ID Q6MMK1_BDEBA Unreviewed; 438 AA.
AC Q6MMK1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 OrderedLocusNames=Bd1627 {ECO:0000313|EMBL:CAE79503.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE79503.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE79503.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842650; CAE79503.1; -; Genomic_DNA.
DR RefSeq; WP_011164105.1; NC_005363.1.
DR AlphaFoldDB; Q6MMK1; -.
DR STRING; 264462.Bd1627; -.
DR TCDB; 2.A.6.6.11; the resistance-nodulation-cell division (rnd) superfamily.
DR KEGG; bba:Bd1627; -.
DR eggNOG; COG1257; Bacteria.
DR HOGENOM; CLU_033422_0_0_7; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000008080; 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; 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:UP000008080}.
SQ SEQUENCE 438 AA; 47896 MW; 5405CF2B1A93058B CRC64;
MTKQLQDIFK GFSKLSREER LKALKEVGAL NEAEADYLAK GGLKDTSLGE KFIENVIGYF
QLPLGVVTNM RVDGKDFVVP MAVEETSIVA ACSKTAKWIR ESGSITTEVI GNEIIGQIQL
AKIRSFADFE KQILAQKNYL IEAANREVAF GLVRRGGGVR DLQVRRVPRG DGSDMAVIHI
LMDPCDAMGA NIINQVCEYL KEPIEQFSGE KVTMCILSNL VDSKVTRAVV RIDDIEPELA
EKIEEASLFA QMDPYRAATN NKGVLNGIDP ILIATGNDWR AVEAGIHAYA CRDGQYRSIT
RWYREGKSLV GVFEAPLVVG TVGGVTTLHP TAMLSMKMLD TKSANELSRI VAAVGLVQNL
GALKALTTVG IIEGHMKLHT KNLALGAGAE EKEIPLVQKK LEEILAIRKR ISLSNAIDVL
KELRAAQKTP ASTTQHHS
//
