NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=WFD11;
PubMed=1556098 [NCBI, ExPASy, EBI, Israel, Japan]
Lam W.L., Doolittle W.F.;
"Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii.";
J. Biol. Chem. 267:5829-5834(1992).

Comments

FUNCTION: Converts HMG-CoA to mevalonate (By similarity).
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: Isoprenoid biosynthesis .
INDUCTION: Inhibited by mevinolin.
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

M83531; AAA73174.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42149; A42149.

3D structure databases

HSSP

P04035; 1HW8. [HSSP ENTRY / PDB]

ModBase

Q59468.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
Graphical view of domain structure.

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; FALSE_NEG.
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

Isoprene biosynthesis; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 403`	`403`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114460`
`ACT_SITE`	`99 99`		`Charge relay system (By similarity).`
`ACT_SITE`	`303 303`		`Charge relay system (By similarity).`
`ACT_SITE`	`398 398`		`Proton donor (By similarity).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 41213 Da [This is the MW of the unprocessed precursor]

CRC64: 7EB79919587BD724 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDAASLADR VREGDLRLHE LEAHADADTA AEARRLLVES QSGASLDAVG NYGFPAEAAE 

        70         80         90        100        110        120 
SAIENMVGSI QVPMGVAGPV SVDGGSVAGE KYLPLATTEG ALLASVNRGC SVINSAGGAT 

       130        140        150        160        170        180 
ARVLKSGMTR APVFRVADVA EAEALVSWTR DNFAALKEAA EETTNHGELL DVTPYVVGNS 

       190        200        210        220        230        240 
VYLRFRYDTK DAMGMNMATI ATEAVCGVVE AETAASLVAL SGNLCSDKKP AAINAVEGRG 

       250        260        270        280        290        300 
RSVTADVRIP REVVEERLHT TPERGRELNT RKNLVGSAKA ASLGFNAHVA NVVAAMFLAT 

       310        320        330        340        350        360 
GQDEAQVVEG ANAITTAEVQ DGDLYVSVSI ASLEVGTVGG GTKLPTQSEG LDILGVSGGG 

       370        380        390        400 
DPAGSNADAL AECIAVGSLA GELSLLSALA SRHLSSAHAE LGR

Q59468 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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