ID A0A2K8WKJ7_9RHOB Unreviewed; 423 AA. AC A0A2K8WKJ7; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 03-MAY-2023, entry version 17. 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=1.1.1.88 {ECO:0000256|RuleBase:RU361219}; GN ORFNames=CDO87_26410 {ECO:0000313|EMBL:AUC56807.1}; OS Sagittula sp. P11. OG Plasmid unnamed5 {ECO:0000313|EMBL:AUC56807.1}. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Sagittula. OX NCBI_TaxID=2009329 {ECO:0000313|EMBL:AUC56807.1, ECO:0000313|Proteomes:UP000232586}; RN [1] {ECO:0000313|EMBL:AUC56807.1, ECO:0000313|Proteomes:UP000232586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P11 {ECO:0000313|EMBL:AUC56807.1, RC ECO:0000313|Proteomes:UP000232586}; RC PLASMID=Plasmid unnamed5 {ECO:0000313|Proteomes:UP000232586}; RA Martinez-Perez C., Mohr W., Kuypers M.M.; RT "Metabolic versatility of a novel N2-fixing alphaproteobacterium isolated RT from an oxygen minimum zone."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3- CC methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88; CC Evidence={ECO:0000256|RuleBase:RU361219}; CC -!- PATHWAY: Metabolic intermediate metabolism; (R)-mevalonate degradation; CC (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1. 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; CP021919; AUC56807.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2K8WKJ7; -. DR EnsemblBacteria; AUC56807; AUC56807; CDO87_26410. DR KEGG; sagu:CDO87_26410; -. DR OrthoDB; 9764892at2; -. DR UniPathway; UPA00257; UER00367. DR Proteomes; UP000232586; Plasmid unnamed5. DR GO; GO:0140643; F:hydroxymethylglutaryl-CoA reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:InterPro. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR CDD; cd00644; HMG-CoA_reductase_classII; 1. DR Gene3D; 1.10.8.660; -; 1. DR InterPro; IPR002202; HMG_CoA_Rdtase. DR InterPro; IPR004553; HMG_CoA_Rdtase_bac-typ. DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf. DR InterPro; IPR023076; HMG_CoA_Rdtase_CS. DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf. DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf. 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 TIGRFAMs; TIGR00532; HMG_CoA_R_NAD; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|RuleBase:RU361219}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361219}; Plasmid {ECO:0000313|EMBL:AUC56807.1}. SQ SEQUENCE 423 AA; 44338 MW; 90549321F4D584FF CRC64; MTDHTSRLPG FAQASREERI GILAERLGGN AEALQLFDNL GPIEGGLVDR LIENAIGVMP VPLGLATNMI VDGEEMLVPM ATEESSVIAA VCNSAKRCRD TGGFFTSYSG SLTIAQVQLC GLSDPRNARA QILGRTDEIR AICDEVDPQL TSLGGGLREV DVRLVEARSG TMVIVHLVVD TLDAMGANAV NSMAERVAPM LAGWTGARPL LRILSNLADR RLTRARAVWP ADQIGGPEVV EAMLLGAEFA EADPYRATTH NKGIMNGISA VVLATGNDTR AIESGAHAYA AQCGQYGPLT HWEKTAEGDL AGTIELPLSL GIVGGATRVH PVAQLCLKVL GADSAEKLAR ITAAVGLAQN FGALRALATD GIQKGHMALH AQNVAIAAGA EGDEIESVAA GLRAHGRVTE AEARKLLDDL RKG //