HMDH_NICSY
ID HMDH_NICSY Reviewed; 604 AA.
AC Q01559;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE Short=HMG-CoA reductase;
DE EC=1.1.1.34;
GN Name=HMGR;
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Protoplast;
RX PubMed=1391779; DOI=10.1007/bf00014504;
RA Genschik P., Criqui M.-C., Parmentier Y., Marbach J., Durr A., Fleck J.,
RA Jamet E.;
RT "Isolation and characterization of a cDNA encoding a 3-hydroxy-3-
RT methylglutaryl coenzyme A reductase from Nicotiana sylvestris.";
RL Plant Mol. Biol. 20:337-341(1992).
CC -!- FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor
CC of all isoprenoid compounds present in plants. Possible role in plant
CC defense mechanisms as well as in the cell cycle.
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.
CC -!- TISSUE SPECIFICITY: Found in protoplasts and leaves submitted to
CC stress. Low levels found in apexes, anthers and roots.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels during the G0-G1
CC transition in the cell cycle of mesophyll protoplasts.
CC -!- INDUCTION: In leaves, by wounding, elicitation, bacterial or fungal
CC infection.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; X63649; CAA45181.1; -; mRNA.
DR PIR; S24760; S24760.
DR RefSeq; NP_001289522.1; NM_001302593.1.
DR AlphaFoldDB; Q01559; -.
DR SMR; Q01559; -.
DR ELM; Q01559; -.
DR STRING; 4096.XP_009781350.1; -.
DR GeneID; 104230282; -.
DR eggNOG; KOG2480; Eukaryota.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000189701; Unplaced.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..604
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase"
FT /id="PRO_0000114445"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..189
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 190..604
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 589
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 604 AA; 65085 MW; 7046D17CAC0D0BA4 CRC64;
MDVRRRSEKP AYPTKEFAAG EKPLKPHKQQ QEQDNSLLIA SDALPLPLYL TNGLFFTMFF
SVMYYLLSRW REKIRNSTPL HVVTFSELVA IASLIASVIY LLGFFGIGFV QSFVSRDNND
ECWDEEDEND EQFLLEEDSR RGPATTLGCT AVPPPPALQI VPMVPPQPSK VAAMSEKPAP
LVTPAASEED EEIIKSVVQG KMPSYSLESK LGDCKRAASI RKEALQRITG KSLEGLPLEG
FDYESILGQC CEMPIGYVQI PVGIAGPLLL DGREYSVPMA TTEGCLVAST NRGCKAIYAS
GGATSVLLRD GMTRAPCVRF GTAKRAAELK FFVEDPVKFE TLAAVFNQSS RFARLQRIQC
AIAGKNLYMR FVCSTGDAMG MNMVSKGVQN VLDYLQNEYP DMDVIGISGN FCSDKKPAAV
NWIEGRGKSV VCEAIITEEV VKKVLKTEVA ALVELNMLKN LTGSAMAGAL GGFNAHASNI
VSAVYIATGQ DPAQNIESSH CITMMEAVND GKDLHVSVTM PSIEVGTVGG GTQLASQSAC
LNLLGVKGAN REVPGSNARL LATIVAGSVL AGELSLMSAI SAGQLVKSHM KYNRSTKDVT
KASS
