HMDH2_GOSHI
ID HMDH2_GOSHI Reviewed; 628 AA.
AC O64967;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
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=HMG2;
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; AF038046; AAC05089.1; -; Genomic_DNA.
DR PIR; T09785; T09785.
DR RefSeq; XP_016674677.1; XM_016819188.1.
DR AlphaFoldDB; O64967; -.
DR SMR; O64967; -.
DR GeneID; 107894010; -.
DR KEGG; ghi:107894010; -.
DR OMA; DDKMTRA; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000189702; Chromosome 15.
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; 2.
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..628
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 2"
FT /id="PRO_0000114439"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 99..212
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 213..628
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 515
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 613
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 67603 MW; BF7704C30EA334F5 CRC64;
MEASRRSAVK PVIVLKPSKR FPLVEDTPGK ASDALPLPLY LTNAVFFTLF FTVVYFLLSR
WREKIRASIP LHAVTFPEIV AIFAFVASLI YLLGFFGIDF VQSLIIRPSG DVWSGEDYEE
ENEVLLHEED ARTVPCGQAL DCSVPSLPHM ARNVTAQRLF DEKPVRVATE EDARKVSCGQ
AVDCSLHSLP PRPPIVTSQK LFHEKTVIVT TEEDEEIIKS VVAGTLPSYS LESKLGDCKR
AAAIRREALQ RLTGRSLSGL PLDGFDYESI LGQCCEMPVG YVQIPVGIAG PLLLNGREYS
VPMATTEGCL VASTNRGCKA IHLSGGATSI LLKDGMTRAP VVRFSTAKRA AELKFYLEDP
ENFDTLAVVF NRSSRFGRLQ SIKCAIAGKN LYLRFTCSTG DAMGMNMVSK GVQNVLDFLQ
TDFPDMDVIG ISGNFCSDKK PAAVNWIEGR GKSVVCEAII EGDVVRKVLK TSVESLVELN
MLKNLTGSAM AGALGGFNAH ASNIVTAIYI ATGQDPAQNV ESSHCITMME AVNDGKDLHI
SVTMPSIEVG TVGGGTQLAS QSACLNLLGV KGASKDVAGA NSRMLATIVT GAVLAGELSL
MSALAAGQLV KSHMKYNRSS KDMSNLSS
