HMR2A_PANGI
ID HMR2A_PANGI Reviewed; 594 AA.
AC A0A0A1C930;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase 2-A {ECO:0000305|PubMed:24569845};
DE Short=HMG-CoA reductase 2 {ECO:0000303|PubMed:24569845};
DE Short=Hydroxymethylglutaryl-CoA reductase {ECO:0000255|PROSITE-ProRule:PRU10003};
DE Short=PgHMGR2 {ECO:0000303|PubMed:24569845};
DE EC=1.1.1.34 {ECO:0000255|PROSITE-ProRule:PRU10003};
GN Name=HMGR2 {ECO:0000303|PubMed:24569845};
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP ACTIVITY REGULATION, INDUCTION BY METHYL JASMONATE, AND SUBCELLULAR
RP 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 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 [3]
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).
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). {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:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast membrane
CC {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:A0A0A1C3I2};
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,
CC seedlings and roots, and, to a lower extent, in seeds, leaves, stems
CC and flowers. {ECO:0000269|PubMed:24569845}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively in mature roots.
CC {ECO:0000269|PubMed:24569845}.
CC -!- INDUCTION: Repressed by darkness in roots and leaves, but increased
CC ginsenosides accumulation. Repressed transiently by mevinolin (Mev).
CC {ECO:0000269|PubMed:24569845}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; KM386695; AIX87980.1; -; mRNA.
DR AlphaFoldDB; A0A0A1C930; -.
DR SMR; A0A0A1C930; -.
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: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..594
FT /note="3-hydroxy-3-methylglutaryl coenzyme A reductase 2-A"
FT /id="PRO_0000446947"
FT TOPO_DOM 1..37
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..549
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:24569845"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24569845"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 405
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 481
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 579
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 594 AA; 63621 MW; 73BD4A202C5A5DE3 CRC64;
MDVRRRPVKS LSSAKTATAG EPPKSQQQHP KASDALPLPL YLTNGLFFTM FFSVMYFLLH
RWREKIRNST PLHVVTLSEL AALVLLMASV IYLLGFFGIG FVRSVIRPSP DAWDILEDDN
AINEEDSRRE PCAEAIDCSL PPKPKIVHMV PQKALNPKSA FADMMVEQPA LAIAPLTEED
EEIVKSVVTG KIPSYSLESK LGDCKKAASI RREALQRITG KSLAGLPLDG FDYKSILGQC
CEMPVGYVQI PVGIAGPLLL NETEYSVPMA TTEGCLVAST NRGCKAIYAS GGATSVLLRD
GMTRAPVVRF STVKRAAELK FFLEEPLNYD TPAHVFNKSS RFGRLQGIKC AVAGKNLYIR
FTCSTGDAMG MNMVSKGVQN VLDFLQSDFP DMDVMGISGN YCSDKKPAAV NWIEGCGKSV
VCEAIIKEEV VKKVLKTNVA ALVELNMLKN LAGSAVAGAL GGFNAHASNI VSAVYISTGQ
DPAQNVESSH CITMMEAVNN GKDLHISVTM PSIEVGTVGG GTQLASQSAC LNLLGVKGAS
KESPGSNSRL LASIVAGSVL AGELSLMSAL AAGQLVKSHM KYNRSSKDIT KLSS
