HMDH1_GOSHI
ID HMDH1_GOSHI Reviewed; 585 AA.
AC O64966;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
DE Short=HMG-CoA reductase 1;
DE EC=1.1.1.34;
GN Name=HMG1;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Acala SJ2;
RA Loguercio L.L., Wilkins T.A.;
RT "Two genomic clones encoding 3-hydroxy-3-methylglutaryl-coenzyme A
RT reductase from cotton (Gossypium hirsutum L.).";
RL (er) Plant Gene Register PGR98-031(1998).
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; AF038045; AAC05088.1; -; Genomic_DNA.
DR PIR; T09782; T09782.
DR AlphaFoldDB; O64966; -.
DR SMR; O64966; -.
DR PRIDE; O64966; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000189702; Genome assembly.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
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;
KW Mitochondrion; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..585
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 1"
FT /id="PRO_0000114438"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 98..169
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 170..585
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 472
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 570
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 62835 MW; 1350E7A9168EBE42 CRC64;
METHRRSSTN SIRSHKPARP IALEDDSTKA SDALPLPLYL TNAVFFTLFF SAVYFLLCRW
REKIRSSTPL HVVTFSEIVA ILASVASFIY LLGFFGIDFV QSLVLRPSAD VWATEDDEVE
SEVLLRNEDA RHVPCGQALD RSIRSLQPPE PIVTAEKVFD EMPVTVMTEE DEEIIRSVVC
GMTPSYSLES KLDDCKRAAA IRREALQRIT GKSLSGLPLD GFDYESILGQ CCEMPVGYEQ
IPVGIAGPLL LNGREYSVPM ATTEGCLVAS TNRGCKAIHL SGGATSVLLR DGMTRAPVVR
FGTAKRAADL KLYLEDPENF ETLACVFNRS SRFARLQSIK CAIAGKNLYL RFSCFTGDAM
GMNMVSKGVQ NVLDFLQTDF PDMDVIGISG NFCSDKKPAA VNWIEGRGKS VVCEAIINGD
VVTKVLKTSV ESLVELNMLK NLTGSAMAGA LGGFNAHASN IVTAVYIATG QDPAQNVESS
HCITMMEAVN GGKDLHVSVT MPSIEVGTVG GGTQLASQSA CLNLLGVKGA SKESPGANSI
LLATIVAGAV LAGELSLMSA LAAGQLVKSH MKYNRSSKDV SKVSS
