ID   HMDH_BORBU              Reviewed;         431 AA.
AC   O51628;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Probable 3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE            Short=HMG-CoA reductase;
DE            EC=1.1.1.88;
GN   OrderedLocusNames=BB_0685;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Converts HMG-CoA to mevalonate. {ECO:0000250}.
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   -!- PATHWAY: Metabolic intermediate metabolism; (R)-mevalonate degradation;
CC       (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR   EMBL; AE000783; AAC67032.1; -; Genomic_DNA.
DR   PIR; D70185; D70185.
DR   RefSeq; NP_212819.1; NC_001318.1.
DR   RefSeq; WP_010889799.1; NC_001318.1.
DR   AlphaFoldDB; O51628; -.
DR   SMR; O51628; -.
DR   STRING; 224326.BB_0685; -.
DR   PRIDE; O51628; -.
DR   EnsemblBacteria; AAC67032; AAC67032; BB_0685.
DR   KEGG; bbu:BB_0685; -.
DR   PATRIC; fig|224326.49.peg.1076; -.
DR   HOGENOM; CLU_033422_0_0_12; -.
DR   OMA; GHMKMHL; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000001807; 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; 3.30.70.420; -; 1.
DR   Gene3D; 3.90.770.10; -; 2.
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   PANTHER; PTHR10572; PTHR10572; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   SUPFAM; SSF55035; SSF55035; 1.
DR   SUPFAM; SSF56542; SSF56542; 1.
DR   TIGRFAMs; TIGR00532; HMG_CoA_R_NAD; 1.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..431
FT                   /note="Probable 3-hydroxy-3-methylglutaryl-coenzyme A
FT                   reductase"
FT                   /id="PRO_0000114466"
FT   ACT_SITE        85
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        278
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        375
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   431 AA;  48922 MW;  A98DA9099AB0CDB4 CRC64;
     MNLESLSSFM ELSKNFRHKS VLEKRQEIKS FLELSYKDFF YNNANEDFLF NMIENYIGYL
     SFPIGIVKNL KINGKYYSLP IATEESSVVA ALNFAAKILE NADLRYSLGE VLGISQIYIK
     SEKDLSKIFV DLGDKIKTWI EPLLTNMNQR GGGFRRLSTR HIKELGIQKL NIYVDTCDAM
     GANLLNSIAE RVAEFIFLEF GYECVLKVLS NDISEFTAKA RFVLDFKHLL PGKEDSWNLA
     KKIELISSIG FYEEERAVTN NKGIMNGITG VCLATFNDTR ALEASVHKFA SKSGKYFPLS
     KFYTTDNALV GEIEIPLQVG TKGGVISFNE ASILSFKIMN VNSKSEFIGI LSCVGLASNF
     AALRALAFNG IQKGHMRLHV NKILHLLKTK YNISDFEKDK LLLEMERMNI YSFDFAFKIL
     KKIRLENENK V