reaction
(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM IENVIGTFEL
 60 PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN GGFTTSSSAP LMHAQVQIVG
120 IQDPLNARLS LLRRKDEIIE LANRKDQLLN SLGGGCRDIE VHTFADTPRG PMLVAHLIVD
180 VRDAMGANTV NTMAEAVAPL MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS
240 GEAVIEGILD AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH
300 YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA QALAEIAVAV
360 GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV DWVARQLVEY HDVRADRAVA
420 LLKQKRGQ
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
57712
Beach M.J.,Rodwell V.W.
Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase.
J. Bacteriol.
171
2994-3001
1989
57713
Wang Y.,Beach M.J.,Rodwell V.W.
(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level.
J. Bacteriol.
171
5567-5571
1989
57714
Wang Y.,Darnay B.G.,Rodwell V.W.
Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
J. Biol. Chem.
265
21634-21641
1990
57715
Darnay B.G.,Wang Y.,Rodwell V.W.
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
J. Biol. Chem.
267
15064-15070
1992
57716
Tabernero L.,Bochar D.A.,Rodwell V.W.,Stauffacher C.V.
Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.
Proc. Natl. Acad. Sci. U.S.A.
96
7167-7171
1999