NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Protoplast;
DOI=10.1007/BF00014504; PubMed=1391779 [NCBI, ExPASy, EBI, Israel, Japan]
Genschik P., Criqui M.-C., Parmentier Y., Marbach J., Durr A., Fleck J., Jamet E.;
"Isolation and characterization of a cDNA encoding a 3-hydroxy-3-methylglutaryl coenzyme A reductase from Nicotiana sylvestris.";
Plant Mol. Biol. 20:337-341(1992).

Comments

FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants. Possible role in plant defense mechanisms as well as in the cell cycle.
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 .
PATHWAY: Context: Plant isoprenoid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Found in protoplasts and leaves submitted to stress. Low levels found in apexes, anthers and roots.
DEVELOPMENTAL STAGE: Expressed at highest levels during the G0-G1 transition in the cell cycle of mesophyll protoplasts.
INDUCTION: In leaves, by wounding, elicitation, bacterial or fungal infection.
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

X63649; CAA45181.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S24760; S24760.

3D structure databases

HSSP

P04035; 1DQA. [HSSP ENTRY / PDB]

ModBase

Q01559.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_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.

TIGRFAMs

TIGR00533; HMG_CoA_R_NADP; 1.

PROSITE

PS00066; HMG_COA_REDUCTASE_1; 1.
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; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 604`	`604`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114445`
`TRANSMEM`	`40 62`	`23`	`Potential.`
`TRANSMEM`	`90 110`	`21`	`Potential.`
`REGION`	`111 189`	`79`	`Linker (By similarity).`
`REGION`	`190 604`	`415`	`Catalytic (By similarity).`
`ACT_SITE`	`283 283`		`Charge relay system (By similarity).`
`ACT_SITE`	`415 415`		`Charge relay system (By similarity).`
`ACT_SITE`	`491 491`		`Charge relay system (By similarity).`
`ACT_SITE`	`589 589`		`Proton donor (By similarity).`
`CARBOHYD`	`347 347`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`460 460`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`593 593`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 604 AA [This is the length of the unprocessed precursor]

Molecular weight: 65085 Da [This is the MW of the unprocessed precursor]

CRC64: 7046D17CAC0D0BA4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDVRRRSEKP AYPTKEFAAG EKPLKPHKQQ QEQDNSLLIA SDALPLPLYL TNGLFFTMFF 

        70         80         90        100        110        120 
SVMYYLLSRW REKIRNSTPL HVVTFSELVA IASLIASVIY LLGFFGIGFV QSFVSRDNND 

       130        140        150        160        170        180 
ECWDEEDEND EQFLLEEDSR RGPATTLGCT AVPPPPALQI VPMVPPQPSK VAAMSEKPAP 

       190        200        210        220        230        240 
LVTPAASEED EEIIKSVVQG KMPSYSLESK LGDCKRAASI RKEALQRITG KSLEGLPLEG 

       250        260        270        280        290        300 
FDYESILGQC CEMPIGYVQI PVGIAGPLLL DGREYSVPMA TTEGCLVAST NRGCKAIYAS 

       310        320        330        340        350        360 
GGATSVLLRD GMTRAPCVRF GTAKRAAELK FFVEDPVKFE TLAAVFNQSS RFARLQRIQC 

       370        380        390        400        410        420 
AIAGKNLYMR FVCSTGDAMG MNMVSKGVQN VLDYLQNEYP DMDVIGISGN FCSDKKPAAV 

       430        440        450        460        470        480 
NWIEGRGKSV VCEAIITEEV VKKVLKTEVA ALVELNMLKN LTGSAMAGAL GGFNAHASNI 

       490        500        510        520        530        540 
VSAVYIATGQ DPAQNIESSH CITMMEAVND GKDLHVSVTM PSIEVGTVGG GTQLASQSAC 

       550        560        570        580        590        600 
LNLLGVKGAN REVPGSNARL LATIVAGSVL AGELSLMSAI SAGQLVKSHM KYNRSTKDVT 


KASS

Q01559 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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