B4G0F3 · MTBC_MAIZE

  • Protein
    Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ 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 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 site281Mg2+ (UniProtKB | ChEBI)
Binding site283Mg2+ (UniProtKB | ChEBI)
Binding site416-417substrate 2; for enolase-phosphatase activity
Binding site450substrate 2; for enolase-phosphatase activity
Binding site476Mg2+ (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

    • UPA00904UER00875
    • UPA00904UER00876
    • UPA00904UER00877

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
    • B73
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea

Accessions

  • Primary accession
    B4G0F3
  • Secondary accessions
    • B6T6D3

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003941561-517Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-242Methylthioribulose-1-phosphate dehydratase
Region278-517Enolase-phosphatase E1

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    517
  • Mass (Da)
    56,970
  • Last updated
    2008-09-23 v1
  • Checksum
    C23101545CF82A4F
MACSGCSCEAAVGAMASEAYLEGAPVREARELVAELCRHFYAQGWVTGTGGSITVKVNDPTVPLADRLIVMSPSGVQKERMVAEDMYVMAADGKVLSAPVAKPWPNKPPKCTDCAPLFMKAYLMRGAGAVIHSHGIETCIATMLIPGAKEFRVTHMEMIKGIKGHGYHDELVIPIIENTPYEYELTDSLSEAIAAYPKATAVLVRNHGIYVWGESWINAKTQAECYHYLLDACIKLYQLGIDWTTPEHGSINNPRRPHSILSPEICNGCHAADSSKCVVLDIEGTTTPISFVTDVMFPYARDNVRKHLTSTFDFEETKEDIKLLRIQIEDDLQNGVAGAVPVPPDEGGKEEVINSLVANVESMIKADRKITSLKQLQGHIWRIGFQKKELQGVVFEDVPVALKNWHASGIKVYIYSSGSREAQRLLFGNTTYGDLRKFLCGYFDTTTGNKRETRSYFEISQSLGVDSPSQILFITDVFQEAIAAKNAGFEVIISIRPGNAPLPDNHGFRTIKSFSEI

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A804NLJ4A0A804NLJ4_MAIZE100282341498
A0A804NLJ5A0A804NLJ5_MAIZE100282341447

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict61in Ref. 2; ACG32666
Sequence conflict333in Ref. 2; ACG32666

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BT042841
EMBL· GenBank· DDBJ
ACF87846.1
EMBL· GenBank· DDBJ
mRNA
EU960548
EMBL· GenBank· DDBJ
ACG32666.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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