ID A0A0E3S393_9EURY Unreviewed; 418 AA.
AC A0A0E3S393;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=MSLAZ_2113 {ECO:0000313|EMBL:AKB75374.1};
OS Methanosarcina lacustris Z-7289.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB75374.1, ECO:0000313|Proteomes:UP000033072};
RN [1] {ECO:0000313|EMBL:AKB75374.1, ECO:0000313|Proteomes:UP000033072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-7289 {ECO:0000313|EMBL:AKB75374.1,
RC ECO:0000313|Proteomes:UP000033072};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009515; AKB75374.1; -; Genomic_DNA.
DR RefSeq; WP_048126832.1; NZ_CP009515.1.
DR AlphaFoldDB; A0A0E3S393; -.
DR STRING; 1434111.MSLAZ_2113; -.
DR GeneID; 24806908; -.
DR KEGG; mls:MSLAZ_2113; -.
DR PATRIC; fig|1434111.4.peg.2802; -.
DR HOGENOM; CLU_001734_2_2_2; -.
DR OrthoDB; 10981at2157; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000033072; 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 418 AA; 45004 MW; E2E9A87DFE3878B1 CRC64;
MFLKDNDLTE DEKLLLQKVL DGDIAFRKIE EFADPLTAVK IRRLAIQEYA KLEFEHIQNF
SLDVETVTKK NIENMIGAVQ IPLGVAGLLK VNGEYADAEY YIPLATTEGA LVASVNRGCS
VITKSGGANV RVFEDEMTRA PVFKLESLDR TKKFYEWVKS PEIFEQMKTV AEKTTRFGKL
LSVKPFVTGT YVYLRFSYDT KDAMGMNMVT IATDAVMHLI EDEFGAHPIT LSGNMCTDKK
PASISTILGR GKTVVAEVTI PEEIVKETLK CTPDAMFEVN YSKNLLGSAR AGALGFNAHA
ANVIAAVYLA CGQDAAHVVE GSTAITSMEL TKYGEIHCSV TLPALPVGTV GGGTGLGTQR
DCLNILGVAG TGDIPGINSR KFAEIVASAV LAGEISLIGA QAAGHLARAH AQLGRGKF
//
