HMDH3_HEVBR
ID HMDH3_HEVBR Reviewed; 586 AA.
AC Q00583;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 3;
DE Short=HMG-CoA reductase 3;
DE EC=1.1.1.34;
GN Name=HMGR3;
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1377968; DOI=10.1007/bf00023395;
RA Chye M.L., Tan C.T., Chua N.H.;
RT "Three genes encode 3-hydroxy-3-methylglutaryl-coenzyme A reductase in
RT Hevea brasiliensis: hmg1 and hmg3 are differentially expressed.";
RL Plant Mol. Biol. 19:473-484(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. Mitochondrion membrane; Multi-pass membrane protein.
CC Plastid membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; M74800; AAA33360.1; -; mRNA.
DR EMBL; M74798; AAA33358.1; -; Genomic_DNA.
DR EMBL; M74799; AAA33359.1; -; Genomic_DNA.
DR PIR; S22521; S22521.
DR AlphaFoldDB; Q00583; -.
DR SMR; Q00583; -.
DR OrthoDB; 907394at2759; -.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
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;
KW Mitochondrion; NADP; Oxidoreductase; Plastid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..586
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 3"
FT /id="PRO_0000114442"
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000250"
FT REGION 108..170
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 171..586
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 172..586
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 473
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 571
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 586 AA; 62970 MW; 0B9D6DCC5979B456 CRC64;
MDEVRRRPPK HIVRKDHDGE VLNSFSHGHH LPPLKPSDYS LPLSLYLANA LVFSLFFSVA
YFLLHRWREK IRKSTPLHIV TFPEIAALIC LVASVIYLLG FFGIGFVHSF SRASTDSWDV
EEYDDDNIII KEDTRPTGAC AAPSLDCSLS LPTKIHAPIV STTTTSTLSD DDEQIIKSVV
SGSIPSYSLE SKLGNCKRAA LIRRETLQRM SGRSLEGLPL DGFDYESILG QCCEMAIGYV
QIPVGIAGPL LLDGKEYTVP MATTEGCLVA SANRGCKAIY ASGGATSVLL RDGMTRAPVV
RFPTAKRAAD LKFFMEDPDN FDTIAVVFNK SSRFARLQSV QCAIAGKNLY MRFSCSTGDA
MGMNMVSKAV QNVIDYLQND FPDMDVIGLT GNFCADKKAA AVNWIEGRGK SVVCEAIIKE
EVVKKVLKTN VAALVELNMI KNLTGSAVAG SLGGFNAHAS NMVTAVYIAT GQDPAQNVES
SHCITMMEAV NDGKDLHISV SMPSIELGTV GGGTQLASQS ACLNLLGVKG ASKDSPGSNS
RLLATIVAGS VLAGELSLMS AIAAGQLVNS HMKYNRSAKD VSKITF
