ID   HMDH_GIBFU              Reviewed;         976 AA.
AC   Q12577; Q12615;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.34;
GN   Name=HMGR; Synonyms=HMGA;
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   moniliforme).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella; Gibberella fujikuroi complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=m567;
RX   MEDLINE=97153466; PubMed=9000379; DOI=10.1007/s002940050174;
RA   Woitek S., Unkles S.E., Kinghorn J.R., Tudzynski B.;
RT   "3-hydroxy-3-methylglutaryl-CoA reductase gene of Gibberella
RT   fujikuroi: isolation and characterization.";
RL   Curr. Genet. 31:38-47(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 613-718.
RC   STRAIN=IMI 58289;
RA   Corrochano L.M., Avalos J.;
RT   "Cloning a segment of the gene encoding 3-hydroxy-3-methyglutaryl
RT   coenzyme A reductase in Phycomyces blakesleeanus and Gibberella
RT   fujikuroi.";
RL   Exp. Mycol. 16:167-171(1992).
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; X94307; CAA63970.1; -; Genomic_DNA.
DR   EMBL; X58370; CAA41261.1; -; Genomic_DNA.
DR   PIR; S17343; S17343.
DR   HSSP; P04035; 1DQA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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   3: Inferred from homology;
KW   Cholesterol biosynthesis; Endoplasmic reticulum; Glycoprotein;
KW   Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transmembrane.
FT   CHAIN         1    976       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114452.
FT   TRANSMEM     37     57       Potential.
FT   TRANSMEM     65     85       Potential.
FT   TRANSMEM     91    111       Potential.
FT   TRANSMEM    170    190       Potential.
FT   TRANSMEM    194    214       Potential.
FT   TRANSMEM    274    294       Potential.
FT   TRANSMEM    402    422       Potential.
FT   REGION      423    517       Linker.
FT   REGION      518    976       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    451    451       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    498    498       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    682    682       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    928    928       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    686    686       R -> S (in Ref. 2; CAA41261).
SQ   SEQUENCE   976 AA;  105395 MW;  2B8F1C9F3CB5A714 CRC64;
     MDHEGCQGQH PQQCCQWVSN AWSEFLDLLK NAETLDIVIM LLGYIAMHLT FVSLFLSMRK
     MGSKFWLGIC TLFSSVFAFL FGLVVTTKLG VPISVILLSE GLPFLVVTIG FEKNIVLTRA
     VMSHAIEHRR IQAQNSKSGK RSPDGSTQNM IQYAVQAAIK EKGFEIIRDY AIEIVILVIG
     AASGVQGGLQ QFCFLAAWTL FFDFILLFTF YTAILSIKLR STVSSVMSIC VWPLRMMASR
     RVAENVAKGD DELNRVRGDA PLFGRKSSSI PKFKVLMILG FIFVNIVNIC SIPFRNPSSM
     STIRTWASSL GGVIAPLSVD PFKVASNGLD AILPTAKSNN RPTLVTVLTP IKYELEYPSI
     HYALGSAASN PAYNDAFHHH FQGYGVGGRM VGGILKSLED PVLSKWIVIA LALSVALNGY
     LFNVARWGIK DPNVPEHNID RNELARAREF NDTGSATLPL GEYVPPTPMR TQPSTPAITD
     DEAEGLHMTK ARPANLPNRS NEELEKLLSE NALREMTDEE VISLSMRGKI PGYALEKTLG
     DFTRAVKIRR SIIARNKAAA DITHSLDRSK LPYENYNWER FFGACCENVI GYMPLPVGVA
     GPLVIDGQSY FIPMATTEGV LVASASRGCK AINSGGGAIT VLTADGMTRG PCVAFETLER
     AGAAKLWLDS EAGQDMMKKA FNSTSRFARL QSMKTALAGT NLYIRFKTTT GDAMGMNMIS
     KGVEHALSVM ANDGGFDDMQ IISVSGNYCT DKKAAALNWI DGRGKGVVAE AIIPGEVVRS
     VLKSDVDSLV ELNVAKNLIG SAMAGSVGGF NAHAANIVAA IFLATGQDPA QVVESANCIT
     IMKNLNGALQ ISVSMPSLEV GTLGGGTILE PQGAMLDILG VRGSHPTNPG DNARRLARII
     GAAVLAGELS LCSALAAGHL VRAHMQHNRS AAPSRSTTPG SSHDARLTGH DQCPRALSVN
     NVDERRRYSE VKAIDE
//