[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. LG 21-11; Mayer M.J., Steel J., Bailey J.A., Hargreaves J.A.; Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.

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.
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

Y09238; CAA70440.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T04357; T04357.

3D structure databases

HSSP

P04035; 1DQA. [HSSP ENTRY / PDB]

ModBase

O24594.

Organism-specific databases

Gramene

O24594; -.

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 InterPro).
GO:0004420;	Molecular function: hydroxymethylglutaryl-CoA reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (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 InterPro).
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.
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

ProtoNet

O24594.

UniRef

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`	`1 579`	`579`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114444`
`TRANSMEM`	`36 56`	`21`	`Potential.`
`TRANSMEM`	`80 100`	`21`	`Potential.`
`TRANSMEM`	`524 544`	`21`	`Potential.`
`REGION`	`101 153`	`53`	`Linker (By similarity).`
`REGION`	`154 579`	`426`	`Catalytic (By similarity).`
`ACT_SITE`	`247 247`		`Charge relay system (By similarity).`
`ACT_SITE`	`379 379`		`Charge relay system (By similarity).`
`ACT_SITE`	`455 455`		`Charge relay system (By similarity).`
`ACT_SITE`	`553 553`		`Proton donor (By similarity).`
`CARBOHYD`	`311 311`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`557 557`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 579 AA [This is the length of the unprocessed precursor]

Molecular weight: 60931 Da [This is the MW of the unprocessed precursor]

CRC64: ECA693F232EB2B6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVRGGVGQG SAARHPPAPE PSRAAARVQA GDALPLPIRH TNLIFSALFA ASLAYLMRRW 

        70         80         90        100        110        120 
REKIRSSTPL HAVGLAEMLA IFGLVASLIY LLSFFGIAFV QSIVSSGDDD EDFLVGSGSS 

       130        140        150        160        170        180 
GSAAAPSRQH AQAPAPCELL GSPAAAPEKM PEDDEEIVAS VVAGKVPSYA LEARLGDCRR 

       190        200        210        220        230        240 
AAGIRREALR RITGRDIEGL PLDGFDYASI LGQCCELPVG YVQLPVGVAG PLLLDGRRFY 

       250        260        270        280        290        300 
LPMATTEGCL VASTNRGCKA IAESGGATSV VLRDAMTRAP VARFPTARRA AELKAFLEDP 

       310        320        330        340        350        360 
ANFDTLSVVF NRSSRFARLQ GVQCAMAGRN LYMRFSCSTG DAMGMNMVSK GVQNVLDFLQ 

       370        380        390        400        410        420 
DDFHDMDVIS ISGNFCSDKK PSAVNWIEGR GKSVVCEAVI GEEVVKKVLK TDVQSLVELN 

       430        440        450        460        470        480 
TIKNLAGSAV AGALGGFNAH ASNIVTAIFI ATGQDPAQNV ESSHCITMLE PVNAGRDLHI 

       490        500        510        520        530        540 
SVTMPSIEVG TVGGGTQLAS QSACLDLLGV RGASRDRPGS NARLLATVVA GGVLAGELSL 

       550        560        570 
LSALAAGQLV KSHMKYNRSS KDVSSTTATE KTRQREVDV

O24594 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