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P14891 (HMDH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.

Subcellular location

Isoform Short: Endoplasmic reticulum membrane; Multi-pass membrane protein.

Isoform Long: Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Found in all tissues. Isoform Short is expressed at low levels specifically in flowers. Ref.3

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.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Short (identifier: P14891-1)

Also known as: HMGR1S;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Long (identifier: P14891-2)

Also known as: HMGR1L;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKKKQAGPQQTCEFVSYKTLLISPSHLSRHLTTSLLSPLSPPWRDYSFPPM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5925923-hydroxy-3-methylglutaryl-coenzyme A reductase 1
PRO_0000114433

Regions

Transmembrane47 – 6923Helical; Potential
Transmembrane97 – 11721Helical; Potential
Region118 – 17154Linker By similarity
Region172 – 592421Catalytic By similarity

Sites

Active site2651Charge relay system By similarity
Active site3971Charge relay system By similarity
Active site4731Charge relay system By similarity
Active site5711Proton donor By similarity

Amino acid modifications

Glycosylation161N-linked (GlcNAc...) Potential
Glycosylation191N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MKKKQAGPQQTCEFVSYKTL LISPSHLSRHLTTSLLSPLS PPWRDYSFPPM in isoform Long.
VSP_041282

Sequences

Sequence LengthMass (Da)Tools
Isoform Short (HMGR1S) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 7EE10127460D3573

FASTA59263,598
        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 

« Hide

Isoform Long (HMGR1L) [UniParc].

Checksum: 1B6A130064AEF1A5
Show »

FASTA64269,280

References

« Hide '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] (ISOFORM SHORT).
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] (ISOFORM SHORT).
[3]"The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-3-methylglutaryl coenzyme A reductase isoform with an extended N-terminal region."
Lumbreras V., Campos N., Boronat A.
Plant J. 8:541-549(1995) [PubMed: 7496400] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), TISSUE SPECIFICITY, ALTERNATIVE INITIATION.
[4]"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. expand/collapse author list , 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.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"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. expand/collapse author list , 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] (ISOFORM SHORT).
Strain: cv. Columbia.
[7]"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.
J04537 mRNA. Translation: AAA76821.1.
L19261 Genomic DNA. Translation: AAA32814.1.
AY488113 mRNA. Translation: AAR83122.1.
AC012394 Genomic DNA. Translation: AAF16652.1.
AC015450 Genomic DNA. Translation: AAG51957.1.
CP002684 Genomic DNA. Translation: AEE35849.1.
AF385690 mRNA. Translation: AAK60283.1.
BT000703 mRNA. Translation: AAN31847.1.
BT010468 mRNA. Translation: AAQ65091.1.
IPIIPI00545411.
IPI01018461.
PIRA32107.
RefSeqNP_177775.2. NM_106299.3.
UniGeneAt.22772.

3D structure databases

ProteinModelPortalP14891.
SMRP14891. Positions 168-569.
ModBaseSearch...

Protein-protein interaction databases

STRINGP14891.

Proteomic databases

PRIDEP14891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID843982.
GenomeReviewsGene locus AT1G76490 in contig CT485782_GR.
KEGGath:AT1G76490.

Organism-specific databases

TAIRAt1g76490.

Phylogenomic databases

eggNOGKOG2480.
InParanoidP14891.
PhylomeDBP14891.

Enzyme and pathway databases

BioCycARA:AT1G76490-MONOMER.
MetaCyc:AT1G76490-MONOMER.

Gene expression databases

GenevestigatorP14891.

Family and domain databases

InterProIPR002202. HMG_CoA_Rdtase.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR004554. HMG_CoA_Rdtase_eu_arc.
IPR023282. HMG_CoA_Rdtase_N.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd.
IPR009029. HMG_CoA_Rdtase_sub-bd.
[Graphical view]
Gene3DG3DSA:3.30.70.420. G3DSA:3.30.70.420. 1 hit.
G3DSA:3.90.770.10. HMG-CoA_red. 2 hits.
G3DSA:1.10.3270.10. HMG_CoA_Rdtase_N. 1 hit.
KOK00021.
PANTHERPTHR10572. HMG-CoA_red. 1 hit.
PfamPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
PRINTSPR00071. HMGCOARDTASE.
SUPFAMSSF55035. HMG_CoA_NAD_bind. 1 hit.
SSF56542. HMG_CoA_sub_bind. 1 hit.
TIGRFAMsTIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITEPS00066. 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]
ProtoNetSearch...

Entry information

Entry nameHMDH1_ARATH
AccessionPrimary (citable) accession number: P14891
Secondary accession number(s): Q6RW12
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 16, 2011
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families