Reviewed, UniProtKB/Swiss-Prot P14891 (HMDH1_ARATH)

Names and origin

Protein names

Recommended name:
    3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
      Short name=HMG-CoA reductase 1
      Short name=HMGR1
    EC=1.1.1.34

Gene names

Name:	HMG1
Ordered Locus Names:	At1g76490
ORF Names:	F15M4.1, F14G6.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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.
Enzyme regulation	Completely inhibited by mevinolin (IC50 = 12.5 nM). Ref.5
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Found in all tissues.
Post-translational modification	Reversibly inactivated by phosphorylation at Ser-577 by Brassica oleracea HMGR kinase A in a cell-free system.
Sequence similarities	Belongs to the HMG-CoA reductase family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	coenzyme A metabolic process Inferred from electronic annotation. Source: InterPro isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from mutant phenotype. Source: TAIR
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: TAIR integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC hydroxymethylglutaryl-CoA reductase activity Ref.2 Inferred from genetic interaction. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	3-hydroxy-3-methylglutaryl-coenzyme A reductase 1		PRO_0000114433
Regions
	Transmembrane	47 – 69	23	Potential
	Transmembrane	97 – 117	21	Potential
	Region	118 – 171	54	Linker By similarity
	Region	172 – 592	421	Catalytic By similarity
Sites
	Active site	265	1	Charge relay system By similarity
	Active site	397	1	Charge relay system By similarity
	Active site	473	1	Charge relay system By similarity
	Active site	571	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	16	1	N-linked (GlcNAc...) Potential
	Glycosylation	19	1	N-linked (GlcNAc...) Potential
	Glycosylation	329	1	N-linked (GlcNAc...) Potential
	Glycosylation	575	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P14891-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 7EE10127460D3573	FASTA	592	63,598
	10 20 30 40 50 60 MDLRRRPPKP PVTNNNNSNG SFRSYQPRTS DDDHRRRATT IAPPPKASDA LPLPLYLTNA 70 80 90 100 110 120 VFFTLFFSVA YYLLHRWRDK IRYNTPLHVV TITELGAIIA LIASFIYLLG FFGIDFVQSF 130 140 150 160 170 180 ISRASGDAWD LADTIDDDDH RLVTCSPPTP IVSVAKLPNP EPIVTESLPE EDEEIVKSVI 190 200 210 220 230 240 DGVIPSYSLE SRLGDCKRAA SIRREALQRV TGRSIEGLPL DGFDYESILG QCCEMPVGYI 250 260 270 280 290 300 QIPVGIAGPL LLDGYEYSVP MATTEGCLVA STNRGCKAMF ISGGATSTVL KDGMTRAPVV 310 320 330 340 350 360 RFASARRASE LKFFLENPEN FDTLAVVFNR SSRFARLQSV KCTIAGKNAY VRFCCSTGDA 370 380 390 400 410 420 MGMNMVSKGV QNVLEYLTDD FPDMDVIGIS GNFCSDKKPA AVNWIEGRGK SVVCEAVIRG 430 440 450 460 470 480 EIVNKVLKTS VAALVELNML KNLAGSAVAG SLGGFNAHAS NIVSAVFIAT GQDPAQNVES 490 500 510 520 530 540 SQCITMMEAI NDGKDIHISV TMPSIEVGTV GGGTQLASQS ACLNLLGVKG ASTESPGMNA 550 560 570 580 590 RRLATIVAGA VLAGELSLMS AIAAGQLVRS HMKYNRSSRD ISGATTTTTT TT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase." Caelles C., Ferrer A., Balcells L., Hegardt F.G., Boronat A. Plant Mol. Biol. 13:627-638(1989) [PubMed: 2491679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"3-hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzymes." Learned R.M., Fink G.R. Proc. Natl. Acad. Sci. U.S.A. 86:2779-2783(1989) [PubMed: 2649893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase." Dale S., Arro M., Becerra B., Morrice N.G., Boronat A., Hardie D.G., Ferrer A. Eur. J. Biochem. 233:506-513(1995) [PubMed: 7588795] [Abstract] Cited for: PROTEIN SEQUENCE OF 573-586, ENZYME REGULATION, PHOSPHORYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15032 mRNA. Translation: CAA33139.1. L19261 Genomic DNA. Translation: AAA32814.1. J04537 mRNA. Translation: AAA76821.1. AC012394 Genomic DNA. Translation: AAF16652.1. AC015450 Genomic DNA. Translation: AAG51957.1. AF385690 mRNA. Translation: AAK60283.1. BT000703 mRNA. Translation: AAN31847.1. BT010468 mRNA. Translation: AAQ65091.1.
IPI	IPI00545411.
PIR	A32107.
3D structure databases
SMR	P14891. Positions 169-568.
ModBase	Search...
Protein-protein interaction databases
STRING	P14891.
Proteomic databases
PRIDE	P14891.
Organism-specific databases
TAIR	At1g76490.
Phylogenomic databases
eggNOG	KOG2480.
InParanoid	P14891.
PhylomeDB	P14891.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G76490-MONOMER.
BRENDA	1.1.1.34. 302.
Gene expression databases
Genevestigator	P14891.
Family and domain databases
InterPro	IPR002202. HMG_CoA_Rdtase_cat. IPR004554. HMG_CoA_Rdtase_I_cat. IPR009023. HMG_CoA_Rdtase_NAD(P)-bd. IPR009029. HMG_CoA_Rdtase_sub-bd. [Graphical view]
Gene3D	G3DSA:3.90.770.10. HMG-CoA_red. 1 hit.
PANTHER	PTHR10572. HMG-CoA_red. 1 hit.
Pfam	PF00368. HMG-CoA_red. 1 hit. [Graphical view]
PRINTS	PR00071. HMGCOARDTASE.
TIGRFAMs	TIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITE	PS00066. HMG_COA_REDUCTASE_1. 1 hit. PS00318. HMG_COA_REDUCTASE_2. 1 hit. PS01192. HMG_COA_REDUCTASE_3. 1 hit. PS50065. HMG_COA_REDUCTASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMDH1_ARATH

Accession

Primary (citable) accession number: P14891

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	February 9, 2010
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)