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Entry: A0A1E7GE40_9EURY
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ID   A0A1E7GE40_9EURY        Unreviewed;       418 AA.
AC   A0A1E7GE40;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BGV40_05130 {ECO:0000313|EMBL:OEU43221.1};
OS   Methanosarcina sp. Ant1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1882735 {ECO:0000313|EMBL:OEU43221.1, ECO:0000313|Proteomes:UP000175834};
RN   [1] {ECO:0000313|EMBL:OEU43221.1, ECO:0000313|Proteomes:UP000175834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant1 {ECO:0000313|EMBL:OEU43221.1};
RA   Buongiorno J., Bird J.T., Krivushin K., Oshurkova V., Shcherbakova V.,
RA   Rivkina E.M., Lloyd K.G., Vishnivetskaya T.;
RT   "Draft Genome Sequence of Antarctic Methanogen Enriched from Dry Valley
RT   Permafrost.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEU43221.1}.
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DR   EMBL; MDTP02000054; OEU43221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7GE40; -.
DR   UniPathway; UPA00058; UER00103.
DR   Proteomes; UP000175834; Unassembled WGS sequence.
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   418 AA;  44931 MW;  80E49FA138D4DDBE CRC64;
     MLQEDYELNE NEKLILQKVV DGDIAFRKIE EFADPFTAVK IRRLAIQELT KLEFEHIQNF
     SLDVEAAAKK NIENMIGAVQ VPLGVAGLLK VNGEYANAEY YIPLATTEGA LVASVNRGCS
     VITKSGGANV RIFEDEMTRA PVFKLDSLDR AKKFYEWVKS PAIFEQMKAV AEKTTRFGKL
     IAVKPFVTGT YVYLRFSYDT KDAMGMNMVT IATDAVMHLI EDEFGAQPIT LSGNMCTDKK
     PASISTILGR GKTVVAEVTI PKEIVKETLK CTPESMFEVN YSKNLLGSAR AGSLGFNAHA
     ANVIAAIYLA CGQDAAHVVE GSTAITSMEL TKYEEIHCSV TLPALPVGTV GGGTGLGTQR
     DCLNILGVAG AGNIPGENSR KFAEIVASAV LAGEISLIGA QAAGHLARAH AQLGRGKF
//
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