ID Q26FY8_FLABB Unreviewed; 478 AA.
AC Q26FY8;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=BBFL7_01971 {ECO:0000313|EMBL:EAS21078.1};
OS Flavobacteria bacterium (strain BBFL7).
OC Bacteria; Bacteroidota; Flavobacteriia.
OX NCBI_TaxID=156586 {ECO:0000313|EMBL:EAS21078.1, ECO:0000313|Proteomes:UP000002172};
RN [1] {ECO:0000313|EMBL:EAS21078.1, ECO:0000313|Proteomes:UP000002172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBFL7 {ECO:0000313|EMBL:EAS21078.1,
RC ECO:0000313|Proteomes:UP000002172};
RA Azam F., Beardsley C., Gaasterland T., Malfatti F., Mayali X., Podell S.,
RA Samo T., Smriga S., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) 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 -!- 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:EAS21078.1}.
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; AAPD01000001; EAS21078.1; -; Genomic_DNA.
DR AlphaFoldDB; Q26FY8; -.
DR STRING; 156586.BBFL7_01971; -.
DR HOGENOM; CLU_033422_0_0_10; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000002172; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|RuleBase:RU361219};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361219};
KW Reference proteome {ECO:0000313|Proteomes:UP000002172};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 478 AA; 52703 MW; CEDB0A8931BBAC74 CRC64;
MQNGLKYQVY RKNRKNPADY CIIVKQGLTL VIVSLSLKFF SMDAPVIGFS KLSKTEKVNW
LVDTYFDGNT AAHDTITRYW NQDQKLQELH DGFSENTITN YYFPFGLAPN FLIDGKLVTI
PMAIEESSVV AAASKAAKFW LNRGGFKTKV RSTVKSGQVH IMYNGLHGEM DAFYAFAKAD
LLQSVQSINA SMKKRGGGLL DLQLINKTDV LAGYYQLHAT FETKDAMGAN FINTTLEQLA
NTLREKANEF QGFSLGMPEV IMSILSNYVP ECVVNVSVSC TINEIGTING VSGEDFARKF
TRAVDIATVE PYRAVTHNKG IMNGIDAVVI ATGNDFRAVE AGVHAYAARD GQYRSLTRAR
VENDVFTFEA DFPLALGTVG GLTSLHPLSK LAMQILENPS AQDLMKVTAV CGLAQNFAAL
HSLVTTGIQA GHMKMHLVNM LEQIGANDDE KLLLKKAFQD KTPSFSGLRE MLADIRKK
//
