ID   HMDH1_HEVBR             Reviewed;         575 AA.
AC   P29057;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 129.
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=HMGR1;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. RRIM 600; TISSUE=Leaf;
RX   PubMed=1714317; DOI=10.1007/bf00023422;
RA   Chye M.L., Kush A., Tan C.T., Chua N.H.;
RT   "Characterization of cDNA and genomic clones encoding 3-hydroxy-3-
RT   methylglutaryl-coenzyme A reductase from Hevea brasiliensis.";
RL   Plant Mol. Biol. 16:567-577(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Venkatachalam P., Priya P., Thulaseedharan A.;
RT   "Cloning and nucleotide sequence analysis of HMGR1 gene in Hevea
RT   brasiliensis.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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 + 2 NADP(+) + CoA = (3S)-3-hydroxy-3-
CC         methylglutaryl-CoA + 2 NADPH + 2 H(+); 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; Multi-pass
CC       membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
CC       Plastid membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR   EMBL; X54657; CAA38467.1; -; Genomic_DNA.
DR   EMBL; X54659; CAA38469.1; -; mRNA.
DR   EMBL; AY352338; AAQ63055.1; -; Genomic_DNA.
DR   PIR; S14955; S14955.
DR   AlphaFoldDB; P29057; -.
DR   SMR; P29057; -.
DR   GlyCosmos; P29057; 3 sites, No reported glycans.
DR   OrthoDB; 310654at2759; -.
DR   UniPathway; UPA00058; UER00103.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:TreeGrafter.
DR   GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR   FunFam; 1.10.3270.10:FF:000002; 3-hydroxy-3-methylglutaryl coenzyme A reductase; 1.
DR   FunFam; 3.30.70.420:FF:000001; 3-hydroxy-3-methylglutaryl coenzyme A reductase; 1.
DR   FunFam; 3.90.770.10:FF:000001; 3-hydroxy-3-methylglutaryl coenzyme A reductase; 1.
DR   Gene3D; 3.90.770.10; 3-hydroxy-3-methylglutaryl-coenzyme A Reductase, Chain A, domain 2; 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: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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane;
KW   Mitochondrion; NADP; Oxidoreductase; Plastid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..575
FT                   /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 1"
FT                   /id="PRO_0000114440"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..160
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          161..575
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..13
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        386
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        462
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        560
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   575 AA;  61695 MW;  BC0A74898B6124D5 CRC64;
     MDTTGRLHHR KHATPVEDRS PTTPKASDAL PLPLYLTNAV FFTLFFSVAY YLLHRWRDKI
     RNSTPLHIVT LSEIVAIVSL IASFIYLLGF FGIDFVQSFI ARASHDVWDL EDTDPNYLID
     EDHRLVTCPP ANISTKTTII AAPTKLPTSE PLIAPLVSEE DEMIVNSVVD GKIPSYSLES
     KLGDCKRAAA IRREALQRMT RRSLEGLPVE GFDYESILGQ CCEMPVGYVQ IPVGIAGPLL
     LNGREYSVPM ATTEGCLVAS TNRGCKAIYL SGGATSVLLK DGMTRAPVVR FASATRAAEL
     KFFLEDPDNF DTLAVVFNKS SRFARLQGIK CSIAGKNLYI RFSCSTGDAM GMNMVSKGVQ
     NVLEFLQSDF SDMDVIGISG NFCSDKKPAA VNWIEGRGKS VVCEAIIKEE VVKKVLKTNV
     ASLVELNMLK NLAGSAVAGA LGGFNAHAGN IVSAIFIATG QDPAQNVESS HCITMMEAVN
     DGKDLHISVT MPSIEVGTVG GGTQLASQSA CLNLLGVKGA NKESPGSNSR LLAAIVAGSV
     LAGELSLMSA IAAGQLVKSH MKYNRSSKDM SKAAS
//