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Database: UniProt
Entry: A0A059B9N3_EUCGR
LinkDB: A0A059B9N3_EUCGR
Original site: A0A059B9N3_EUCGR 
ID   A0A059B9N3_EUCGR        Unreviewed;       596 AA.
AC   A0A059B9N3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=1.1.1.34 {ECO:0000256|RuleBase:RU361219};
GN   ORFNames=EUGRSUZ_H05009 {ECO:0000313|EMBL:KCW62370.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW62370.1};
RN   [1] {ECO:0000313|EMBL:KCW62370.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW62370.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC         methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
CC         Evidence={ECO:0000256|RuleBase:RU361219};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005084, ECO:0000256|RuleBase:RU361219}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361219}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
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; KK198760; KCW62370.1; -; Genomic_DNA.
DR   RefSeq; XP_010025658.1; XM_010027356.2.
DR   AlphaFoldDB; A0A059B9N3; -.
DR   STRING; 71139.A0A059B9N3; -.
DR   EnsemblPlants; KCW62370; KCW62370; EUGRSUZ_H05009.
DR   GeneID; 104415929; -.
DR   Gramene; KCW62370; KCW62370; EUGRSUZ_H05009.
DR   KEGG; egr:104415929; -.
DR   eggNOG; KOG2480; Eukaryota.
DR   InParanoid; A0A059B9N3; -.
DR   OMA; GCKAIAM; -.
DR   OrthoDB; 816560at2759; -.
DR   UniPathway; UPA00058; UER00103.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR   CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR   Gene3D; 1.10.3270.10; HMGR, N-terminal domain; 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; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR   InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR   InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR   InterPro; IPR023282; HMG_CoA_Rdtase_N.
DR   InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR   InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR   NCBIfam; TIGR00533; HMG_CoA_R_NADP; 1.
DR   PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   PANTHER; PTHR10572:SF44; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE 1; 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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU361219};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Membrane {ECO:0000256|RuleBase:RU361219};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU361219};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361219};
KW   Transmembrane {ECO:0000256|RuleBase:RU361219};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361219"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361219"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  63669 MW;  725B2B01B29AA9F0 CRC64;
     MDVRRRPSKP VAAVDSPKPK AKRSPSPLKH SVDEDTSLKV PLSLYLLNAS VICAFFTLLC
     YLLSRWHDKM RSSSPFHVLS TLELAAFVAF AASFVYLLIF FGVEFFRSLL LRPSSDLWAD
     DCEDEKVVSV VAEGFLQKAP CGQALDGETP KLDFDPVKPA APKAKPVETE KWDEQIDLSE
     EDEEVIASVV AGTTPSYSLE SKLGDCRRAA AVRREALQRM TGKSLAGLPL EGFDYESILG
     QCCEMPVGYV QIPVGIAGPL ELDGREYSVP MATTEGCLVA STNRGCKAIA MSGGANSILL
     RDGMTRAPVV RFGLAKRAAE LKFYLESPAN FEALSSVFNS SSRFARLQSI KGAIAGKNLY
     LRFSCSTGDA MGMNMVSKGV QNIMDFLQKD FPDMDVMGIS SNFCSDKKPA AVNWIEGRGK
     SVVCEAVIKG DVVRKVLKTS VEALVELNML KNLTGSAMAG ALGGFNAHAS NIVTAIYIAT
     GQDPAQNVES SHCITMMEAV NDGKDLHVSV TMPSIEVGTV GGGTQLASQS ACLNLLGVKG
     ANREAPGSNS RLLATVVAGS VLAGELSLMS ALAAGQLVKS HMKYNRSNKA ASKVSS
//
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