ID A0A0R2DN51_9LACO Unreviewed; 421 AA.
AC A0A0R2DN51;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=FD13_GL001384 {ECO:0000313|EMBL:KRN01156.1};
OS Levilactobacillus senmaizukei DSM 21775 = NBRC 103853.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423803 {ECO:0000313|EMBL:KRN01156.1, ECO:0000313|Proteomes:UP000051589};
RN [1] {ECO:0000313|EMBL:KRN01156.1, ECO:0000313|Proteomes:UP000051589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21775 {ECO:0000313|EMBL:KRN01156.1,
RC ECO:0000313|Proteomes:UP000051589};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN01156.1}.
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; AYZH01000032; KRN01156.1; -; Genomic_DNA.
DR RefSeq; WP_061777453.1; NZ_BCWD01000034.1.
DR AlphaFoldDB; A0A0R2DN51; -.
DR STRING; 1423803.FD13_GL001384; -.
DR PATRIC; fig|1423803.3.peg.1420; -.
DR OrthoDB; 9764892at2; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000051589; 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; 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}.
SQ SEQUENCE 421 AA; 45251 MW; 4F65ADA965BD6924 CRC64;
MDQTPFYRQS YGARRDQLAQ ASHLTADQLA TLAANRQTTD EDLIENYLTT YGLPEGVAVN
LQVDGQAVAV PMVTEEPSVI AAASNGGRLL SGQSGITTVV ANHELMGQIV FQHVADQPAL
RQWLQDHEAT LLAVADAAHP SIKRRGGGAR SIRVRLLRPD WVSLDLFVDV SEAMGANLVN
TMAEAVATYI RSQLDVDILM SILSNFATRS LVTASCVVPV DQMKTKTISG QTVAQRICAA
SDYAQIDPYR AVTHNKGIMN GIDAVVLAMG NDWRAVESGV HAYASRRGRY QGVSRWWLDD
DQKLHGELTI PLTLGVVGGA TRVLPLVSVN QLIAKVTSVR QLMGITAAVG LAQNVAALRA
LVTDGIQKGH MHLQLKSLAL SVGAQEAEVA AVAERLADQT QPTIEQAQTA LTVVRAENLK
K
//
