ID T0TK54_LACLC Unreviewed; 410 AA.
AC T0TK54;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 38.
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=LLT6_11635 {ECO:0000313|EMBL:EQC57939.1};
OS Lactococcus cremoris subsp. cremoris TIFN6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234876 {ECO:0000313|EMBL:EQC57939.1, ECO:0000313|Proteomes:UP000015854};
RN [1] {ECO:0000313|EMBL:EQC57939.1, ECO:0000313|Proteomes:UP000015854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN6 {ECO:0000313|EMBL:EQC57939.1,
RC ECO:0000313|Proteomes:UP000015854};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(2013).
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:EQC57939.1}.
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DR EMBL; ATBB01000068; EQC57939.1; -; Genomic_DNA.
DR AlphaFoldDB; T0TK54; -.
DR PATRIC; fig|1234876.3.peg.386; -.
DR UniPathway; UPA00257; UER00367.
DR Proteomes; UP000015854; 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 Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 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; 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:UP000015854}.
SQ SEQUENCE 410 AA; 44910 MW; 62B2BA64460E52D2 CRC64;
MRKKFYQMSP QERLNSLNLS EKSQEILSEM ALDTTILDNL IENQISEFEL PMGIAQNFVI
NGQSFLIPMV TEEPSVIAAA SNGAKIAGNF VAEIKERLMR GQIVFYDVKN SDKIANEILE
KQEKIFEQAE LSYPSIVKRG GGLREVSSRI FSSQKFLSVD VKVDVKDAMG ANIINSILEG
IAELFRRWFP DEKILFSILS NYATESLVKV TCEIPVERLS KKADGYEIGQ KIMAASQYSK
IDPYRASTHN KGIMNGINAV ILATGNDTRA ISAAIHAYAA KDGAYQGLAN WELQEKMLVG
ELEIPLPVAT VGGGVKVLPK AQAAMEILGI SDAKELAKVI AAVGLAQNLA ALRALVSEGI
QQGHMSLQAR SLALSVGAQA DEIAILSQQL RKEKVMNQEV AQNLLKNLRK
//
