ID   HMDH_ARCFU              Reviewed;         436 AA.
AC   O28538;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.34;
GN   Name=hmgA; OrderedLocusNames=AF_1736;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Converts HMG-CoA to mevalonate (By similarity).
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   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
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DR   EMBL; AE000782; AAB89513.1; -; Genomic_DNA.
DR   PIR; G69466; G69466.
DR   RefSeq; NP_070564.1; -.
DR   HSSP; P13702; 1QAY.
DR   GeneID; 1484959; -.
DR   GenomeReviews; AE000782_GR; AF_1736.
DR   KEGG; afu:AF1736; -.
DR   NMPDR; fig|224325.1.peg.1725; -.
DR   TIGR; AF_1736; -.
DR   HOGENOM; O28538; -.
DR   OMA; O28538; GIQRGHM.
DR   BioCyc; AFUL224325:AF_1736-MON; -.
DR   BRENDA; 1.1.1.34; 7576.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:EC.
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; IPR004553; HMG_CoA_Rdtase_II_bac/I_arc.
DR   Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1.
DR   PANTHER; PTHR10572; HMG-CoA_red; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   TIGRFAMs; TIGR00532; HMG_CoA_R_NAD; 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   Complete proteome; Isoprene biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    436       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114459.
FT   ACT_SITE     99     99       Charge relay system (By similarity).
FT   ACT_SITE    277    277       Charge relay system (By similarity).
FT   ACT_SITE    293    293       Charge relay system (By similarity).
FT   ACT_SITE    390    390       Proton donor (By similarity).
SQ   SEQUENCE   436 AA;  47146 MW;  BE0C2D61FA2A97A4 CRC64;
     MQVLRLDRRH YKSGKIRRAM SSRIPGFYKL SVEERLKKVA EFAGLSDEEV KAVLSQGLPL
     DVADRMIENV IGTFELPLGI ATNFLIDGKD YLIPMAIEEP SVVAAASNAA RMARESGGFT
     TDYTGSLMIG QIQVTKLLNP NAAKFEVLRQ KDEIIERANE CDPMLVNLGG GCKDIEARVI
     DTIMGKMLIV HLIVDVKDAM GANAVNTMCE KVAPFIERIT GGKVYLRIIS NLAAYRLARA
     KAVFDKDVIG GEEVVEGIML AYAFAAADPF RCATHNKGIM NGISALMIAT GNDFRAIEAG
     AHSYAAIGGY KPLTTYEVDR KGNLVGTIEI PMAVGVIGGA TKVNPLAKIS LKILGVNTAE
     ELARVAAALG LAQNFAALRA LATEGIQRGH MELHARNLAI MAGATGDEVD RVVEIMVRDG
     KIRLDYAKEV LERLRS
//