HMR2B_PANGI
ID HMR2B_PANGI Reviewed; 589 AA.
AC U5JCC6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase 2-B {ECO:0000305|Ref.1};
DE Short=HMG-CoA reductase 2 {ECO:0000303|Ref.1};
DE Short=Hydroxymethylglutaryl-CoA reductase {ECO:0000255|PROSITE-ProRule:PRU10003};
DE Short=PgHMGR2 {ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1};
DE EC=1.1.1.34 {ECO:0000255|PROSITE-ProRule:PRU10003};
GN Name=HMGR2 {ECO:0000303|Ref.1};
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].
RA Luo H., Chen S.;
RT "Cloning and expression analysis of PgHMGR2 gene in Panax ginseng.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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, AND NOMENCLATURE.
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:29378087). Promotes
CC triterpenes accumulation in roots (By similarity).
CC {ECO:0000250|UniProtKB:A0A0A1C3I2, ECO:0000250|UniProtKB:P14891,
CC 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 -!- 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:0000305}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; JX648390; AGL08682.1; -; mRNA.
DR AlphaFoldDB; U5JCC6; -.
DR SMR; U5JCC6; -.
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: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; NADP;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="3-hydroxy-3-methylglutaryl coenzyme A reductase 2-B"
FT /id="PRO_0000446948"
FT TOPO_DOM 1..35
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..544
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 400
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 476
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 574
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 589 AA; 62906 MW; 4638B7A92BBD3812 CRC64;
MDVRRRPVTK TLTAGEPLKS QNQHSSSLKA SDALPLPLYL TNGLFFTMFF SVMYFLLHRW
REKIRNSVPL HVVTLSELAA LVLLVASVIY LLGFFGIGFV QSLIRPSPDS WDILEDDNAI
LEEDSRCEPC AAAIDCSLPP NLKIARMVPQ KHKSAFADVV EEQKQSASAT IIDEDEEIIN
AVVAGTTPSY SLESKLGDCL KAAAIRREAL QRITGKSLDG LPLDGFDYES ILGQCCEMPV
GYVQVPVGIA GPLLLNETEY SVPMATTEGC LVASTNRGCK AIYASGGATS VLLKDGMTRA
PVVRFGSAKR AAELKFFLED PMNFETLALV FNKSSRFGRL QGIKCAIAGK NLYMRFTCST
GDAMGMNMVS KGVQNVLDFL QNDFPDMDVM GISGNYCSDK KPAAVNWIEG RGKSVVCEAI
IKEEVVKKVL KTNVAALVEL NMLKNLAGSA VAGALGGFNA HASNIVSAVY VAAGQDPAQN
IESSHCITMM EAVNDGKDLH ISVTMPSIEV GTVGGGTQLA SQSACLNLLG VKGASKESPG
PNSRLLASIV AGSVLAGELS LMSALAAGQL VKSHMKFNRS SKDVSKLSS
