Q9SYM5 · RHM1_ARATH

  • Protein
    Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
  • Gene
    RHM1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II) (PubMed:14671019, PubMed:17190829, PubMed:19056285).
Plays a major role in supplying UDP-rhamnose for flavonol biosynthesis (PubMed:18757557).
Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).

Miscellaneous

The increased accumulation of auxin in rol1-2 seedlings appears to be caused by a flavonol-induced modification of auxin transport (PubMed:18567791, PubMed:21502189).
In bacteria, TDP-L-rhamnose is formed by the successive action of three different enzymes on TDP-D-glucose. In plants, on the other hand, a single polypeptide probably catalyzes all three reactions that lead to the conversion of UDP-D-glucose to UDP-L-rhamnose

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
NAD+ (UniProtKB | Rhea| CHEBI:57540 )

NADP+ (UniProtKB | Rhea| CHEBI:58349 )

Pathway

Carbohydrate biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site13-19NAD+ (UniProtKB | ChEBI)
Binding site132substrate
Active site133Proton donor
Active site134Proton acceptor
Active site159Proton acceptor
Binding site391-397NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Cellular Componentplasmodesma
Molecular FunctiondTDP-glucose 4,6-dehydratase activity
Molecular Functionisomerase activity
Molecular Functionoxidoreductase activity
Molecular FunctionUDP-glucose 4,6-dehydratase activity
Molecular FunctionUDP-L-rhamnose synthase activity
Biological Processauxin export across the plasma membrane
Biological Processcell differentiation
Biological Processcell wall organization
Biological Processflavonol biosynthetic process
Biological Processregulation of cell population proliferation
Biological ProcessUDP-rhamnose biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
  • Alternative names
    • Protein REPRESSOR OF LRX1 1
    • Rhamnose biosynthetic enzyme 1 (AtRHM1)

Including 2 domains:

  • Recommended name
    UDP-glucose 4,6-dehydratase
  • EC number
  • Recommended name
    UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase
  • EC number

Gene names

    • Name
      RHM1
    • Synonyms
      ROL1
    • ORF names
      T30F21.10
    • Ordered locus names
      At1g78570

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9SYM5

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Hyponastic growth, aberrant pavement cell and stomatal morphology in cotyledons, and defective trichome formation.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis283In rol1-2; Abolishes dehydratase activity in vitro (PubMed:16766693).
Induces aberrant accumulation of flavonols leading to alterations in plant growth and cell shape formation (PubMed:18567791, PubMed:18757557).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 17 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001832521-669Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in roots, stems, leaves, seedlings, inflorescence tips, and siliques. Detected in the adaxial side of cotyledons, in the emerging leaves and in trichomes. Also detected in the root tip, more precisely in the epidermal cells in the meristematic and elongation zone.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Domain

The dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.

Sequence similarities

In the C-terminal section; belongs to the dTDP-4-dehydrorhamnose reductase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    669
  • Mass (Da)
    75,372
  • Last updated
    2000-05-01 v1
  • Checksum
    FB8DF9C864F176D4
MASYTPKNILITGAAGFIASHVANRLIRSYPDYKIVVLDKLDYCSNLKNLNPSKHSPNFKFVKGDIASADLVNHLLITEGIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDALVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMRGQVLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVGHVYNIGTKKERRVNDVAKDICKLFNMDPEANIKFVDNRPFNDQRYFLDDQKLKKLGWSERTTWEEGLKKTMDWYTQNPEWWGDVSGALLPHPRMLMMPGGRHFDGSEDNSLAATLSEKPSQTHMVVPSQRSNGTPQKPSLKFLIYGKTGWIGGLLGKICDKQGIAYEYGKGRLEDRSSLLQDIQSVKPTHVFNSAGVTGRPNVDWCESHKTETIRANVAGTLTLADVCREHGLLMMNFATGCIFEYDDKHPEGSGIGFKEEDTPNFTGSFYSKTKAMVEELLKEYDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVNIPNSMTVLDELLPISIEMAKRNLKGIWNFTNPGVVSHNEILEMYRDYINPEFKWANFTLEEQAKVIVAPRSNNEMDASKLKKEFPELLSIKESLIKYAYGPNKKT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC007260
EMBL· GenBank· DDBJ
AAD30579.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE36122.1
EMBL· GenBank· DDBJ
Genomic DNA
AY042833
EMBL· GenBank· DDBJ
AAK68773.1
EMBL· GenBank· DDBJ
mRNA
AY081471
EMBL· GenBank· DDBJ
AAM10033.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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