P14891 · HMDH1_ARATH
- Protein3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- GeneHMG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids592 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants.
Catalytic activity
- (R)-mevalonate + CoA + 2 NADP+ = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H+ + 2 NADPH
Activity regulation
Regulated at the post-translational level in response to alterations of sphingolipid and sterol biosynthetic pathways. Negatively regulated by a PP2A-dependent dephosphorylation occurring at a site different than Ser-577. Completely inhibited by mevinolin (IC50 = 12.5 nM). Reversibly inactivated by phosphorylation at Ser-577 by spinach or Brassica oleracea HMGR kinases in a cell-free system (PubMed:10318703, PubMed:7588795).
Down-regulated by KIN10 through its phosphorylation at Ser-577 (PubMed:28263378).
Down-regulated by KIN10 through its phosphorylation at Ser-577 (PubMed:28263378).
Pathway
Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 265 | Charge relay system | ||||
Sequence: E | ||||||
Active site | 397 | Charge relay system | ||||
Sequence: K | ||||||
Active site | 473 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 571 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | hydroxymethylglutaryl-CoA reductase (NADPH) activity | |
Biological Process | coenzyme A metabolic process | |
Biological Process | isopentenyl diphosphate biosynthetic process, mevalonate pathway | |
Biological Process | isoprenoid biosynthetic process | |
Biological Process | sterol biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- EC number
- Short namesAtHMGR1 ; HMG-CoA reductase 1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP14891
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform Short
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Also observed within spherical structures located along the endoplasmic reticulum strands.
Isoform Long
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 47-69 | Helical | ||||
Sequence: ASDALPLPLYLTNAVFFTLFFSV | ||||||
Transmembrane | 97-117 | Helical | ||||
Sequence: AIIALIASFIYLLGFFGIDFV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Dwarfing, early senescence, and sterility. 65% lower levels in triterpenoids content and 50% lower levels in sterol content. Hmg1 and hmg2 double mutants are lethal during male gametophyte development.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 577 | Abolishes the inactivation of activity by KIN10. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000114433 | 1-592 | 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 | |||
Sequence: MDLRRRPPKPPVTNNNNSNGSFRSYQPRTSDDDHRRRATTIAPPPKASDALPLPLYLTNAVFFTLFFSVAYYLLHRWRDKIRYNTPLHVVTITELGAIIALIASFIYLLGFFGIDFVQSFISRASGDAWDLADTIDDDDHRLVTCSPPTPIVSVAKLPNPEPIVTESLPEEDEEIVKSVIDGVIPSYSLESRLGDCKRAASIRREALQRVTGRSIEGLPLDGFDYESILGQCCEMPVGYIQIPVGIAGPLLLDGYEYSVPMATTEGCLVASTNRGCKAMFISGGATSTVLKDGMTRAPVVRFASARRASELKFFLENPENFDTLAVVFNRSSRFARLQSVKCTIAGKNAYVRFCCSTGDAMGMNMVSKGVQNVLEYLTDDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAVIRGEIVNKVLKTSVAALVELNMLKNLAGSAVAGSLGGFNAHASNIVSAVFIATGQDPAQNVESSQCITMMEAINDGKDIHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASTESPGMNARRLATIVAGAVLAGELSLMSAIAAGQLVRSHMKYNRSSRDISGATTTTTTTT | ||||||
Glycosylation | 16 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 19 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 575 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 577 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Inactivated by phosphorylation at Ser-577 by KIN10 activated form (PubMed:28263378).
Probably also phosphorylated at additional sites (PubMed:10318703, PubMed:7588795).
Probably also phosphorylated at additional sites (PubMed:10318703, PubMed:7588795).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in all tissues. Isoform Short is expressed at low levels specifically in flowers. Expressed in both the tapetum and microspores.
Induction
Down-regulated by light in immature leaves, but not in roots. Not regulated by myriocin, squalestatin or terbinafine.
Gene expression databases
Interaction
Subunit
Interacts (via N-terminus) with B''ALPHA and B''BETA.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-45 | Disordered | ||||
Sequence: MDLRRRPPKPPVTNNNNSNGSFRSYQPRTSDDDHRRRATTIAPPP | ||||||
Compositional bias | 10-26 | Polar residues | ||||
Sequence: PPVTNNNNSNGSFRSYQ | ||||||
Region | 118-171 | Linker | ||||
Sequence: QSFISRASGDAWDLADTIDDDDHRLVTCSPPTPIVSVAKLPNPEPIVTESLPEE | ||||||
Region | 172-592 | Catalytic | ||||
Sequence: DEEIVKSVIDGVIPSYSLESRLGDCKRAASIRREALQRVTGRSIEGLPLDGFDYESILGQCCEMPVGYIQIPVGIAGPLLLDGYEYSVPMATTEGCLVASTNRGCKAMFISGGATSTVLKDGMTRAPVVRFASARRASELKFFLENPENFDTLAVVFNRSSRFARLQSVKCTIAGKNAYVRFCCSTGDAMGMNMVSKGVQNVLEYLTDDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAVIRGEIVNKVLKTSVAALVELNMLKNLAGSAVAGSLGGFNAHASNIVSAVFIATGQDPAQNVESSQCITMMEAINDGKDIHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASTESPGMNARRLATIVAGAVLAGELSLMSAIAAGQLVRSHMKYNRSSRDISGATTTTTTTT |
Domain
The N-terminal domain (1-178) of the short isoform is necessary and sufficient for directing the protein to the endoplasmic reticulum and to spherical structures.
Sequence similarities
Belongs to the HMG-CoA reductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
P14891-1
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.
- NameShort
- SynonymsHMGR1S
- Length592
- Mass (Da)63,598
- Last updated1990-04-01 v1
- Checksum7EE10127460D3573
P14891-2
- NameLong
- SynonymsHMGR1L
- Differences from canonical
- 1-1: M → MKKKQAGPQQTCEFVSYKTLLISPSHLSRHLTTSLLSPLSPPWRDYSFPPM
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_041282 | 1 | in isoform Long | |||
Sequence: M → MKKKQAGPQQTCEFVSYKTLLISPSHLSRHLTTSLLSPLSPPWRDYSFPPM | ||||||
Compositional bias | 10-26 | Polar residues | ||||
Sequence: PPVTNNNNSNGSFRSYQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15032 EMBL· GenBank· DDBJ | CAA33139.1 EMBL· GenBank· DDBJ | mRNA | ||
J04537 EMBL· GenBank· DDBJ | AAA76821.1 EMBL· GenBank· DDBJ | mRNA | ||
L19261 EMBL· GenBank· DDBJ | AAA32814.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY488113 EMBL· GenBank· DDBJ | AAR83122.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012394 EMBL· GenBank· DDBJ | AAF16652.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC015450 EMBL· GenBank· DDBJ | AAG51957.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE35849.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF385690 EMBL· GenBank· DDBJ | AAK60283.1 EMBL· GenBank· DDBJ | mRNA | ||
BT000703 EMBL· GenBank· DDBJ | AAN31847.1 EMBL· GenBank· DDBJ | mRNA | ||
BT010468 EMBL· GenBank· DDBJ | AAQ65091.1 EMBL· GenBank· DDBJ | mRNA |