HMDH2_CAPAN
ID HMDH2_CAPAN Reviewed; 604 AA.
AC Q9XEL8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2;
DE Short=HMG-CoA reductase 2;
DE EC=1.1.1.34;
GN Name=HMGR2;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ha S.H., Kim J.B., Lee S.W., Hwang Y.S.;
RT "Pathogen-inducible HMGR2 gene from hot pepper.";
RL Submitted (NOV-1998) 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; AF110383; AAD28179.1; -; mRNA.
DR AlphaFoldDB; Q9XEL8; -.
DR SMR; Q9XEL8; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000189700; Genome assembly.
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: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; NADP;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..604
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 2"
FT /id="PRO_0000114436"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 112..188
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 189..604
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 589
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 604 AA; 64881 MW; CCCE77884BC5A362 CRC64;
MDVRRRSEEA VYSSKVFAAD EKPLKPHKQQ QEEDNTLLID ASDALPLPLY FTNGLFFTMF
FSVMYFLLSR WREKIRNSTP LHVVTLSELG AIVSLIASVI YLLGFFGIGF VQTFVARGNN
DSWDEEDEND EQFILEEDSR RGPCAAATTL GCAVPTPPAK HIAPIVPQQP AVSIAEKPAP
LVTPAASEED EEIIKSVVQG KIPSYSLESK LGDCKRAASI RKEVLQRITG KSLEGLPLDG
FNYESILGQC CEMTIGYVQI PVGIAGPLLL NGREYSVPMA TTEGCLVAST NRGCKAIYAS
GGATSILLRD GMTRAPCVRF GTAKRAAELK FFVEDPINFE TLANVFNQSS RFARLQRIQC
AIAGKNLHMR FVCSTGDAMG MNMVSKGVQN VLDYLQNEYA DMDVIGISAN FCSDKKPAAV
NWIEGRGKSV VCEAIITEEV VKKVLKTEVA ALVELNMLKN LTGSALAGAL GGFNAHASNI
VSAVYIATGQ DPAQNIESSH CITMMEAVND GKDLHISVTM PSIEVGTVGG GTQLASQSAC
LNLLGVKGAN REAPGSNARL LATIVAGSVL AGELSLMSAI SAGQLVNSHM KYNRSTKDVT
KASS
