A0A803N242 · A0A803N242_CHEQI

  • 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.

TypeIDPosition(s)Description
Binding site123substrate 1; for methylthioribulose-1-phosphate dehydratase activity
Binding site157Zn2+ (UniProtKB | ChEBI)
Binding site159Zn2+ (UniProtKB | ChEBI)
Active site182Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity
Binding site232Zn2+ (UniProtKB | ChEBI)
Binding site461Mg2+ (UniProtKB | ChEBI)
Binding site463Mg2+ (UniProtKB | ChEBI)
Binding site596-597substrate 2; for enolase-phosphatase activity
Binding site630substrate 2; for enolase-phosphatase activity
Binding site656Mg2+ (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

Organism names

  • Taxonomic identifier
  • Strain
    • cv. PI 614886
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Atripliceae > Chenopodium

Accessions

  • Primary accession
    A0A803N242

Proteomes

Genome annotation databases

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-310Methylthioribulose-1-phosphate dehydratase
Domain40-254Class II aldolase/adducin N-terminal
Region458-697Enolase-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
    697
  • Mass (Da)
    76,160
  • Last updated
    2021-06-02 v1
  • Checksum
    A1488CD2C86FF638
MAFASAASVGPLAAGNGLKMANSTTTQAYLESKPVQEAKALLTELCRQFYHLGWVGGTGGSITLKVHDDSIPKPQQIIIMSPSGVQKERMLSEDMYVLSSDGSTVSAPSPKPYPNKPPKCSDCGPLFMKDHQLKVYDIKSQSFVQAYQMRNAGAVIHSHGMESCLVTMMNPTSNEFRITHMEMIKGIQGHGYYDELVVPIIENSAHERDLTDALAAAIEAYPKTTAVLVRNHGIYVWGDSWISAKTQTLLRMIASPTGSGKSYTVDDSFSAEERHTPRLAGVLLIVVSMQAECYHYLFDAAIKLNQMGLDWSTPTHGPIKRIQADFRSGERAVSAKAGTSGLNPGEPKPRCIVLDIEGTTTPISFVTDVLFPYARDNVGRHLSSTYDSPETQDDIKLLRGQVEEDLKAGVVGAVPIPSDDEGKEEVIAALVANVGGHIWRTGFQNNELEGVVFEDRCIVLDIEGTTTPISFVTDVLFPYARDNVGRHLSSTYDSPETQDDIKLLRGQVEEDLKAGVVGAVPIPSDDEGKEEVIAALVANVGGMIKADRKITALKQLQGHIWRTGFQNNELEGVVFEDVPEALERWHSSGIKVYIYSSGSRLAQRLIFGNTKYGDLRKYLCGFFDTAVGNKRETQSYVEIFNSMGVDDPSEILFVTDVYQEATAAKEAGLEVLISVRPGNGPLPENHGFKTVNSFSEI

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp