Sequence of HMDH2_ARATH

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
hydroxymethylglutaryl-CoA reductase (NADPH)
P43256
Arabidopsis thaliana
562
60715
Reaction
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MEDLRRRFPT KKNGEEISNV AVDPPLRKAS DALPLPLYLT NTFFLSLFFA TVYFLLSRWR
 60 EKIRNSTPLH VVDLSEICAL IGFVASFIYL LGFCGIDLIF RSSSDDDVWV NDGMIPCNQS
120 LDCREVLPIK PNSVDPPRES ELDSVEDEEI VKLVIDGTIP SYSLETKLGD CKRAAAIRRE
180 AVQRITGKSL TGLPLEGFDY NSILGQCCEM PVGYVQIPVG IAGPLLLDGV EYSVPMATTE
240 GCLVASTNRG FKAIHLSGGA FSVLVKDAMT RAPVVRFPSA RRAALVMFYL QDPSNFERLS
300 LIFNKSSRFA RLQSITCTIA GRNLYPRFAC STGDAMGMNM VSKGVQNVLD FVKSEFPDMD
360 VIGISGNYCS DKKASAVNWI EGRGKHVVCE AFIKAEIVEK VLKTSVEALV ELNTLKNLVG
420 SAMAGSLGGF NAHSSNIVSA VFIATGQDPA QNVESSHCMT MILPDGDDLH ISVSMPCIEV
480 GTVGGGTQLA SQAACLNLLG VKGSNNEKPG SNAQQLARIV AGSVLAGELS LMSAIAAGQL
540 VKSHMKYNRS SRDIGPSSQV NR
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
293317
Enjuto M.,Balcells L.,Campos N.,Caelles C.,Arro M.,Boronat A.
Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme.
Proc. Natl. Acad. Sci. U.S.A.
91
927-931
1994
293318
Lin X.,Kaul S.,Rounsley S.D.,Shea T.P.,Benito M.-I.,Town C.D.,Fujii C.Y.,Mason T.M.,Bowman C.L.,Barnstead M.E.,Feldblyum T.V.,Buell C.R.,Ketchum K.A.,Lee J.J.,Ronning C.M.,Koo H.L.,Moffat K.S.,Cronin L.A.,Shen M.,Pai G.,Van Aken S.,Umayam L.,Tallon L.J.,Gill J.E.,Adams M.D.,Carrera A.J.,Creasy T.H.,Goodman H.M.,Somerville C.R.,Copenhaver G.P.,Preuss D.,Nierman W.C.,White O.,Eisen J.A.,Salzberg S.L.,Fraser C.M.,Venter J.C.
Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.
Nature
402
761-768
1999
293319
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
293320
Yamada K.,Lim J.,Dale J.M.,Chen H.,Shinn P.,Palm C.J.,Southwick A.M.,Wu H.C.,Kim C.J.,Nguyen M.,Pham P.K.,Cheuk R.F.,Karlin-Newmann G.,Liu S.X.,Lam B.,Sakano H.,Wu T.,Yu G.,Miranda M.,Quach H.L.,Tripp M.,Chang C.H.,Lee J.M.,Toriumi M.J.,Chan M.M.,Tang C.C.,Onodera C.S.,Deng J.M.,Akiyama K.,Ansari Y.,Arakawa T.,Banh J.,Banno F.,Bowser L.,Brooks S.Y.,Carninci P.,Chao Q.,Choy N.,Enju A.,Goldsmith A.D.,Gurjal M.,Hansen N.F.,Hayashizaki Y.,Johnson-Hopson C.,Hsuan V.W.,Iida K.,Karnes M.,Khan S.,Koesema E.,Ishida J.,Jiang P.X.,Jones T.,Kawai J.,Kamiya A.,Meyers C.,Nakajima M.,Narusaka M.,Seki M.,Sakurai T.,Satou M.,Tamse R.,Vaysberg M.,Wallender E.K.,Wong C.,Yamamura Y.,Yuan S.,Shinozaki K.,Davis R.W.,Theologis A.,Ecker J.R.
Empirical analysis of transcriptional activity in the Arabidopsis genome.
Science
302
842-846
2003
293321
Enjuto M.,Lumbreras V.,Marin C.,Boronat A.
Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues.
Plant Cell
7
517-527
1995
293322
Suzuki M.,Kamide Y.,Nagata N.,Seki H.,Ohyama K.,Kato H.,Masuda K.,Sato S.,Kato T.,Tabata S.,Yoshida S.,Muranaka T.
Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels.
Plant J.
37
750-761
2004
293323
Ohyama K.,Suzuki M.,Masuda K.,Yoshida S.,Muranaka T.
Chemical phenotypes of the hmg1 and hmg2 mutants of Arabidopsis demonstrate the in-planta role of HMG-CoA reductase in triterpene biosynthesis.
Chem. Pharm. Bull.
55
1518-1521
2007
293324
Suzuki M.,Nakagawa S.,Kamide Y.,Kobayashi K.,Ohyama K.,Hashinokuchi H.,Kiuchi R.,Saito K.,Muranaka T.,Nagata N.
Complete blockage of the mevalonate pathway results in male gametophyte lethality.
J. Exp. Bot.
60
2055-2064
2009
293325
Nieto B.,Fores O.,Arro M.,Ferrer A.
Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways.
Phytochemistry
70
53-59
2009