[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. VFNT Cherry; DOI=10.1007/BF00014502; PubMed=1391777 [NCBI, ExPASy, EBI, Israel, Japan] Park H.S., Denbow C.J., Cramer C.L.; "Structure and nucleotide sequence of tomato HMG2 encoding 3-hydroxy-3-methyl-glutaryl coenzyme A reductase."; Plant Mol. Biol. 20:327-331(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1104/pp.112.2.727; PubMed=8883384 [NCBI, ExPASy, EBI, Israel, Japan] Daraselia N.D., Tarchevskaya S., Narita J.O.; "The promoter for tomato 3-hydroxy-3-methylglutaryl coenzyme A reductase gene 2 has unusual regulatory elements that direct high-level expression."; Plant Physiol. 112:727-733(1996).

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 .
PATHWAY: Context: Plant isoprenoid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum 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

M63642; AAA34169.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U68072; AAB62581.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S25316; S25316.

3D structure databases

HSSP

P04035; 1DQA. [HSSP ENTRY / PDB]

ModBase

P48022.

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`	`1 602`	`602`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase 2.`	`PRO_0000114443`
`TRANSMEM`	`44 67`	`24`	`Potential.`
`TRANSMEM`	`95 115`	`21`	`Potential.`
`REGION`	`116 187`	`72`	`Linker (By similarity).`
`REGION`	`188 602`	`415`	`Catalytic (By similarity).`
`COMPBIAS`	`30 34`	`5`	`Poly-Gln.`
`ACT_SITE`	`281 281`		`Charge relay system (By similarity).`
`ACT_SITE`	`413 413`		`Charge relay system (By similarity).`
`ACT_SITE`	`489 489`		`Charge relay system (By similarity).`
`ACT_SITE`	`587 587`		`Proton donor (By similarity).`
`CARBOHYD`	`124 124`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`345 345`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`458 458`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`591 591`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`56 56`		`Missing (in Ref. 2; AAB62581).`
`CONFLICT`	`186 186`		`G -> E (in Ref. 2; AAB62581).`
`CONFLICT`	`339 339`		`S -> T (in Ref. 2; AAB62581).`
`CONFLICT`	`369 370`		`LC -> FV (in Ref. 2; AAB62581).`

Sequence information

Length: 602 AA [This is the length of the unprocessed precursor]

Molecular weight: 64715 Da [This is the MW of the unprocessed precursor]

CRC64: 0266E55E2EB953BD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDVRRRSEEP VYPSKVFAAD EKPLKPHKKQ QQQQEDKNTL LIDASDALPL PLYLTTNGLF 

        70         80         90        100        110        120 
FTMFFSVMYF LLSRWREKIR NSTPLHVVTL SELGAIVSLI ASVIYLLGFF GIGFVQTFVS 

       130        140        150        160        170        180 
RGNNDSWDEN DEEFLLKEDS RCGPATTLGC AVPAPPARQI APMAPPQPSM SMVEKPAPLI 

       190        200        210        220        230        240 
TSASSGEDEE IIKSVVQGKI PSYSLESKLG DCKRAASIRK EVMQRITGKS LEGLPLEGFN 

       250        260        270        280        290        300 
YESILGQCCE MPIGYVQIPV GIAGPLLLNG KEFSVPMATT EGCLVASTNR GCKAIYASGG 

       310        320        330        340        350        360 
ATCILLRDGM TRAPCVRFGT AKRAAELKFF VEDPIKFESL ANVFNQSSRF ARLQRIQCAI 

       370        380        390        400        410        420 
AGKNLYMRLC CSTGDAMGMN MVSKGVQNVL DYLQNEYPDM DVIGISGNFC SDKKPAAVNW 

       430        440        450        460        470        480 
IEGRGKSVVC EAIITEEVVK KVLKTEVAAL VELNMLKNLT GSAMAGALGG FNAHASNIVS 

       490        500        510        520        530        540 
AVFIATGQDP AQNIESSHCI TMMEAVNDGK DLHISVTMPS IEVGTVGGGT QLASQSACLN 

       550        560        570        580        590        600 
LLGVKGANRE APGSNARLLA TVVAGSVLAG ELSLMSAISS GQLVNSHMKY NRSTKDVTKA 


SS

P48022 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