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Database: UniProt
Entry: B6AZ98_9RHOB
LinkDB: B6AZ98_9RHOB
Original site: B6AZ98_9RHOB 
ID   B6AZ98_9RHOB            Unreviewed;       435 AA.
AC   B6AZ98;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=RB2083_3787 {ECO:0000313|EMBL:EDZ44272.1};
OS   Rhodobacteraceae bacterium HTCC2083.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ44272.1, ECO:0000313|Proteomes:UP000005746};
RN   [1] {ECO:0000313|Proteomes:UP000005746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX   PubMed=21036993; DOI=10.1128/JB.01268-10;
RA   Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT   Roseobacter.";
RL   J. Bacteriol. 193:319-320(2011).
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}.
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DR   EMBL; DS995276; EDZ44272.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AZ98; -.
DR   STRING; 314270.RB2083_3787; -.
DR   eggNOG; COG1257; Bacteria.
DR   HOGENOM; CLU_033422_0_0_5; -.
DR   OrthoDB; 9764892at2; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000005746; 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   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; PS00066; HMG_COA_REDUCTASE_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005746}.
SQ   SEQUENCE   435 AA;  45329 MW;  547AA792A6E3CE71 CRC64;
     MSEVPTRSQA FVSSRLDGFR HFEPKDRLAT LTKMAGLSSA DQIALGGIDA LPVELANGMI
     ENVIGKFEIP LGVATNFTVN GRDYLVPMAV EEPSVVAAAS YMAKIARGCG GFSSSSTRPI
     MRAQVQILGL ADPHGARMRI LEAADALIAL ANSRDKVLIG LGGGCTEIEV HIFDDTPIGP
     MVVLHLLVDV RDAMGANTVN TMAEMVAPKV EEITGGNVRL RILSNLADKR LVRARVSITP
     AALSTETLDG AEVARGITEA CALAIVDPYR ATTHNKGIMN GIDPVVIATG NDWRAVEAGA
     HAWAARSGRY TSLSRWEVAS SGNLIGTLEL PMALGIVGGA TKTHPAAQAA LRLMGVTSAT
     KLAEVTVAVG LAQNMAALRA LSTEGIQKGH MALHARNIAI TAGAKGQAVD LVAKALVAAG
     DVSVDKAKDV LSQIT
//
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