ID   HMDH1_GOSHI             Reviewed;         585 AA.
AC   O64966;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
DE            Short=HMG-CoA reductase 1;
DE            EC=1.1.1.34;
GN   Name=HMG1;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Acala SJ2;
RA   Loguercio L.L., Wilkins T.A.;
RT   "Two genomic clones encoding 3-hydroxy-3-methylglutaryl-coenzyme A
RT   reductase from cotton (Gossypium hirsutum L.).";
RL   (er) Plant Gene Register PGR98-031.
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. Mitochondrion membrane; Multi-pass membrane
CC       protein. Plastid membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
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DR   EMBL; AF038045; AAC05088.1; -; Genomic_DNA.
DR   PIR; T09782; T09782.
DR   HSSP; P04035; 1HWI.
DR   BRENDA; 1.1.1.34; 1857.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane;
KW   Mitochondrion; NADP; Oxidoreductase; Plastid; Transmembrane.
FT   CHAIN         1    585       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase 1.
FT                                /FTId=PRO_0000114438.
FT   TRANSMEM     38     58       Potential.
FT   TRANSMEM     77     97       Potential.
FT   REGION       98    169       Linker (By similarity).
FT   REGION      170    585       Catalytic (By similarity).
FT   ACT_SITE    264    264       Charge relay system (By similarity).
FT   ACT_SITE    396    396       Charge relay system (By similarity).
FT   ACT_SITE    472    472       Charge relay system (By similarity).
FT   ACT_SITE    570    570       Proton donor (By similarity).
FT   CARBOHYD    328    328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    441    441       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    574    574       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   585 AA;  62835 MW;  1350E7A9168EBE42 CRC64;
     METHRRSSTN SIRSHKPARP IALEDDSTKA SDALPLPLYL TNAVFFTLFF SAVYFLLCRW
     REKIRSSTPL HVVTFSEIVA ILASVASFIY LLGFFGIDFV QSLVLRPSAD VWATEDDEVE
     SEVLLRNEDA RHVPCGQALD RSIRSLQPPE PIVTAEKVFD EMPVTVMTEE DEEIIRSVVC
     GMTPSYSLES KLDDCKRAAA IRREALQRIT GKSLSGLPLD GFDYESILGQ CCEMPVGYEQ
     IPVGIAGPLL LNGREYSVPM ATTEGCLVAS TNRGCKAIHL SGGATSVLLR DGMTRAPVVR
     FGTAKRAADL KLYLEDPENF ETLACVFNRS SRFARLQSIK CAIAGKNLYL RFSCFTGDAM
     GMNMVSKGVQ NVLDFLQTDF PDMDVIGISG NFCSDKKPAA VNWIEGRGKS VVCEAIINGD
     VVTKVLKTSV ESLVELNMLK NLTGSAMAGA LGGFNAHASN IVTAVYIATG QDPAQNVESS
     HCITMMEAVN GGKDLHVSVT MPSIEVGTVG GGTQLASQSA CLNLLGVKGA SKESPGANSI
     LLATIVAGAV LAGELSLMSA LAAGQLVKSH MKYNRSSKDV SKVSS
//