HMGR1_PANGI
ID HMGR1_PANGI Reviewed; 573 AA.
AC A0A0A1C3I2; A0A0N7APJ8; D0EAP5; F8QQQ8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase 1 {ECO:0000303|PubMed:24569845};
DE Short=HMG-CoA reductase 1 {ECO:0000303|PubMed:24569845};
DE Short=Hydroxymethylglutaryl-CoA reductase {ECO:0000255|PROSITE-ProRule:PRU10003};
DE Short=PgHMGR1 {ECO:0000303|PubMed:24569845};
DE EC=1.1.1.34 {ECO:0000255|PROSITE-ProRule:PRU10003};
GN Name=HMGR1 {ECO:0000303|PubMed:24569845, ECO:0000303|PubMed:30577538,
GN ECO:0000303|Ref.3}; Synonyms=HMGR {ECO:0000303|Ref.2};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, ACTIVITY REGULATION, INDUCTION BY DARKNESS AND METHYL JASMONATE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Yunpoong;
RX PubMed=24569845; DOI=10.1104/pp.113.222596;
RA Kim Y.-J., Lee O.R., Oh J.Y., Jang M.-G., Yang D.-C.;
RT "Functional analysis of 3-hydroxy-3-methylglutaryl coenzyme a reductase
RT encoding genes in triterpene saponin-producing ginseng.";
RL Plant Physiol. 165:373-387(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hou S., Han M., Liu C., Yang L.;
RT "Cloning and expression analysis of HMGR, SS, SE, DS, and bAS genes in
RT Panax ginseng.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim Y.K., Park S.U.;
RT "Cloning and characterization of 3-hydroxy-3-methylglutaryl coenzyme A
RT reductase (HMGR) in Panax ginseng.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [5]
RP REVIEW.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
RN [6]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ABIOTIC FACTORS.
RX PubMed=30577538; DOI=10.3390/molecules24010014;
RA Zhang T., Han M., Yang L., Han Z., Cheng L., Sun Z., Yang L.;
RT "The effects of environmental factors on ginsenoside biosynthetic enzyme
RT gene expression and saponin abundance.";
RL Molecules 24:0-0(2018).
CC -!- FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor
CC of all isoprenoid compounds present in plants (By similarity).
CC Component of the triterpene saponins (e.g. ginsenosides or panaxosides)
CC and phytosterols biosynthetic pathways (PubMed:24569845,
CC PubMed:29378087). Promotes triterpenes accumulation in roots
CC (PubMed:24569845). {ECO:0000250|UniProtKB:P14891,
CC ECO:0000269|PubMed:24569845, ECO:0000303|PubMed:29378087}.
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 -!- ACTIVITY REGULATION: Competitive inhibition by mevinolin (Mev) is
CC leading to a significant reduction of total ginsenoside in adventitious
CC roots. Triggered by darkness. {ECO:0000269|PubMed:24569845}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localized in
CC intracellular vesicles. {ECO:0000269|PubMed:24569845}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in the petioles of seedlings and
CC roots (both in main roots and lateral roots), and, to a lower extent,
CC in seeds, seedlings, leaves, stems and flowers.
CC {ECO:0000269|PubMed:24569845, ECO:0000269|PubMed:30577538}.
CC -!- DEVELOPMENTAL STAGE: Relatively constant levels in mature roots
CC (PubMed:24569845). Rapid decrease in roots and leaves from the leaf
CC opened to the green fruit stage (PubMed:30577538). At the leaf opened
CC stage, accumulates mostly in roots (PubMed:30577538).
CC {ECO:0000269|PubMed:24569845, ECO:0000269|PubMed:30577538}.
CC -!- INDUCTION: Induced in the hypocotyl of a 4 days-etiolated seedling and
CC reversed by light exposure within 2 hours. Inhibited by dark treatment
CC in 7-days-old seedling, where true leaves are emerged. Repressed by
CC darkness in roots and leaves, but increased ginsenosides accumulation.
CC Triggered by methyl jasmonate (MJ). Repressed transiently by mevinolin
CC (Mev) (PubMed:24569845). Influenced in roots by relative humidity and
CC photosynthetically active radiation (PAR), and in leaves by rain and
CC soil water potential (PubMed:30577538). {ECO:0000269|PubMed:24569845,
CC ECO:0000269|PubMed:30577538}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KM386694; AIX87979.1; -; mRNA.
DR EMBL; KJ939263; AJV26444.1; -; mRNA.
DR EMBL; GU565097; ADI80346.1; -; mRNA.
DR EMBL; GQ455990; ACW83617.1; -; mRNA.
DR AlphaFoldDB; A0A0A1C3I2; -.
DR SMR; A0A0A1C3I2; -.
DR UniPathway; UPA00058; UER00103.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0005778; C:peroxisomal 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:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0016135; P:saponin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IMP:UniProtKB.
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 Chloroplast; Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis;
KW Membrane; NADP; Oxidoreductase; Peroxisome; Plastid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..573
FT /note="3-hydroxy-3-methylglutaryl coenzyme A reductase 1"
FT /id="PRO_0000446946"
FT TOPO_DOM 1..45
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..528
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24569845"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 460
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 558
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 2..4
FT /note="DVR -> ETS (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..11
FT /note="KL -> IP (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="P -> L (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="I -> V (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> T (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="P -> L (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> T (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> F (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="FN -> SK (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> K (in Ref. 2; AJV26444)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="F -> L (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 345..347
FT /note="GDA -> VDV (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="I -> T (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="D -> E (in Ref. 3; ACW83617)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> E (in Ref. 3; ACW83617)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="N -> NH (in Ref. 3; ACW83617)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="L -> V (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="A -> S (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..456
FT /note="FIA -> YIP (in Ref. 3; ACW83617)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="H -> Q (in Ref. 3; ADI80346)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="N -> D (in Ref. 2; AJV26444 and 3; ADI80346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 61680 MW; 856C045EFA2261D3 CRC64;
MDVRRRLPPK LRRPLPITES SHHHRKTPFP ADVDRSPSPT PKASDALPLP LYLTNGIFFT
LFFSVAYYLL HRWRDKIRSS TPLHIVTLSE LAAIVSLIAS FIYLLGFFGI DFVQSFVSRA
DVDVDIDVEP DILEADRRPC SKLMDQPPPP PVVMSSEEDE EIVKSVVSGK TPSYSLESKL
GDCYRAASIR REAVQRTTGR SLLGLPLDGF DYESILGQCC EMPIGYVQIP VGIAGPLLLN
GCEYVVPMAT TEGCLVASTN RGCKAIYACG GATGILLKDG MTRAPVVRFS TAKRASDLKF
FLEDPLNFDT LAVVFNKSSR FARLQSIQCS MAGKNLYIRF CCSTGDAMGM NMVSKGVQNV
LEFLQSDFPD MDVIGISGNF CSDKKPAAVN WIEGRGKSVV CEAIITDDVV KKVLKTTVPA
LVELNMLKNL AGSAVAGALG GFNAHAANIV SAVFIATGQD PAQNIESSHC ITMMEAINNG
KDLHISVTMP SIEVGTVGGG TQLASQSACL NLLGVKGANK ESHGSNSRLL ATIVAGSVLA
GELSLMSAIA AGQLVRSHMK YNRSSRDMSK IGS
