HMDH_SACS2
ID HMDH_SACS2 Reviewed; 409 AA.
AC O08424; Q9UWT6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=9171410; DOI=10.1128/jb.179.11.3632-3638.1997;
RA Bochar D.A., Brown J.R., Doolittle W.F., Klenk H.-P., Lam W., Schenk M.E.,
RA 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 of
RT the hmgA gene, and purification and kinetic characterization of the gene
RT 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 PubMed=10701121; DOI=10.1139/g99-108;
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., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT 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 PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., 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:
CC Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
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; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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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; WP_010923027.1; NC_002754.1.
DR AlphaFoldDB; O08424; -.
DR SMR; O08424; -.
DR STRING; 273057.SSO0531; -.
DR EnsemblBacteria; AAK40851; AAK40851; SSO0531.
DR GeneID; 44129547; -.
DR KEGG; sso:SSO0531; -.
DR PATRIC; fig|273057.12.peg.530; -.
DR eggNOG; arCOG04260; Archaea.
DR HOGENOM; CLU_001734_2_2_2; -.
DR InParanoid; O08424; -.
DR OMA; DDKMTRA; -.
DR PhylomeDB; O08424; -.
DR BioCyc; MetaCyc:MON-14624; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 3.30.70.420; -; 1.
DR Gene3D; 3.90.770.10; -; 1.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR PANTHER; PTHR10572; PTHR10572; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; SSF55035; 1.
DR SUPFAM; SSF56542; SSF56542; 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; PS50065; HMG_COA_REDUCTASE_4; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..409
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase"
FT /id="PRO_0000114465"
FT ACT_SITE 99
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 400
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 245
FT /note="V -> L (in Ref. 1; AAC45370)"
FT /evidence="ECO:0000305"
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
