HMDH1_HEVBR
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 25-MAY-2022, entry version 119.
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 + 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; 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 OrthoDB; 907394at2759; -.
DR UniPathway; UPA00058; UER00103.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 1.10.3270.10; -; 1.
DR Gene3D; 3.30.70.420; -; 1.
DR Gene3D; 3.90.770.10; -; 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 PANTHER; PTHR10572; PTHR10572; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; SSF55035; 1.
DR SUPFAM; SSF56542; SSF56542; 1.
DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 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..18
FT /note="Basic and acidic 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
