ID A0A0B5HZL7_ARCG3 Unreviewed; 388 AA.
AC A0A0B5HZL7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase {ECO:0000256|RuleBase:RU361219};
DE Short=HMG-CoA reductase {ECO:0000256|RuleBase:RU361219};
DE EC=1.1.1.34 {ECO:0000256|RuleBase:RU361219};
GN ORFNames=QT06_C0001G0398 {ECO:0000313|EMBL:AJF61239.1};
OS Archaeon GW2011_AR15.
OC Archaea.
OX NCBI_TaxID=1579373 {ECO:0000313|EMBL:AJF61239.1, ECO:0000313|Proteomes:UP000031776};
RN [1] {ECO:0000313|Proteomes:UP000031776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA Taylor R.C., Williams K.H., Banfield J.F.;
RT "Genomic expansion of domain archaea highlights roles for organisms from
RT new phyla in anaerobic carbon cycling.";
RL Curr. Biol. 25:690-701(2015).
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 Evidence={ECO:0000256|ARBA:ARBA00000020,
CC ECO:0000256|RuleBase:RU361219};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC {ECO:0000256|RuleBase:RU361219}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00007661, ECO:0000256|RuleBase:RU361219}.
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DR EMBL; CP010425; AJF61239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5HZL7; -.
DR STRING; 1579373.QT06_C0001G0398; -.
DR HOGENOM; CLU_001734_2_2_2; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000031776; Chromosome.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 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 NCBIfam; TIGR00533; HMG_CoA_R_NADP; 1.
DR PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR PANTHER; PTHR10572:SF24; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 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 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU361219};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361219}.
SQ SEQUENCE 388 AA; 41043 MW; F9DA1B3315FA112D CRC64;
MGTNSGSAKK LHEMAEEERR AFLEKKLGVN LENIKKSILN EKQADANIEN LIGSAQLPMG
IAGPVKVSGE HAKGEFYIPL ATTEGALVAS VSRGCSVISK SGGAEAVIIK NEQTRSILFK
AKSVKEAKKF TEWAEENFEK LKKAGEEGER FLRIIGIDSY VVGLNVWLRI KADTSDAMGM
NMVTIAGKKI ADYVSKNYEI EFVSESGNMC VDKKPGAMNL IESRGKRVIA SVSIPEEVIE
SVLKTTSDNL ADMNYRKNLL GSAASGSLGY NAHFANIIAA MFIATGQDAA HVVDGSLGFT
TVEKNEGGVN FSVTLSSLQV GTVGGGTGLK TQKEALSIMG VAGPGNPPGA NSKKLAEITA
AAVLAGEISL LGALCSKELS SSHQKLNR
//
