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Database: UniProt
Entry: HMDH1_ORYSJ
LinkDB: HMDH1_ORYSJ
Original site: HMDH1_ORYSJ 
ID   HMDH1_ORYSJ             Reviewed;         532 AA.
AC   Q0DY59; P48019;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
DE            Short=HMG-CoA reductase 1;
DE            EC=1.1.1.34;
GN   Name=HMG1; OrderedLocusNames=Os02g0713900, LOC_Os02g48330;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Catalyzes the synthesis of mevalonate. The specific precursor
CC       of all isoprenoid compounds present in plants.
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:0000255|PROSITE-ProRule:PRU10003};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF09829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP008208; BAF09829.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015623837.1; XM_015768351.1.
DR   AlphaFoldDB; Q0DY59; -.
DR   SMR; Q0DY59; -.
DR   STRING; 39947.Q0DY59; -.
DR   GlyCosmos; Q0DY59; 2 sites, No reported glycans.
DR   PaxDb; 39947-Q0DY59; -.
DR   GeneID; 9272427; -.
DR   KEGG; osa:9272427; -.
DR   eggNOG; KOG2480; Eukaryota.
DR   InParanoid; Q0DY59; -.
DR   OrthoDB; 816560at2759; -.
DR   PlantReactome; R-OSA-1119615; Mevalonate pathway.
DR   UniPathway; UPA00058; UER00103.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
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:SF14; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 1"
FT                   /id="PRO_0000114446"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          77..117
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          78..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..532
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        419
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        517
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   532 AA;  55615 MW;  D70406C15BA50127 CRC64;
     MDVRRGGGGG RIVGAARRAL TWGALPLPMR ITNGLAMVSL VLSSCDLLRL CSDRERPLGG
     REFATVVYLV SLFAHPDAPA TTTGDDDDGQ GGSRRARPAA AEPAPMHGHG GGMMEADDEE
     IVAAVASGAL PSHRLESRLG DCRRAARLRR EALRRVTGRG VEGLPFDGMD YQAILGQCCE
     MPVGYVQLPV GVAGPLLLDG REYHVPMATT EGCLVASVNR GCRAISASGG AFSVLLRDAM
     SRAPAVKLPS AMRAAELKAF AEAPANFELL AAVFNRSSRF GRLQDIRCAL AGRNLYMRFS
     CITGDAMGMN MVSKGVENVL GYLQNVFPDM DVISVSGNYC SDKKPTAVNW IEGRGKSVVC
     EAIIKGDVVQ KVLKTTVEKL VELNIIKNLA GSAVAGALGG FNAHASNIVT ALFIATGQDP
     AQNVESSQCI TMLEEVNDGD DLHISVTMPS IEVGTIGGGT CLASQAACLN LLGVKGSNHG
     SPGANAKRLA TIVAGSVLAG ELSLLAALAS GHLVKSHMMY NRSSKDVAKA AS
//
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