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A0A0E0BJ42 · A0A0E0BJ42_9ORYZ

  • 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 site114substrate 1; for methylthioribulose-1-phosphate dehydratase activity
Binding site132Zn2+ (UniProtKB | ChEBI)
Binding site134Zn2+ (UniProtKB | ChEBI)
Active site157Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity
Binding site207Zn2+ (UniProtKB | ChEBI)
Binding site282Mg2+ (UniProtKB | ChEBI)
Binding site284Mg2+ (UniProtKB | ChEBI)
Binding site417-418substrate 2; for enolase-phosphatase activity
Binding site451substrate 2; for enolase-phosphatase activity
Binding site477Mg2+ (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
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza

Accessions

  • Primary accession
    A0A0E0BJ42

Proteomes

Genome annotation databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-242Methylthioribulose-1-phosphate dehydratase
Domain31-234Class II aldolase/adducin N-terminal
Region279-518Enolase-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
    518
  • Mass (Da)
    56,911
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    5524A8F9955A1CFF439B8476E9A95720
MACCGGGRGEGAAATESEAYLEGEAVREARELVAELCRHFYGQGWVTGTGGSITVKANDPALPLADQLIVMSPSGVQKERMVAEDMYVLSADGKVLSSPVSKPWPNKPPKCTDCAPLFMKAYLMRGAGAVIHSHGMETCIATMLDPGAKEFRMTHMEMIKGIKGHGYRDELVVPIIENTPYEYELTDSLAEAIAAYPKATAVLVRNHGIYVWGDSWINAKTQAECYHYLFDAAIKLYQLGIDWTTPEHGPINSAKRPRSVLSSSIPNGCADSKSSKNCVVLDIEGTTTPISFVTDVMFPYARDNVRKHLTSTYSSDETKEDIKLLRIQVEEDLKNGIVGSVPIPPDDADKEEVINALVANVESMIKADRKITSLKQLQGHIWRTGFESKELQGVVFDDVPEALKHWHASGMKVYIYSSGSREAQRLLFGNTAYGDLRQYLCGFFDTTTGNKRETRSYFEISQSLGVDSPAQILFITDVFQEAVAAKSAGFEVIISIRPGNAPLPENHGFRTIKSFSEI

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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