ID A0A1F8TLG7_9CHLR Unreviewed; 393 AA.
AC A0A1F8TLG7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-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};
DE Flags: Fragment;
GN ORFNames=A2Z49_07370 {ECO:0000313|EMBL:OGO72960.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_56_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797670 {ECO:0000313|EMBL:OGO72960.1, ECO:0000313|Proteomes:UP000177731};
RN [1] {ECO:0000313|EMBL:OGO72960.1, ECO:0000313|Proteomes:UP000177731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO72960.1}.
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; MGOL01000029; OGO72960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8TLG7; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000177731; Unassembled WGS sequence.
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; 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}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGO72960.1"
SQ SEQUENCE 393 AA; 41302 MW; BFF6A75779797E5D CRC64;
TGEQGLAAEQ ADHMIENVVG RFALPLGVAL NFIVNRREVL VPMVVEEPSI VAGASFMAKL
ARPGGGFTAH CTPPEMIGQV QILDVADLPA ARLAIVDQKA ALLEEIAGID PVLKRLGGGP
RDLEVRLIAE SPIGPFLVVH LIYDVRDAMG ANAINTAVER IAPRLEALTG GRAHLRILSN
LADRRLASAH CTILLSELAF GEYAAEDVRD GIIAAWAFAA ADPYRAATHN KGIMNGVDPI
VIATGNDWRA IEAGAHAYAA RSGRYTSLST WGKDALGNLV GTLEIPMAVG IVGGATKVHP
AARAALKLMG VTSASGLAEI IVSVGLAQNL AALRALATEG IQRGHMGLHA RQVAIAAGAE
GDMIERLAAQ LSAEKTVRID RAEAILKEWK QTK
//
