ID A0A0A7KGE6_9FLAO Unreviewed; 440 AA.
AC A0A0A7KGE6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=M666_02445 {ECO:0000313|EMBL:AIZ43638.1};
OS Cellulophaga baltica 18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=1348584 {ECO:0000313|EMBL:AIZ43638.1, ECO:0000313|Proteomes:UP000030786};
RN [1] {ECO:0000313|EMBL:AIZ43638.1, ECO:0000313|Proteomes:UP000030786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18 {ECO:0000313|EMBL:AIZ43638.1,
RC ECO:0000313|Proteomes:UP000030786};
RX PubMed=24428166; DOI=10.1111/1462-2920.12391;
RA Holmfeldt K., Howard-Varona C., Solonenko N., Sullivan M.B.;
RT "Contrasting genomic patterns and infection strategies of two co-existing
RT Bacteroidetes podovirus genera.";
RL Environ. Microbiol. 16:2501-2513(2014).
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}.
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DR EMBL; CP009976; AIZ43638.1; -; Genomic_DNA.
DR RefSeq; WP_029444951.1; NZ_CP009976.1.
DR AlphaFoldDB; A0A0A7KGE6; -.
DR STRING; 1348584.M666_02445; -.
DR GeneID; 78059593; -.
DR KEGG; cbat:M666_02445; -.
DR HOGENOM; CLU_033422_0_0_10; -.
DR OrthoDB; 9764892at2; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000030786; Chromosome.
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; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR NCBIfam; TIGR00532; HMG_CoA_R_NAD; 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; 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}.
SQ SEQUENCE 440 AA; 48797 MW; E5914283C213B02B CRC64;
MNTPIEGFSK LTKEEKIAWI AKSYTTNSNE TIAILKRYWN ADETLQKLHD EFIENTITNY
YLPLGIAPNF LINDTLYAIP MAIEESSVVA AASKAAKFWL KRGGFKTTVI NTEKVGQVHF
MYTGAFEKLE SFFNLIAPKL KEDAKDITKN MEKRGGGITA ITLRNKTAEL ENYYQLHCTF
ETLDAMGANF INSCLEQFAE TLKNEFAKSP EFKEHEEQLE IVMSILSNYV PNCLVRAEVS
CPIEQLNEDN NSTAQDFAEK IVRAVQIAKV EPYRAVTHNK GIMNGIDAVV LATGNDFRAI
EAGIHAYAAK DGSYSSLTNA SIENGIFKFW IEIPLALGTV GGLTGLHPLV KLALEILQNP
SAKDLMQIVA VAGLAQNFAA VRSLVTTGIQ QGHMKMHLMN ILNQLGASEG DKKTLVHHFK
HNTVTHSAVI AAYNSLQEKE
//
