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HMDH_MAIZE
ID   HMDH_MAIZE              Reviewed;         579 AA.
AC   O24594;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
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   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. LG 21-11;
RA   Mayer M.J., Steel J., Bailey J.A., Hargreaves J.A.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR   EMBL; Y09238; CAA70440.1; -; Genomic_DNA.
DR   PIR; T04357; T04357.
DR   AlphaFoldDB; O24594; -.
DR   SMR; O24594; -.
DR   STRING; 4577.GRMZM2G393337_P02; -.
DR   PaxDb; O24594; -.
DR   PRIDE; O24594; -.
DR   eggNOG; KOG2480; Eukaryota.
DR   UniPathway; UPA00058; UER00103.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; O24594; 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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..579
FT                   /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase"
FT                   /id="PRO_0000114444"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..153
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          154..579
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          555..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        247
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        455
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        553
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   579 AA;  60931 MW;  ECA693F232EB2B6A CRC64;
     MEVRGGVGQG SAARHPPAPE PSRAAARVQA GDALPLPIRH TNLIFSALFA ASLAYLMRRW
     REKIRSSTPL HAVGLAEMLA IFGLVASLIY LLSFFGIAFV QSIVSSGDDD EDFLVGSGSS
     GSAAAPSRQH AQAPAPCELL GSPAAAPEKM PEDDEEIVAS VVAGKVPSYA LEARLGDCRR
     AAGIRREALR RITGRDIEGL PLDGFDYASI LGQCCELPVG YVQLPVGVAG PLLLDGRRFY
     LPMATTEGCL VASTNRGCKA IAESGGATSV VLRDAMTRAP VARFPTARRA AELKAFLEDP
     ANFDTLSVVF NRSSRFARLQ GVQCAMAGRN LYMRFSCSTG DAMGMNMVSK GVQNVLDFLQ
     DDFHDMDVIS ISGNFCSDKK PSAVNWIEGR GKSVVCEAVI GEEVVKKVLK TDVQSLVELN
     TIKNLAGSAV AGALGGFNAH ASNIVTAIFI ATGQDPAQNV ESSHCITMLE PVNAGRDLHI
     SVTMPSIEVG TVGGGTQLAS QSACLDLLGV RGASRDRPGS NARLLATVVA GGVLAGELSL
     LSALAAGQLV KSHMKYNRSS KDVSSTTATE KTRQREVDV
 
 
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