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Database: UniProt
Entry: A0A0F4LRP6_9LACO
LinkDB: A0A0F4LRP6_9LACO
Original site: A0A0F4LRP6_9LACO 
ID   A0A0F4LRP6_9LACO        Unreviewed;       420 AA.
AC   A0A0F4LRP6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   Name=hmgA {ECO:0000313|EMBL:KJY60983.1};
GN   ORFNames=JG30_11710 {ECO:0000313|EMBL:KJY60983.1};
OS   Bombilactobacillus mellifer.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Bombilactobacillus.
OX   NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY60983.1, ECO:0000313|Proteomes:UP000033558};
RN   [1] {ECO:0000313|EMBL:KJY60983.1, ECO:0000313|Proteomes:UP000033558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin4 {ECO:0000313|EMBL:KJY60983.1,
RC   ECO:0000313|Proteomes:UP000033558};
RA   Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA   Vasquez A.;
RT   "Comparative genomics of the lactic acid bacteria isolated from the honey
RT   bee gut.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJY60983.1}.
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DR   EMBL; JXJQ01000009; KJY60983.1; -; Genomic_DNA.
DR   RefSeq; WP_046316999.1; NZ_KQ034028.1.
DR   AlphaFoldDB; A0A0F4LRP6; -.
DR   STRING; 1218492.JG30_11710; -.
DR   PATRIC; fig|1218492.5.peg.1314; -.
DR   HOGENOM; CLU_033422_0_0_9; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000033558; 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; 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; 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:UP000033558}.
SQ   SEQUENCE   420 AA;  45239 MW;  442BC14F3168C422 CRC64;
     MTKFYELSTE QRLQQLEEQG ILTASEKALF RDNTALPTTI ASRLVENQIG TFPLPLGLAN
     HFLIDGHQYL VPMAIEEPSV IAAASNAAQR VARSGGFTTQ VQRQGIRAQI VFVGQLGQPQ
     KFLKAQQRAL KQVALQAHPS LIAHGGGLRQ ITVQQQEEFV EFQLLIDPGE AMGANVVNTI
     AEAVGHYLQI QLPQLEYLMA ILSNHAPEQK VQAVAEVQFE QLQTSNLSGE VVARKIVQAS
     KLAHISLARA ATHNKGIMNG VQAVVLATGN DTRNVAASVY AGLNDQHRSL SSWHLTPKGL
     RGVLNLNLPL GSVGGAISTL PLAQINLKIL QHPSAAQLMR IIASVGLASN LAALRALVTQ
     GIQAGHMNLQ LQSLALMAGA RTSEIDLIVK QLRQQPQQAN LAQAKALITK LRQQSQGGIE
//
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