ID   HMDH2_GOSHI             Reviewed;         628 AA.
AC   O64967;
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 2;
DE            Short=HMG-CoA reductase 2;
DE            EC=1.1.1.34;
GN   Name=HMG2;
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; AF038046; AAC05089.1; -; Genomic_DNA.
DR   PIR; T09785; T09785.
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    628       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase 2.
FT                                /FTId=PRO_0000114439.
FT   TRANSMEM     38     58       Potential.
FT   TRANSMEM     78     98       Potential.
FT   REGION       99    212       Linker (By similarity).
FT   REGION      213    628       Catalytic (By similarity).
FT   ACT_SITE    307    307       Charge relay system (By similarity).
FT   ACT_SITE    439    439       Charge relay system (By similarity).
FT   ACT_SITE    515    515       Charge relay system (By similarity).
FT   ACT_SITE    613    613       Proton donor (By similarity).
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    484    484       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    617    617       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    625    625       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   628 AA;  67603 MW;  BF7704C30EA334F5 CRC64;
     MEASRRSAVK PVIVLKPSKR FPLVEDTPGK ASDALPLPLY LTNAVFFTLF FTVVYFLLSR
     WREKIRASIP LHAVTFPEIV AIFAFVASLI YLLGFFGIDF VQSLIIRPSG DVWSGEDYEE
     ENEVLLHEED ARTVPCGQAL DCSVPSLPHM ARNVTAQRLF DEKPVRVATE EDARKVSCGQ
     AVDCSLHSLP PRPPIVTSQK LFHEKTVIVT TEEDEEIIKS VVAGTLPSYS LESKLGDCKR
     AAAIRREALQ RLTGRSLSGL PLDGFDYESI LGQCCEMPVG YVQIPVGIAG PLLLNGREYS
     VPMATTEGCL VASTNRGCKA IHLSGGATSI LLKDGMTRAP VVRFSTAKRA AELKFYLEDP
     ENFDTLAVVF NRSSRFGRLQ SIKCAIAGKN LYLRFTCSTG DAMGMNMVSK GVQNVLDFLQ
     TDFPDMDVIG ISGNFCSDKK PAAVNWIEGR GKSVVCEAII EGDVVRKVLK TSVESLVELN
     MLKNLTGSAM AGALGGFNAH ASNIVTAIYI ATGQDPAQNV ESSHCITMME AVNDGKDLHI
     SVTMPSIEVG TVGGGTQLAS QSACLNLLGV KGASKDVAGA NSRMLATIVT GAVLAGELSL
     MSALAAGQLV KSHMKYNRSS KDMSNLSS
//