ID   HMDH_PICJA              Reviewed;         934 AA.
AC   O74164;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.34;
GN   Name=HMG;
OS   Pichia jadinii (Yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98320604; PubMed=9647847;
RA   Shimada H., Kondo K., Fraser P.D., Miura Y., Saito T., Misawa N.;
RT   "Increased carotenoid production by the food yeast Candida utilis
RT   through metabolic engineering of the isoprenoid pathway.";
RL   Appl. Environ. Microbiol. 64:2676-2680(1998).
CC   -!- FUNCTION: Involved in the control of cholesterol biosynthesis. It
CC       is the rate-limiting enzyme of the sterol biosynthesis.
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   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
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DR   EMBL; AB012603; BAA31937.1; -; mRNA.
DR   HSSP; P04035; 1DQA.
DR   BRENDA; 1.1.1.34; 288941.
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:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
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; 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; 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   Cholesterol biosynthesis; Endoplasmic reticulum; Glycoprotein;
KW   Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transmembrane.
FT   CHAIN         1    934       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114454.
FT   TRANSMEM    112    132       Potential.
FT   TRANSMEM    142    162       Potential.
FT   TRANSMEM    257    277       Potential.
FT   TRANSMEM    335    355       Potential.
FT   TRANSMEM    422    442       Potential.
FT   REGION      443    521       Linker.
FT   REGION      522    934       Catalytic.
FT   ACT_SITE    618    618       Charge relay system (By similarity).
FT   ACT_SITE    752    752       Charge relay system (By similarity).
FT   ACT_SITE    828    828       Charge relay system (By similarity).
FT   ACT_SITE    924    924       Proton donor (By similarity).
FT   CARBOHYD    361    361       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    364    364       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    382    382       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    682    682       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   934 AA;  101234 MW;  3C3E43FC5623601C CRC64;
     MFYHGASANQ HWIAVDDLSK VPVDVDHYNV VPFQFRRAGE YKEPVLSGIV ELDEVKFVVS
     QSDAAEQWQQ LTAEDGTVWR SRAYHGKLGK YSDMAVGAFN KVLNLVRGAE TFDIALVTCA
     YIAMFYTLFN LFARMRAVGS KVWLGLSTLV SSFFAFLFAL YITTRVLDLS IPFLSLSEGI
     PFFVAVVGFN NKILLAEKVL QNQLNAQSSK NDAPTVLYQA LREQGPLLLR DHLFMITAFL
     GCSFYASYLD GLKNFCILAA LILAFDILTT STFLSAILSL KLEINQIHRS TLLREQLEDD
     GLTETTVDDV LKSNSLAGTK TFTDAPSTLV TVAKVAGVSV FFGLHFYGFG SAWLSDLSAG
     NETNDTFTLY DAVADQIPIG SNGTLVTLFP TRFFLPEKLS TQIEAVVLSF IGLISTAARD
     KYISKFILFA FAVSASINVY LLNVARIHTT RLEDAIELKK PKKKASKTAV SVPKAVVVKD
     SETTKSSEIL HSSSESESEQ SSRPLEQVIE LYKDGKVKTL VDDEVVSLVT AGKLPLYALE
     KQLGDNLRAV AIRRKAISDL ADAPVLRSNK LPYLHYDYDR VFGACCENVI GYMPLPVGVA
     GPLIIDGKPY HIPMATTEGC LVASAMRGCK AINLGGGVTT VLTKDGMTRG PCVKFPSLKR
     AGQCKLWLDS DEGQEEMKKA FNSTSRFARL QHLQTALAGD LLFIRFRTVT GDAMGMNMIS
     KGVEYALKQM TEVFGWDDMM VVSVSGNYCT DKKPAAVNWI NGRGKSVVAE ASIPKDAVVK
     VLKSSVKAVV DVNVNKNLIG SAMAGSVGGF NAQAANMVTA VYLALGQDPA QNVESSNCIT
     LMTETEDGDL KVSVSMPSIE VGTIGGGTIL DPQGSMLELL GVRGPADVPG ENARQLAKIV
     ASIVLSGELS LVSALAAGHL VQSHMQHNRA AAKK
//