ID HMDH2_ARATH Reviewed; 562 AA. AC P43256; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 25-NOV-2008, entry version 76. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2; DE Short=HMG-CoA reductase 2; DE Short=HMGR2; DE EC=1.1.1.34; GN Name=HMG2; OrderedLocusNames=At2g17370; ORFNames=F5J6.24; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=94134744; PubMed=8302869; RA Enjuto M., Balcells L., Campos N., Caelles C., Arro M., Boronat A.; RT "Arabidopsis thaliana contains two differentially expressed 3-hydroxy- RT 3-methylglutaryl-CoA reductase genes, which encode microsomal forms of RT the enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 91:927-931(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: Catalyzes the synthesis of mevalonate. The specific CC precursor of all isoprenoid compounds present in plants. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3- CC hydroxy-3-methylglutaryl-CoA + 2 NADPH. CC -!- PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid CC biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Restricted to young seedlings, roots, and CC inflorescences. CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L19262; AAA67317.1; -; Genomic_DNA. DR EMBL; AC002329; AAB86514.1; -; Genomic_DNA. DR EMBL; AY057680; AAL15311.1; -; mRNA. DR EMBL; AY143930; AAN28869.1; -; mRNA. DR PIR; D84551; D84551. DR RefSeq; NP_179329.1; -. DR UniGene; At.432; -. DR HSSP; P04035; 1DQA. DR GeneID; 816244; -. DR GenomeReviews; CT485783_GR; AT2G17370. DR KEGG; ath:AT2G17370; -. DR NMPDR; fig|3702.1.peg.8729; -. DR TAIR; At2g17370; -. DR ArrayExpress; P43256; -. DR GermOnline; AT2G17370; Arabidopsis thaliana. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002202; HMG_CoA_Rdtase_cat. DR InterPro; IPR004554; HMG_CoA_Rdtase_I_cat. DR Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1. DR PANTHER; PTHR10572; HMG-CoA_red; 1. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1. DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Glycoprotein; KW Isoprene biosynthesis; Membrane; NADP; Oxidoreductase; Transmembrane. FT CHAIN 1 562 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase 2. FT /FTId=PRO_0000114434. FT TRANSMEM 32 56 Potential. FT TRANSMEM 77 100 Potential. FT REGION 101 146 Linker (By similarity). FT REGION 147 562 Catalytic (By similarity). FT ACT_SITE 240 240 Charge relay system (By similarity). FT ACT_SITE 372 372 Charge relay system (By similarity). FT ACT_SITE 448 448 Charge relay system (By similarity). FT ACT_SITE 544 544 Proton donor (By similarity). FT CARBOHYD 118 118 N-linked (GlcNAc...) (Potential). FT CARBOHYD 304 304 N-linked (GlcNAc...) (Potential). FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 562 AA; 60715 MW; A4BF6BE6796C940A CRC64; MEDLRRRFPT KKNGEEISNV AVDPPLRKAS DALPLPLYLT NTFFLSLFFA TVYFLLSRWR EKIRNSTPLH VVDLSEICAL IGFVASFIYL LGFCGIDLIF RSSSDDDVWV NDGMIPCNQS LDCREVLPIK PNSVDPPRES ELDSVEDEEI VKLVIDGTIP SYSLETKLGD CKRAAAIRRE AVQRITGKSL TGLPLEGFDY NSILGQCCEM PVGYVQIPVG IAGPLLLDGV EYSVPMATTE GCLVASTNRG FKAIHLSGGA FSVLVKDAMT RAPVVRFPSA RRAALVMFYL QDPSNFERLS LIFNKSSRFA RLQSITCTIA GRNLYPRFAC STGDAMGMNM VSKGVQNVLD FVKSEFPDMD VIGISGNYCS DKKASAVNWI EGRGKHVVCE AFIKAEIVEK VLKTSVEALV ELNTLKNLVG SAMAGSLGGF NAHSSNIVSA VFIATGQDPA QNVESSHCMT MILPDGDDLH ISVSMPCIEV GTVGGGTQLA SQAACLNLLG VKGSNNEKPG SNAQQLARIV AGSVLAGELS LMSAIAAGQL VKSHMKYNRS SRDIGPSSQV NR //