NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1007/BF00023395; PubMed=1377968 [NCBI, ExPASy, EBI, Israel, Japan]
Chye M.L., Tan C.T., Chua N.H.;
"Three genes encode 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hevea brasiliensis: hmg1 and hmg3 are differentially expressed.";
Plant Mol. Biol. 19:473-484(1992).

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

M74800; AAA33360.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74798; AAA33358.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74799; AAA33359.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S22521; S22521.

3D structure databases

HSSP

P04035; 1HWI. [HSSP ENTRY / PDB]

ModBase

Q00583.

Ontologies

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

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`	`1 586`	`586`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase 3.`	`PRO_0000114442`
`TRANSMEM`	`36 59`	`24`	`By similarity.`
`TRANSMEM`	`87 107`	`21`	`By similarity.`
`REGION`	`108 170`	`63`	`Linker (By similarity).`
`REGION`	`171 586`	`416`	`Catalytic (By similarity).`
`REGION`	`172 586`	`415`	`Catalytic (By similarity).`
`ACT_SITE`	`265 265`		`Charge relay system (By similarity).`
`ACT_SITE`	`397 397`		`Charge relay system (By similarity).`
`ACT_SITE`	`473 473`		`Charge relay system (By similarity).`
`ACT_SITE`	`571 571`		`Proton donor (By similarity).`
`CARBOHYD`	`575 575`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 586 AA [This is the length of the unprocessed precursor]

Molecular weight: 62970 Da [This is the MW of the unprocessed precursor]

CRC64: 0B9D6DCC5979B456 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDEVRRRPPK HIVRKDHDGE VLNSFSHGHH LPPLKPSDYS LPLSLYLANA LVFSLFFSVA 

        70         80         90        100        110        120 
YFLLHRWREK IRKSTPLHIV TFPEIAALIC LVASVIYLLG FFGIGFVHSF SRASTDSWDV 

       130        140        150        160        170        180 
EEYDDDNIII KEDTRPTGAC AAPSLDCSLS LPTKIHAPIV STTTTSTLSD DDEQIIKSVV 

       190        200        210        220        230        240 
SGSIPSYSLE SKLGNCKRAA LIRRETLQRM SGRSLEGLPL DGFDYESILG QCCEMAIGYV 

       250        260        270        280        290        300 
QIPVGIAGPL LLDGKEYTVP MATTEGCLVA SANRGCKAIY ASGGATSVLL RDGMTRAPVV 

       310        320        330        340        350        360 
RFPTAKRAAD LKFFMEDPDN FDTIAVVFNK SSRFARLQSV QCAIAGKNLY MRFSCSTGDA 

       370        380        390        400        410        420 
MGMNMVSKAV QNVIDYLQND FPDMDVIGLT GNFCADKKAA AVNWIEGRGK SVVCEAIIKE 

       430        440        450        460        470        480 
EVVKKVLKTN VAALVELNMI KNLTGSAVAG SLGGFNAHAS NMVTAVYIAT GQDPAQNVES 

       490        500        510        520        530        540 
SHCITMMEAV NDGKDLHISV SMPSIELGTV GGGTQLASQS ACLNLLGVKG ASKDSPGSNS 

       550        560        570        580 
RLLATIVAGS VLAGELSLMS AIAAGQLVNS HMKYNRSAKD VSKITF

Q00583 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