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   16-JUN-2009, entry version 67.
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   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; 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.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Converts HMG-CoA to mevalonate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NAD(+) = 3-hydroxy-3-
CC       methylglutaryl-CoA + 2 NADH.
CC   -!- PATHWAY: Metabolic intermediate metabolism; mevalonic acid
CC       degradation; HMG-CoA from (R)-mevalonic acid: step 1/1.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000783; AAC67032.1; -; Genomic_DNA.
DR   PIR; D70185; D70185.
DR   RefSeq; NP_212819.1; -.
DR   HSSP; P13702; 1QAY.
DR   GeneID; 1195537; -.
DR   GenomeReviews; AE000783_GR; BB_0685.
DR   KEGG; bbu:BB0685; -.
DR   NMPDR; fig|224326.1.peg.1069; -.
DR   TIGR; BB_0685; -.
DR   HOGENOM; O51628; -.
DR   OMA; O51628; GIQRGHM.
DR   BioCyc; BBUR224326:BB_0685-MON; -.
DR   BRENDA; 1.1.1.88; 142596.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:InterPro.
DR   GO; GO:0042282; F:hydroxymethylglutaryl-CoA reductase activity; IEA:EC.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002202; HMG_CoA_Rdtase_cat.
DR   InterPro; IPR004553; HMG_CoA_Rdtase_II_bac/I_arc.
DR   Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1.
DR   PANTHER; PTHR10572; HMG-CoA_red; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   TIGRFAMs; TIGR00532; HMG_CoA_R_NAD; 1.
DR   PROSITE; PS00066; HMG_COA_REDUCTASE_1; FALSE_NEG.
DR   PROSITE; PS00318; HMG_COA_REDUCTASE_2; FALSE_NEG.
DR   PROSITE; PS01192; HMG_COA_REDUCTASE_3; FALSE_NEG.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    431       Probable 3-hydroxy-3-methylglutaryl-
FT                                coenzyme A reductase.
FT                                /FTId=PRO_0000114466.
FT   ACT_SITE     85     85       Charge relay system (By similarity).
FT   ACT_SITE    278    278       Charge relay system (By similarity).
FT   ACT_SITE    375    375       Proton donor (By similarity).
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
//