HMDH3_SOLTU
ID HMDH3_SOLTU Reviewed; 574 AA.
AC Q41438;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 3;
DE Short=HMG-CoA reductase 3;
DE EC=1.1.1.34;
DE AltName: Full=HMG3.3;
GN Name=HMG3;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Itoh Y., Yoshioka H., Doke N.;
RT "Structure and nucleotide sequence of potato HMG3 encoding 3-hydroxy-3-
RT methylglutaryl coenzyme A reductase.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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 mature petals and anthers.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; U51986; AAB52552.1; -; mRNA.
DR EMBL; AB022690; BAA93631.1; -; Genomic_DNA.
DR PIR; S59946; S59946.
DR PIR; T07112; T07112.
DR RefSeq; NP_001274940.1; NM_001288011.1.
DR AlphaFoldDB; Q41438; -.
DR SMR; Q41438; -.
DR STRING; 4113.PGSC0003DMT400048075; -.
DR EnsemblPlants; PGSC0003DMT400048075; PGSC0003DMT400048075; PGSC0003DMG400018679.
DR GeneID; 102577467; -.
DR Gramene; PGSC0003DMT400048075; PGSC0003DMT400048075; PGSC0003DMG400018679.
DR KEGG; sot:102577467; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_2_2_1; -.
DR InParanoid; Q41438; -.
DR OMA; MMEAING; -.
DR OrthoDB; 907394at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q41438; 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..574
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 3"
FT /id="PRO_0000114450"
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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..161
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 162..574
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 562
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 574 AA; 62159 MW; E020BB10EF4779E4 CRC64;
MDVRRRPVKP LYPSEHISSG EPLKPHNQDS SVKASDALPL PLYLTNGLFF TMFFSVMYFL
LHRWREKIRN GIPLHVLNFS ELVAMVSLIA SVIYLLGFFG IGFVQSFVSK GNNDSWDVED
ESPEQFIDRT VTPPPVRRNI PMKSVPVAEK TAQIITPFSS EDDEVVIKSV VEGRIPSYSL
ESKLGDCKRA AFIRKEALQR SSGKSLEGLP LDGFDYESIL GQCCEMPIGY IQIPVGIAGP
LLLNGKEFSV PMATTEGCLV ASTNRGCKAI YVSGGATSVL FRDAMTRAPV VRFGSAKRAA
ELKFFVEDPM NFETLSVVFN KSSRFARLQN IQCAIAGKNL YMRFSCSTGD AMGMNMVSKG
VQNVLDYLQN EYPDMDIIGI SGNYCSDKKP AAVNWIEGRG KSVVCEAIIK EDVVKKVLKT
EVATLVELNM LKNLTGSAMA GALGGFNAHA SNIVSAVYLA TGQDPAQNIE SSHCITMMEA
VNDGKDLHIS VTMPSIEVGT VGGGTQLASQ SACLNLLGVK GANREAPGSN ARLLATIVAG
SVLAGELSLM SAISAGQLVK SHMKYNRSCK DVTK
