ID   HMDH_BLAGE              Reviewed;         856 AA.
AC   P54960;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.34;
OS   Blattella germanica (German cockroach).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Orthopteroidea; Dictyoptera; Blattaria; Blattellidae;
OC   Blattellinae; Blattella.
OX   NCBI_TaxID=6973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93238692; PubMed=8477698;
RA   Martinez-Gonzalez J., Buesa C., Piulachs M.D., Belles X.,
RA   Hegardt F.G.;
RT   "Molecular cloning, developmental pattern and tissue expression of 3-
RT   hydroxy-3-methylglutaryl coenzyme A reductase of the cockroach
RT   Blattella germanica.";
RL   Eur. J. Biochem. 213:233-241(1993).
CC   -!- FUNCTION: Synthesis of mevalonate for the production of non-sterol
CC       isoprenoids, which are essential for growth differentiation.
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.
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DR   EMBL; X70034; CAA49628.1; -; mRNA.
DR   PIR; S30338; S30338.
DR   HSSP; P04035; 1DQA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
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   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    856       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114430.
FT   TRANSMEM     12     32       Potential.
FT   TRANSMEM     89    109       Potential.
FT   TRANSMEM    123    143       Potential.
FT   TRANSMEM    190    210       Potential.
FT   TRANSMEM    344    364       Potential.
FT   REGION      365    443       Linker.
FT   REGION      443    771       Catalytic.
FT   ACT_SITE    528    528       Charge relay system (By similarity).
FT   ACT_SITE    659    659       Charge relay system (By similarity).
FT   ACT_SITE    735    735       Charge relay system (By similarity).
FT   ACT_SITE    834    834       Proton donor (By similarity).
FT   CARBOHYD    326    326       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    412    412       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    700    700       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    838    838       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   856 AA;  93157 MW;  833273836FC55AAA CRC64;
     MVGRLFRAHG QFCASHPWEV IVATLTLTVC MLTVDQRPLG LPPGWGHNCI TLEEYNAADM
     IVMTLIRCVA VLYSYYQFCH LQKLGSKYIL GIAGLFTVFS SFVFSSSVIN FLGSDVSDLK
     DALFFFLLLI DLSKATVLAQ FALSSRSQDE VKHNIARGIA MLGPTITLDT VVETLVIGVG
     MLSGVRRLEV LCCFACMSVI VNYVVFMTFY PACLSLILEL SRSGESGRPA WHDKSLIIKA
     LHEEDQKPNP VVQRVKVIMS AGLMLVHAHR WVRCLSIALW PDLTSLRYFC THCDTGVSYS
     RWSFASEGEE LPTVKLVTGD SVVNSNSTDD AQLHYYIMRW LTVSADHIVI LILLLALAVK
     FVFFETRDEL TTTRGMDGWV EVSSPVEHKY VQTEQPSCSA PEQPLEEPPA SNRSIDECLS
     VCKSDVGAQA LSDCEVMALV TSGHIAGYQL EKVVRNPERG VGIRRQILTK TADLKDALDN
     LPYKNYDYLK VMGACCENVI GYMPVPVGVA GPLNLDGRLV HVPLATTEGC LVASTNRGMR
     ALMRCGVTSR IVADGMTRGP VVRFPNIDRA SEAMLWMQVP YNFEQIKKNF DSTSRFARLS
     KIHIRVAGRH LFIRFIATTG DAMGMNMLSK GTEVALAYVQ QVYPDMEILS LSGNFCTDKK
     PAAVNWIEGR GKSVVCEAIV PADIIKSVLK TSVQALMDVN ITKNLIGSAV AGSIGGFNAH
     AANIVTAIFI ATGQDPAQNV GSSNCMTLME PWGEDGKDLY VSCTMPSIEI GTIGGGTVLP
     PQAACLDMLG VRGANEMCPG ENANTLARIV CGTVLAGELS LMSALAAGHL VKSHMRHNRS
     SVSTSGSEPS TPACKS
//