NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. RRIM 600;
TISSUE=Leaf;
DOI=10.1007/BF00023422; PubMed=1714317 [NCBI, ExPASy, EBI, Israel, Japan]
Chye M.L., Kush A., Tan C.T., Chua N.H.;
"Characterization of cDNA and genomic clones encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase from Hevea brasiliensis.";
Plant Mol. Biol. 16:567-577(1991).

Comments

FUNCTION: Catalyzes the synthesis of mevalonate. The specific precursor of all isoprenoid compounds present in plants.
CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP⁺ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.
PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3 .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. Plastid membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the HMG-CoA reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54658; CAA38468.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S14953; S14953.

3D structure databases

HSSP

P04035; 1DQA. [HSSP ENTRY / PDB]

ModBase

P29058.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0042170;	Cellular component: plastid membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004420;	Molecular function: hydroxymethylglutaryl-CoA reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0015936;	Biological process: coenzyme A metabolic process (inferred from electronic annotation from InterPro).
GO:0008299;	Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.770.10; HMG-CoA_red; 1.

PANTHER

PTHR10572; HMG-CoA_red; 1.

Pfam

PF00368; HMG-CoA_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00071; HMGCOARDTASE.

PROSITE

PS00066; HMG_COA_REDUCTASE_1; PARTIAL.
PS00318; HMG_COA_REDUCTASE_2; 1.
PS01192; HMG_COA_REDUCTASE_3; 1.
PS50065; HMG_COA_REDUCTASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; Mitochondrion; NADP; Oxidoreductase; Plastid; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 210`	`>210`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase 2.`	`PRO_0000114441`
`TRANSMEM`	`166 186`	`21`	`Potential.`
`ACT_SITE`	`21 21`		`Charge relay system (By similarity).`
`ACT_SITE`	`97 97`		`Charge relay system (By similarity).`
`ACT_SITE`	`195 195`		`Proton donor (By similarity).`
`CARBOHYD`	`199 199`		`N-linked (GlcNAc...) (Potential).`
`NON_TER`	`1 1`

Sequence information

Length: 210 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 21564 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 059C3C30766BD911 [This is a checksum on the sequence]

        10         20         30         40         50         60 
LESDFADMDV IGISGNFCSD KKPAAVNWIE GRGKSVVCEA IIKEEVVKKV LKTDVALLVE 

        70         80         90        100        110        120 
LNMLKNLAGS AVAGALGGFN AHAGNIVSAI FIATGQDPAQ NVESSHCITM MEAVNDGKDL 

       130        140        150        160        170        180 
HISVTLPSIE VGTVGGGTQL ASQSACLNLL GVMGACKESP GSYSRLLATI VAGSVLAGEL 

       190        200        210 
SLMSAIAAGQ LVKSHMKYNR SSKDVSKAAS

P29058 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools