ID   HMDH2_SOLTU             Reviewed;         595 AA.
AC   Q41437;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2;
DE            Short=HMG-CoA reductase 2;
DE            EC=1.1.1.34;
DE   AltName: Full=HMG2.2;
GN   Name=HMG2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kennebec; TISSUE=Tuber;
RX   MEDLINE=97201488; PubMed=9049274; DOI=10.1023/A:1005743011651;
RA   Korth K.L., Stermer B.A., Bhattacharyya M.K., Dixon R.A.;
RT   "HMG-CoA reductase gene families that differentially accumulate
RT   transcripts in potato tubers are developmentally expressed in floral
RT   tissues.";
RL   Plant Mol. Biol. 33:545-551(1997).
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: Expressed in young flowers and in mature
CC       sepals and ovaries.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
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DR   EMBL; U51985; AAB52551.1; -; mRNA.
DR   HSSP; P04035; 1HWI.
DR   BRENDA; 1.1.1.34; 296.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane;
KW   NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    595       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase 2.
FT                                /FTId=PRO_0000114449.
FT   TRANSMEM     48     68       Potential.
FT   TRANSMEM     92    112       Potential.
FT   REGION      113    183       Linker (By similarity).
FT   REGION      184    595       Catalytic (By similarity).
FT   ACT_SITE    278    278       Charge relay system (By similarity).
FT   ACT_SITE    410    410       Charge relay system (By similarity).
FT   ACT_SITE    486    486       Charge relay system (By similarity).
FT   ACT_SITE    584    584       Proton donor (By similarity).
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    121    121       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    342    342       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    455    455       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    588    588       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   595 AA;  63842 MW;  0FA7069849D41D57 CRC64;
     MDVRRRSEKP VYPSKVFGAD EKPLKPHNNQ QQEDNNTLLI DASDALPLPL YLTNGLFFTM
     FFSVMYFLLS RWREKIRNST PLHVVTLSEL GAIVSLIASV IYLLGFFGIG FVQTFVSRGN
     NDSWDENDEE FLLKEDSRCG PATTLGCAIP APPARQISPM APPQPAMSMV EKPSPLITPA
     SSEEDEEIIN SVVQGKFPSY SLVIQLGDVS AAASLRKEVM QRITGKSLEG LPLEGFTYES
     ILGQCCEMPI GYVQIPVGIA GPLLLNGKEF SVPMATTEGC LVASTNRGCK AIYASGGATC
     IVLRDGMTRA PCVRFGTAKR AAELKFFVED PIKFETLANV FNQSSRFGRL QRIQCAIAGK
     NLYMRFVCST GDAMGMNMVS KGVQNVLDYL QNEYPDMDVI GISGNFCSDK KPAAVNWIEG
     RGKSVVCEAI ITEEVVKKVL KTEVAALVEL NMLKNLTGSA MAGALGGFNA HASNIVSAVF
     IATGQDPAQN IESSHCITMM EAVNDGKDLH ISVTMPSIEV GTVGGGTQLA SQSACLNLLG
     VKGANREAPG SNARLLATVV AGSVLAGELS LMSAISAGQL VNSHMKYNRS TKASS
//