[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=10971716 [NCBI, ExPASy, EBI, Israel, Japan] Duportets L., Belles X., Rossignol F., Couillaud F.; "Molecular cloning and structural analysis of 3-hydroxy-3-methylglutaryl coenzyme A reductase of the moth Agrotis ipsilon."; Insect Mol. Biol. 9:385-392(2000).

Comments

FUNCTION: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation (By similarity).
CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP⁺ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.
ENZYME REGULATION: The activity of HMG-CoA-reductase is suppressed by exogenous mevalonate.
PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3 .
PATHWAY: Context: 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

AJ009675; CAA08775.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04035; 1HWI. [HSSP ENTRY / PDB]

ModBase

O76819.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
IPR004816; HMG_CoA_Rdtase_I_metazoan.
IPR000731; SSD_5TM.
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

TIGR00920; 2A060605; 1.
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.
PS50156; SSD; 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`	`1 833`	`833`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114429`
`TRANSMEM`	`10 32`	`23`	`Potential.`
`TRANSMEM`	`91 117`	`27`	`Potential.`
`TRANSMEM`	`160 180`	`21`	`Potential.`
`TRANSMEM`	`301 321`	`21`	`Potential.`
`REGION`	`322 419`	`98`	`Linker.`
`REGION`	`420 833`	`414`	`Catalytic.`
`ACT_SITE`	`504 504`		`Charge relay system (By similarity).`
`ACT_SITE`	`635 635`		`Charge relay system (By similarity).`
`ACT_SITE`	`711 711`		`Charge relay system (By similarity).`
`ACT_SITE`	`809 809`		`Proton donor (By similarity).`
`CARBOHYD`	`680 680`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`715 715`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`720 720`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`813 813`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`825 825`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 833 AA [This is the length of the unprocessed precursor]

Molecular weight: 89790 Da [This is the MW of the unprocessed precursor]

CRC64: 7E9ADD4B4439A035 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVWGAHGEF CARHQWEVIV ATLALLACAA SVERNGPGNR SEHCAGWARA CPGLEAEYQA 

        70         80         90        100        110        120 
ADAVIMTFVR CAALLYAYYQ ISNLHKIASK YLLIIAGVFS TFASFIFTSA VASLFWSELA 

       130        140        150        160        170        180 
SIKDAPFLFL LVADVARGAR MAKAGWSAGE DQGKRVGRAL ALLGPTATLD TLLAVLLVGV 

       190        200        210        220        230        240 
GALSGVPRLE HMCTFACLAL LVDYLVFVTF YPACLSLVAD FASGRKEMSP DSPFSEADLK 

       250        260        270        280        290        300 
PNPVVQRVKM IMAAGLLCVH LTSRWPWSSD NGIIEGPTDT LTPTSNDNIL LHSYVKWFSV 

       310        320        330        340        350        360 
SADYIVIATL LCALIIKFVF FEEQRNWVID MNDMTVKEVV QEQARSKPKF SVGDDSNSEV 

       370        380        390        400        410        420 
STQTEGVLED EWPTLSPSSS AAKLNSKKRP MAECLEIYRS EGACVSLSDE EVVMLVEQSH 

       430        440        450        460        470        480 
IPLHRLEAVL GDPLRGVRLR RKVVGARFQT ELAIKQLPYL NYDYSKVLNA CCENVIGYVG 

       490        500        510        520        530        540 
VPVGYAGPLV VDGKPYMIPM ATTEGALVAS TNRGAKAIGI RGVTSVVEDV GMTRAPAIKL 

       550        560        570        580        590        600 
PNVVRAHECR QWIDNKDNYA VIKEAFDSTS RFARLQEIHI GVDGATLYLR FRATTGDAMG 

       610        620        630        640        650        660 
MNMVSKGAEN ALKLLKNYFP DMEVISLSGN YCSDKKAAAI NWVKGRGKRV VCETTITSDS 

       670        680        690        700        710        720 
LRTIFKTDAK TLARCNKIKN LSGSALAGSI GGNNAHAANM VTAIYIATGQ DPAQNVTSSN 

       730        740        750        760        770        780 
CSTNMEVCGE NGEDLYVTCT MPSLEVGTVG GGTILTGQGA CLDILGVKGA GARPAENSAR 

       790        800        810        820        830 
LASLICATVL AGELSLMAAL VNSDLVKSHM RHNRSTVNVQ VQAENITLKV PTL

O76819 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