HMDH2_SOLTU
ID HMDH2_SOLTU Reviewed; 595 AA.
AC Q41437;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2;
DE Short=HMG-CoA reductase 2;
DE EC=1.1.1.34;
DE AltName: Full=HMG2.2;
GN Name=HMG2;
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=9049274; DOI=10.1023/a:1005743011651;
RA Korth K.L., Stermer B.A., Bhattacharyya M.K., Dixon R.A.;
RT "HMG-CoA reductase gene families that differentially accumulate transcripts
RT in potato tubers are developmentally expressed in floral tissues.";
RL Plant Mol. Biol. 33:545-551(1997).
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 young flowers and in mature sepals and
CC ovaries.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; U51985; AAB52551.1; -; mRNA.
DR RefSeq; NP_001275402.1; NM_001288473.1.
DR AlphaFoldDB; Q41437; -.
DR SMR; Q41437; -.
DR STRING; 4113.PGSC0003DMT400008902; -.
DR GeneID; 102577889; -.
DR KEGG; sot:102577889; -.
DR eggNOG; KOG2480; Eukaryota.
DR InParanoid; Q41437; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q41437; 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; 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..595
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 2"
FT /id="PRO_0000114449"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 113..183
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 184..595
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 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 595 AA; 63842 MW; 0FA7069849D41D57 CRC64;
MDVRRRSEKP VYPSKVFGAD EKPLKPHNNQ QQEDNNTLLI DASDALPLPL YLTNGLFFTM
FFSVMYFLLS RWREKIRNST PLHVVTLSEL GAIVSLIASV IYLLGFFGIG FVQTFVSRGN
NDSWDENDEE FLLKEDSRCG PATTLGCAIP APPARQISPM APPQPAMSMV EKPSPLITPA
SSEEDEEIIN SVVQGKFPSY SLVIQLGDVS AAASLRKEVM QRITGKSLEG LPLEGFTYES
ILGQCCEMPI GYVQIPVGIA GPLLLNGKEF SVPMATTEGC LVASTNRGCK AIYASGGATC
IVLRDGMTRA PCVRFGTAKR AAELKFFVED PIKFETLANV FNQSSRFGRL QRIQCAIAGK
NLYMRFVCST GDAMGMNMVS KGVQNVLDYL QNEYPDMDVI GISGNFCSDK KPAAVNWIEG
RGKSVVCEAI ITEEVVKKVL KTEVAALVEL NMLKNLTGSA MAGALGGFNA HASNIVSAVF
IATGQDPAQN IESSHCITMM EAVNDGKDLH ISVTMPSIEV GTVGGGTQLA SQSACLNLLG
VKGANREAPG SNARLLATVV AGSVLAGELS LMSAISAGQL VNSHMKYNRS TKASS
