ID   HMDH_AGRIP              Reviewed;         833 AA.
AC   O76819;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.34;
GN   Name=HMGR;
OS   Agrotis ipsilon (Black cutworm moth).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Noctuinae; Agrotis.
OX   NCBI_TaxID=56364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20428295; PubMed=10971716;
RX   DOI=10.1046/j.1365-2583.2000.00200.x;
RA   Duportets L., Belles X., Rossignol F., Couillaud F.;
RT   "Molecular cloning and structural analysis of 3-hydroxy-3-
RT   methylglutaryl coenzyme A reductase of the moth Agrotis ipsilon.";
RL   Insect Mol. Biol. 9:385-392(2000).
CC   -!- FUNCTION: Synthesis of mevalonate for the production of non-sterol
CC       isoprenoids, which are essential for growth differentiation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-
CC       hydroxy-3-methylglutaryl-CoA + 2 NADPH.
CC   -!- ENZYME REGULATION: The activity of HMG-CoA-reductase is suppressed
CC       by exogenous mevalonate.
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   -!- 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; AJ009675; CAA08775.1; -; mRNA.
DR   HSSP; P04035; 1HWI.
DR   BRENDA; 1.1.1.34; 264922.
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   InterPro; IPR004816; HMG_CoA_Rdtase_I_metazoan.
DR   InterPro; IPR000731; SSD_5TM.
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; TIGR00920; 2A060605; 1.
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.
DR   PROSITE; PS50156; SSD; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane;
KW   NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    833       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114429.
FT   TRANSMEM     10     32       Potential.
FT   TRANSMEM     91    117       Potential.
FT   TRANSMEM    160    180       Potential.
FT   TRANSMEM    301    321       Potential.
FT   REGION      322    419       Linker.
FT   REGION      420    833       Catalytic.
FT   ACT_SITE    504    504       Charge relay system (By similarity).
FT   ACT_SITE    635    635       Charge relay system (By similarity).
FT   ACT_SITE    711    711       Charge relay system (By similarity).
FT   ACT_SITE    809    809       Proton donor (By similarity).
FT   CARBOHYD    680    680       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    715    715       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    720    720       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    813    813       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    825    825       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   833 AA;  89790 MW;  7E9ADD4B4439A035 CRC64;
     MKVWGAHGEF CARHQWEVIV ATLALLACAA SVERNGPGNR SEHCAGWARA CPGLEAEYQA
     ADAVIMTFVR CAALLYAYYQ ISNLHKIASK YLLIIAGVFS TFASFIFTSA VASLFWSELA
     SIKDAPFLFL LVADVARGAR MAKAGWSAGE DQGKRVGRAL ALLGPTATLD TLLAVLLVGV
     GALSGVPRLE HMCTFACLAL LVDYLVFVTF YPACLSLVAD FASGRKEMSP DSPFSEADLK
     PNPVVQRVKM IMAAGLLCVH LTSRWPWSSD NGIIEGPTDT LTPTSNDNIL LHSYVKWFSV
     SADYIVIATL LCALIIKFVF FEEQRNWVID MNDMTVKEVV QEQARSKPKF SVGDDSNSEV
     STQTEGVLED EWPTLSPSSS AAKLNSKKRP MAECLEIYRS EGACVSLSDE EVVMLVEQSH
     IPLHRLEAVL GDPLRGVRLR RKVVGARFQT ELAIKQLPYL NYDYSKVLNA CCENVIGYVG
     VPVGYAGPLV VDGKPYMIPM ATTEGALVAS TNRGAKAIGI RGVTSVVEDV GMTRAPAIKL
     PNVVRAHECR QWIDNKDNYA VIKEAFDSTS RFARLQEIHI GVDGATLYLR FRATTGDAMG
     MNMVSKGAEN ALKLLKNYFP DMEVISLSGN YCSDKKAAAI NWVKGRGKRV VCETTITSDS
     LRTIFKTDAK TLARCNKIKN LSGSALAGSI GGNNAHAANM VTAIYIATGQ DPAQNVTSSN
     CSTNMEVCGE NGEDLYVTCT MPSLEVGTVG GGTILTGQGA CLDILGVKGA GARPAENSAR
     LASLICATVL AGELSLMAAL VNSDLVKSHM RHNRSTVNVQ VQAENITLKV PTL
//