ID   HMDH_SULSO              Reviewed;         409 AA.
AC   O08424; Q9UWT6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   16-JUN-2009, entry version 66.
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=SSO0531; ORFNames=C22_020;
OS   Sulfolobus solfataricus.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   MEDLINE=97315236; PubMed=9171410;
RA   Bochar D.A., Brown J.R., Doolittle W.F., Klenk H.-P., Lam W.,
RA   Schenk M.E., Stauffacher C.V., Rodwell V.W.;
RT   "3-hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus
RT   solfataricus: DNA sequence, phylogeny, expression in Escherichia coli
RT   of the hmgA gene, and purification and kinetic characterization of the
RT   gene product.";
RL   J. Bacteriol. 179:3632-3638(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   MEDLINE=20165948; PubMed=10701121; DOI=10.1139/gen-43-1-116;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D.,
RA   Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C.,
RA   Kushwaha N., Lafleur E., Medina N., Peng X., Penny S.L., She Q.,
RA   St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F.,
RA   Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of
RT   the extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   MEDLINE=21332296; PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Converts HMG-CoA to mevalonate.
CC   -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-
CC       hydroxy-3-methylglutaryl-CoA + 2 NADPH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5;
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius. Stable at 90 degrees
CC         Celsius;
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.
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; U95360; AAC45370.1; -; Genomic_DNA.
DR   EMBL; Y18930; CAB57768.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40851.1; -; Genomic_DNA.
DR   PIR; D90199; D90199.
DR   PIR; T51306; T51306.
DR   RefSeq; NP_342061.1; -.
DR   HSSP; P04035; 1HWI.
DR   GeneID; 1454818; -.
DR   GenomeReviews; AE006641_GR; SSO0531.
DR   KEGG; sso:SSO0531; -.
DR   NMPDR; fig|273057.1.peg.484; -.
DR   HOGENOM; O08424; -.
DR   OMA; O08424; AHFANII.
DR   BioCyc; SSOL273057:SSO0531-MON; -.
DR   BRENDA; 1.1.1.34; 2070.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
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   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; FALSE_NEG.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Isoprene biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    409       3-hydroxy-3-methylglutaryl-coenzyme A
FT                                reductase.
FT                                /FTId=PRO_0000114465.
FT   ACT_SITE     99     99       Charge relay system (By similarity).
FT   ACT_SITE    305    305       Charge relay system (By similarity).
FT   ACT_SITE    400    400       Proton donor (By similarity).
FT   CONFLICT    245    245       V -> L (in Ref. 1; AAC45370).
SQ   SEQUENCE   409 AA;  44009 MW;  8D1FA64E117CFF46 CRC64;
     MKIDEVVEKL VKGEISFHEV DNLLEANAAM VARRLALEKI VGVGLPSIGS TVIDYSEIKN
     KNAENVIGAI QIPLGIVGPI RVNGDYAKGD FYVPMATTEG ALIASVNRGI KAVTLSGGVR
     AKVLKDEMTR APVFKFDSIE QIPNFLKFIE ENLEKIRNIA NSTSHHGKLK SITPFVLGNN
     VWLRFSFETG DAMGMNMVTI AVEKVCEFIE ENFPSADCLA VSGNMCSDKK QTNVNSLFGR
     GKTVVAEALI KKDVIRNILH SNAQLIHDIN LRKNWLGTAR AGSLSQFNAH FANIVTAIFI
     ATGQDVAQIV ESSSGYTWTE VRGEDLYISV TLPSLEVGTV GGGTRLPTQK EALSIMGVYG
     SGNPPGSNAK KLAEIIASTV LSGELNLLAA LSNKELGKAH AKLGRAMKV
//