HMDH1_SOLTU
ID HMDH1_SOLTU Reviewed; 596 AA.
AC P48020;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
DE Short=HMG-CoA reductase 1;
DE Short=HMGR;
DE Short=HMGR1;
DE EC=1.1.1.34;
GN Name=HMG1;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kennebec; TISSUE=Tuber;
RX PubMed=1283354; DOI=10.2307/3869418;
RA Choi D., Ward B.L., Bostock R.M.;
RT "Differential induction and suppression of potato 3-hydroxy-3-
RT methylglutaryl coenzyme A reductase genes in response to Phytophthora
RT infestans and to its elicitor arachidonic acid.";
RL Plant Cell 4:1333-1344(1992).
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.
CC -!- TISSUE SPECIFICITY: Expressed in flower primordia and anthers.
CC -!- INDUCTION: Induced by wounding. This enhancement is greatly reduced by
CC treatment with arachidonic acid or after inoculation with the fungal
CC pathogen, P.infestans.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; L01400; AAA93498.1; -; mRNA.
DR PIR; S59944; S59944.
DR RefSeq; NP_001275461.1; NM_001288532.1.
DR AlphaFoldDB; P48020; -.
DR SMR; P48020; -.
DR STRING; 4113.PGSC0003DMT400035542; -.
DR GeneID; 102577654; -.
DR KEGG; sot:102577654; -.
DR eggNOG; KOG2480; Eukaryota.
DR InParanoid; P48020; -.
DR OrthoDB; 907394at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P48020; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
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; 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..596
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 1"
FT /id="PRO_0000114448"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..183
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 184..596
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 486
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 584
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 63917 MW; 4E7060D3ADC6EE60 CRC64;
MDVRRRPVKP LYTSKDASAG EPLKQQEVSS PKASDALPLP LYLTNGLFFT MFFSVMYFLL
VRWREKIRNS IPLHVVTLSE LLAMVSLIAS VIYLLGFFGI GFVQSFVSRS NSDSWDIEDE
NAEQLIIEED SRRGPCAAAT TLGCVVPPPP VRKIAPMVPQ QPAKVALSQT EKPSPIIMPA
LSEDDEEIIQ SVVQGKTPSY SLESKLGDCM RAASIRKEAL QRITGKSLEG LPLEGFDYSS
ILGQCCEMPV GYVQIPVGIA GPLLLDGREY SVPMATTEGC LVASTNRGCK AIFVSGGADS
VLLRDGMTRA PVVRFTTAKR AAELKFFVED PLNFETLSLM FNKSSRFARL QGIQCAIAGK
NLYITFSCST GDAMGMNMVS KGVQNVLDYL QSEYPDMDVI GISGNFCSDK KPAAVNWIEG
RGKSVVCEAI IKEEVVKKVL KTEVAALVEL NMLKNLTGSA MAGALGGFNA HASNIVSAVY
LATGQDPAQN VESSHCITMM EAVNDGKDLH VSVTMPSIEV GTVGGGTQLA SQSACLNLLG
VKGANRDAPG SNARLLATIV AGSVLAGELS LMSAISAGQL VKSHMKYNRS IKDISK
