A0A398A8X8 · A0A398A8X8_BRACM

  • Protein
    Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site108substrate 1; for methylthioribulose-1-phosphate dehydratase activity
Binding site126Zn2+ (UniProtKB | ChEBI)
Binding site128Zn2+ (UniProtKB | ChEBI)
Active site151Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity
Binding site201Zn2+ (UniProtKB | ChEBI)
Binding site265Mg2+ (UniProtKB | ChEBI)
Binding site267Mg2+ (UniProtKB | ChEBI)
Binding site400-401substrate 2; for enolase-phosphatase activity
Binding site434substrate 2; for enolase-phosphatase activity
Binding site460Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity
Molecular Function2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity
Molecular Functionacireductone synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionmethylthioribulose 1-phosphate dehydratase activity
Molecular Functionzinc ion binding
Biological ProcessL-methionine salvage from methylthioadenosine
Biological ProcessL-methionine salvage from S-adenosylmethionine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1

Including 2 domains:

  • Recommended name
    Methylthioribulose-1-phosphate dehydratase
  • EC number
  • Short names
    MTRu-1-P dehydratase
  • Recommended name
    Enolase-phosphatase E1
  • EC number
  • Alternative names
    • 2,3-diketo-5-methylthio-1-phosphopentane phosphatase

Gene names

    • ORF names
      BRARA_B01398

Organism names

  • Taxonomic identifier
  • Strain
    • cv. B-3
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica

Accessions

  • Primary accession
    A0A398A8X8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-236Methylthioribulose-1-phosphate dehydratase
Domain25-228Class II aldolase/adducin N-terminal
Region262-501Enolase-phosphatase E1

Sequence similarities

In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
In the N-terminal section; belongs to the aldolase class II family. MtnB subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    501
  • Mass (Da)
    55,332
  • Last updated
    2018-12-05 v1
  • MD5 Checksum
    3E5A8A2298A9018A4A9E1F2AC20BA3D1
MAAAEAMIGFPQAYLESREVKETSSLVTELCRHFYTQGWVSGTGGSITIKVHDASIPKPDQLIVMSPSGVQKERMGPEDMYILSPNGSVISAPSPKPYPNKLPKCTDCAPLFMKAYEMRNAGAVIHSHGMESCLVTMLNPQAKEFRITHMEMIKGIQGHGYYDELVVPIIENTAYENELTDSLTKAIIAYPKATAVLVRNHGVYIWGDSWIHAKTQAECYHYLFDAAIKLHQLGLDAATPEHGPIQRATHSQNQTESTRRCIVLDIEGTTTPITFVTDVLFPYARENVGKHLSLTYDTAETQEDIKLLRAQVEEDLTQGVTGTVPVPHADEGKDEVIAAMVSNVEAMIKADRKITALKELQGHIWRTGFKCNELKSVVFEDVADALEKWHSSGTKVYIYSSGSRLAQRLLFGNTSYGDLRKYLSGFFDTTIGNKKESKSYKEITETLGVDDPSEILFVTDVYQEATAAKAAGLEAIISIRPGNASLPENHGFKTVTSFSQI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM010629
EMBL· GenBank· DDBJ
RID74292.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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