A0A1J7GQM8 · A0A1J7GQM8_LUPAN

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.

TypeIDPosition(s)Description
Binding site82substrate 1; for methylthioribulose-1-phosphate dehydratase activity
Binding site100Zn2+ (UniProtKB | ChEBI)
Binding site102Zn2+ (UniProtKB | ChEBI)
Active site125Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity
Binding site175Zn2+ (UniProtKB | ChEBI)
Binding site255Mg2+ (UniProtKB | ChEBI)
Binding site257Mg2+ (UniProtKB | ChEBI)
Binding site390-391substrate 2; for enolase-phosphatase activity
Binding site424substrate 2; for enolase-phosphatase activity
Binding site450Mg2+ (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
      TanjilG_23000

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Tanjil
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > genistoids sensu lato > core genistoids > Genisteae > Lupinus

Accessions

  • Primary accession
    A0A1J7GQM8

Proteomes

Genome annotation databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-202Class II aldolase/adducin N-terminal
Region1-210Methylthioribulose-1-phosphate dehydratase
Region252-478Enolase-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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    478
  • Mass (Da)
    53,043
  • Last updated
    2017-02-15 v1
  • Checksum
    498ACD967D388E37
MAELCRHFYTLGWVSGTGGSITIKVHDDSIPKPHQIILTAPSGVQKERMEPEDMYVLFQDGSVLSAPSPKPYPHKPPKCSDCSPLFMKAYEMRDAGAVYHSHGIESCLVTMINPLSKEFRITHMEMIKGIKGHGYYDELVVPIIENTAYEYELTDSFAKAIEAYPKTTAVLVRNHGVFVWGDSWISAKTQSECYHYLFDAAIKLHQLGLDWSTPDHGPKQGARRGLSLAGESNLSVKARKTEGEIDPFPRCVVLDIEGTTTPISFVSEVLFPYARDNVGRHLSATYDTPDTQNDIKLLRSQIQSDLEQGIAGAVPVPEDDAGKEEVIAAIVANVDAMIKADRKITALKELQGHIWKTGYENNELEGIVFDDVPEALEKWHALGIKVYIYSSGSRLAQRLIFGKTNYGDLRKYLSGFFDTTVGNKKETPSYVNIFESLGVDKPSDILFVTDVYQEATAAKAADHWAGQQSYCCAKAYGN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM007379
EMBL· GenBank· DDBJ
OIV92400.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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