ID   HMDH1_SOLTU             Reviewed;         596 AA.
AC   P48020;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
DE            Short=HMG-CoA reductase 1;
DE            Short=HMGR1;
DE            Short=HMGR;
DE            EC=1.1.1.34;
GN   Name=HMG1;
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=93144952; PubMed=1283354; DOI=10.1105/tpc.4.10.1333;
RA   Choi D., Ward B.L., Bostock R.M.;
RT   "Differential induction and suppression of potato 3-hydroxy-3-
RT   methylglutaryl coenzyme A reductase genes in response to Phytophthora
RT   infestans and to its elicitor arachidonic acid.";
RL   Plant Cell 4:1333-1344(1992).
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 flower primordia and anthers.
CC   -!- INDUCTION: Induced by wounding. This enhancement is greatly
CC       reduced by treatment with arachidonic acid or after innoculation
CC       with the fungal pathogen, P.infestans.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
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DR   EMBL; L01400; AAA93498.1; -; mRNA.
DR   PIR; S59944; S59944.
DR   HSSP; P04035; 1DQA.
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; FALSE_NEG.
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    596       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase 1.
FT                                /FTId=PRO_0000114448.
FT   TRANSMEM     41     61       Potential.
FT   TRANSMEM     83    103       Potential.
FT   REGION      104    183       Linker (By similarity).
FT   REGION      184    596       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    342    342       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    455    455       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    588    588       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   596 AA;  63917 MW;  4E7060D3ADC6EE60 CRC64;
     MDVRRRPVKP LYTSKDASAG EPLKQQEVSS PKASDALPLP LYLTNGLFFT MFFSVMYFLL
     VRWREKIRNS IPLHVVTLSE LLAMVSLIAS VIYLLGFFGI GFVQSFVSRS NSDSWDIEDE
     NAEQLIIEED SRRGPCAAAT TLGCVVPPPP VRKIAPMVPQ QPAKVALSQT EKPSPIIMPA
     LSEDDEEIIQ SVVQGKTPSY SLESKLGDCM RAASIRKEAL QRITGKSLEG LPLEGFDYSS
     ILGQCCEMPV GYVQIPVGIA GPLLLDGREY SVPMATTEGC LVASTNRGCK AIFVSGGADS
     VLLRDGMTRA PVVRFTTAKR AAELKFFVED PLNFETLSLM FNKSSRFARL QGIQCAIAGK
     NLYITFSCST GDAMGMNMVS KGVQNVLDYL QSEYPDMDVI GISGNFCSDK KPAAVNWIEG
     RGKSVVCEAI IKEEVVKKVL KTEVAALVEL NMLKNLTGSA MAGALGGFNA HASNIVSAVY
     LATGQDPAQN VESSHCITMM EAVNDGKDLH VSVTMPSIEV GTVGGGTQLA SQSACLNLLG
     VKGANRDAPG SNARLLATIV AGSVLAGELS LMSAISAGQL VKSHMKYNRS IKDISK
//