A0A8T1NXV9 · A0A8T1NXV9_CARIL

  • 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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site115substrate 1; for methylthioribulose-1-phosphate dehydratase activity
Binding site133Zn2+ (UniProtKB | ChEBI)
Binding site135Zn2+ (UniProtKB | ChEBI)
Active site158Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity
Binding site208Zn2+ (UniProtKB | ChEBI)
Binding site289Mg2+ (UniProtKB | ChEBI)
Binding site291Mg2+ (UniProtKB | ChEBI)
Binding site424-425substrate 2; for enolase-phosphatase activity
Binding site458substrate 2; for enolase-phosphatase activity
Binding site484Mg2+ (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

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
      CIPAW_12G119100
      , I3842_12G117600

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fagales > Juglandaceae > Carya

Accessions

  • Primary accession
    A0A8T1NXV9

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-243Methylthioribulose-1-phosphate dehydratase
Domain32-235Class II aldolase/adducin N-terminal
Region286-525Enolase-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
    525
  • Mass (Da)
    57,521
  • Last updated
    2022-10-12 v1
  • Checksum
    D3C46209ABD7E454
MAAVPAVAVNGVKLGMPSQAYLEGKAVKDTRVLISDLCRQFYNLGWVSGTGGSITIKVHDDSIPKPHQLIVMSPSGVQKERMVPEDMYVLSPDGSILSQPSPKPYPHKPPKCSDCGPLFLKAYEMCNSGAVIHSHGVESCLVTMLHPLSKEFRITHMEMIKGIKGHGYYDELVVPIIENTAYEYELTESLAKAIEAYPKTTAVLVRNHGIYIWGDSWINAKTQAECYHYLFDAAIKLHQLGLDWSTPNHGPIWNVKGGLGSGASANMSVKAGASADHGIEPLRRCIVLDIEGTTTPISFVTEVLFPYARDNVGRHLSATYETAETQDDINLLRSQVQDDLDQGIVGAVPIPSDSAGKEEVIAALVANVEAMIKADRKITALKQLQGHIWRTGFETNELEAVVFEDVPEALEKWHALGIKVYIYSSGSRLAQRLIFGNTSYGDLRKYLSGFFDTTVGNKREIRSYVEISESVGVDKPSEVLFVTDVYQEAEAAKAAGLEVMVSIRPGNGPLPENHGFKTIKSFSEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM031820
EMBL· GenBank· DDBJ
KAG6634441.1
EMBL· GenBank· DDBJ
Genomic DNA
CM031836
EMBL· GenBank· DDBJ
KAG6685565.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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