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Database: UniProt
Entry: V7HY74_9LACO
LinkDB: V7HY74_9LACO
Original site: V7HY74_9LACO 
ID   V7HY74_9LACO            Unreviewed;       428 AA.
AC   V7HY74;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=LEQ_0622 {ECO:0000313|EMBL:ETA73966.1};
OS   Ligilactobacillus equi DPC 6820.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA73966.1, ECO:0000313|Proteomes:UP000018559};
RN   [1] {ECO:0000313|EMBL:ETA73966.1, ECO:0000313|Proteomes:UP000018559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA73966.1,
RC   ECO:0000313|Proteomes:UP000018559};
RX   PubMed=24435863;
RA   O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT   "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT   equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL   Genome Announc. 2:e01155-e01113(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}.
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:ETA73966.1}.
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DR   EMBL; AWWH01000135; ETA73966.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7HY74; -.
DR   PATRIC; fig|1392007.3.peg.1199; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000018559; 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   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018559}.
SQ   SEQUENCE   428 AA;  46102 MW;  B24562E9032CB847 CRC64;
     MEVFMKAIHK FYQKSWQERL AILAQSQLLS DDEIKLFQVN GHQAELFDSL IENYVTDYSL
     PQGLATNYVI DGHEYLIPMV TEEPSVVAAS SNGAGLVKRA GGFQSHITER LMVGQVVLEK
     VAEPAKLKAT ILAQEADFLA CANEAHPSIV KRGGGARFLE VRILSESEGL LSLDLAVDVQ
     EAMGANMLNT MLEALAQKIR QELGQEVLMA ILSNYAVHSL VTVTCEIEPK LLAKGELSGE
     EVAQKIALAS HVAQLDPSRA ATHNKGIMNG IDAVVLASGN DWRAIEAGAH AYASRDGQYR
     GLSQWNYQDG KLHGSLTLPM PVGSVGGSIG VIPLVKANHQ LLQIKDAKQL ATVIVAVGLG
     QNLAALKALV TDGIQKGHMH LQLKTLAVKV GATQSEVTSL VAQMEKAGKR DENSARQLLA
     QIRESRGN
//
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