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Database: UniProt
Entry: A0A1D7Y0E4_9FLAO
LinkDB: A0A1D7Y0E4_9FLAO
Original site: A0A1D7Y0E4_9FLAO 
ID   A0A1D7Y0E4_9FLAO        Unreviewed;       427 AA.
AC   A0A1D7Y0E4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=FORMB_20350 {ECO:0000313|EMBL:AOR29063.1};
OS   Formosa sp. Hel1_33_131.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1336794 {ECO:0000313|EMBL:AOR29063.1, ECO:0000313|Proteomes:UP000094750};
RN   [1] {ECO:0000313|EMBL:AOR29063.1, ECO:0000313|Proteomes:UP000094750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_33_131 {ECO:0000313|EMBL:AOR29063.1,
RC   ECO:0000313|Proteomes:UP000094750};
RA   Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA   Chafee M.;
RT   "Glycan utilization in Formosa spp.";
RL   Submitted (SEP-2016) 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}.
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DR   EMBL; CP017260; AOR29063.1; -; Genomic_DNA.
DR   RefSeq; WP_069677260.1; NZ_CP017260.1.
DR   AlphaFoldDB; A0A1D7Y0E4; -.
DR   STRING; 1336794.FORMB_20350; -.
DR   KEGG; for:FORMB_20350; -.
DR   PATRIC; fig|1336794.4.peg.1995; -.
DR   OrthoDB; 9764892at2; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000094750; 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   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   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; PS00066; HMG_COA_REDUCTASE_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094750}.
SQ   SEQUENCE   427 AA;  47075 MW;  5DB21B7D762C15FD CRC64;
     MENSVSGFSK FTKAEKIDWL IANHFQNNPK AKADLERYWN TDEVLQKLHD EFTENTISNF
     YLPFGVAPNF LINDKMYVIP MTIEESSVVA AASNAAKFWM ERGGFKAEVL STTKVGQVHF
     MFHGAFSELE ALFKTIKPQL FEETKAITKN MEARGGGILD IALMDKTEKL SGYYQLHTTF
     ETKDAMGANF INSCLEQIAT TFKSCSKDIQ VVMSILSNYV PDCLVRAEVS CKVDALATNT
     YTGQEFADTF LQAVRIAEIE PYRAVTHNKG IMNGVDSVVL ATGNDFRAVE AGVHAYAARS
     GSYSSLTHAS IEDGAFKFWI ELPLALGTVG GLTGLHPLVK TALELLGKPS AKELMEIVAV
     AGLAQNFAAL KSLTTTGIQQ GHMKMHLLNI LNQFEANATE KIHLIEHFKT HTVTHSAVVE
     AIENLRA
//
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