[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Kennebec; TISSUE=Tuber; DOI=10.1023/A:1005743011651; PubMed=9049274 [NCBI, ExPASy, EBI, Israel, Japan] Korth K.L., Stermer B.A., Bhattacharyya M.K., Dixon R.A.; "HMG-CoA reductase gene families that differentially accumulate transcripts in potato tubers are developmentally expressed in floral tissues."; Plant Mol. Biol. 33:545-551(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Itoh Y., Yoshioka H., Doke N.; "Structure and nucleotide sequence of potato HMG3 encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase."; Submitted (JAN-1999) 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 .
PATHWAY: Context: Plant isoprenoid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Expressed in mature petals and anthers.
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

U51986; AAB52552.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022690; BAA93631.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S59946; S59946.
T07112; T07112.

3D structure databases

HSSP

P04035; 1HW8. [HSSP ENTRY / PDB]

ModBase

Q41438.

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`	`1 574`	`574`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase 3.`	`PRO_0000114450`
`TRANSMEM`	`41 61`	`21`	`Potential.`
`TRANSMEM`	`83 103`	`21`	`Potential.`
`REGION`	`104 161`	`58`	`Linker (By similarity).`
`REGION`	`162 574`	`413`	`Catalytic (By similarity).`
`ACT_SITE`	`256 256`		`Charge relay system (By similarity).`
`ACT_SITE`	`388 388`		`Charge relay system (By similarity).`
`ACT_SITE`	`464 464`		`Charge relay system (By similarity).`
`ACT_SITE`	`562 562`		`Proton donor (By similarity).`
`CARBOHYD`	`78 78`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`113 113`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`320 320`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`433 433`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`566 566`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 574 AA [This is the length of the unprocessed precursor]

Molecular weight: 62159 Da [This is the MW of the unprocessed precursor]

CRC64: E020BB10EF4779E4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDVRRRPVKP LYPSEHISSG EPLKPHNQDS SVKASDALPL PLYLTNGLFF TMFFSVMYFL 

        70         80         90        100        110        120 
LHRWREKIRN GIPLHVLNFS ELVAMVSLIA SVIYLLGFFG IGFVQSFVSK GNNDSWDVED 

       130        140        150        160        170        180 
ESPEQFIDRT VTPPPVRRNI PMKSVPVAEK TAQIITPFSS EDDEVVIKSV VEGRIPSYSL 

       190        200        210        220        230        240 
ESKLGDCKRA AFIRKEALQR SSGKSLEGLP LDGFDYESIL GQCCEMPIGY IQIPVGIAGP 

       250        260        270        280        290        300 
LLLNGKEFSV PMATTEGCLV ASTNRGCKAI YVSGGATSVL FRDAMTRAPV VRFGSAKRAA 

       310        320        330        340        350        360 
ELKFFVEDPM NFETLSVVFN KSSRFARLQN IQCAIAGKNL YMRFSCSTGD AMGMNMVSKG 

       370        380        390        400        410        420 
VQNVLDYLQN EYPDMDIIGI SGNYCSDKKP AAVNWIEGRG KSVVCEAIIK EDVVKKVLKT 

       430        440        450        460        470        480 
EVATLVELNM LKNLTGSAMA GALGGFNAHA SNIVSAVYLA TGQDPAQNIE SSHCITMMEA 

       490        500        510        520        530        540 
VNDGKDLHIS VTMPSIEVGT VGGGTQLASQ SACLNLLGVK GANREAPGSN ARLLATIVAG 

       550        560        570 
SVLAGELSLM SAISAGQLVK SHMKYNRSCK DVTK

Q41438 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