HMDH3_ORYSJ
ID HMDH3_ORYSJ Reviewed; 561 AA.
AC Q9XHL5; Q6Z8N5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=HMG3; Synonyms=HMGR3; OrderedLocusNames=Os08g0512700, LOC_Os08g40180;
GN ORFNames=P0711H09.15;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ha S.-H., Lee S.-W., Hwang Y.-S.;
RT "Isolation and characterization of two differentially expressed hydroxy-
RT methylglutaryl-CoA reductase genes from rice.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-561.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF110382; AAD38873.1; -; Genomic_DNA.
DR EMBL; AP004765; BAD10066.1; -; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK060545; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015648250.1; XM_015792764.1.
DR AlphaFoldDB; Q9XHL5; -.
DR SMR; Q9XHL5; -.
DR STRING; 4530.OS08T0512700-01; -.
DR PaxDb; Q9XHL5; -.
DR PRIDE; Q9XHL5; -.
DR GeneID; 4346017; -.
DR KEGG; osa:4346017; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_2_0_1; -.
DR InParanoid; Q9XHL5; -.
DR OrthoDB; 907394at2759; -.
DR PlantReactome; R-OSA-1119615; Mevalonate pathway.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q9XHL5; OS.
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..561
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 3"
FT /id="PRO_0000114447"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 90..145
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..561
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 448
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 546
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 119..121
FT /note="PPP -> RA (in Ref. 1; AAD38873)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="V -> E (in Ref. 1; AAD38873)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="A -> R (in Ref. 1; AAD38873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 59401 MW; B2A826D6A1BA0B1C CRC64;
MEVRRRAPLP PPPGRVQAGD ALPLPIRHTN LIFSALFAAS LAYLMRRWRE KIRSSTPLHV
VGLAEMLAIF GLVASLIYLL SFFGIAFVQS IVSSSDDEEE DFLVGPARGS SAAAAVAPPP
PPSSPAQCSL LGSPHDDAAR ERMPEEDEEI VSSVVAGKVP SYVLETKLGD CRRAAGIRRE
AVRRITGRQI EGLPLDGFDY ASILGQCCEL PVGYVQLPVG IAGPLLLDGQ RFYVPMATTE
GCLVASTNRG CKAIAESGGA VSVVLRDGMT RAPVARLPTA RRAAELKAFL EDSVNFNTLS
MVFNRSSRFA RLQGVQCAMA GRNLYMRFSC CTGDAMGMNM VSKGVQNVLD YLQDDFPDMD
VISISGNFCS DKKPAAVNWI EGRGKSVVCE AVIKEDVVKK VLKTNVQSLV ELNVIKNLAG
SAVAGALGGF NAHASNIVTA IFIATGQDPA QNVESSHCIT MLEAVNDGRD LHISVTMPSI
EVGTVGGGTQ LASQAACLDL LGVKGANRES PGSNARLLAT VVAGGVLAGE LSLLSALAAG
QLVKSHMKYN RSSKDMSKVI S
