B4G0F3 · MTBC_MAIZE
- ProteinProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Catalytic activity
- S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 zinc ion per subunit.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 114 | substrate 1; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: C | ||||||
Binding site | 132 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 134 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 157 | Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: E | ||||||
Binding site | 207 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 281 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 283 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 416-417 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: SS | ||||||
Binding site | 450 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: K | ||||||
Binding site | 476 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity | |
Molecular Function | 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity | |
Molecular Function | acireductone synthase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | methylthioribulose 1-phosphate dehydratase activity | |
Molecular Function | zinc ion binding | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | L-methionine salvage from S-adenosylmethionine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
Including 2 domains:
- Recommended nameMethylthioribulose-1-phosphate dehydratase
- EC number
- Short namesMTRu-1-P dehydratase
- Recommended nameEnolase-phosphatase E1
- EC number
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionB4G0F3
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000394156 | 1-517 | Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 | |||
Sequence: MACSGCSCEAAVGAMASEAYLEGAPVREARELVAELCRHFYAQGWVTGTGGSITVKVNDPTVPLADRLIVMSPSGVQKERMVAEDMYVMAADGKVLSAPVAKPWPNKPPKCTDCAPLFMKAYLMRGAGAVIHSHGIETCIATMLIPGAKEFRVTHMEMIKGIKGHGYHDELVIPIIENTPYEYELTDSLSEAIAAYPKATAVLVRNHGIYVWGESWINAKTQAECYHYLLDACIKLYQLGIDWTTPEHGSINNPRRPHSILSPEICNGCHAADSSKCVVLDIEGTTTPISFVTDVMFPYARDNVRKHLTSTFDFEETKEDIKLLRIQIEDDLQNGVAGAVPVPPDEGGKEEVINSLVANVESMIKADRKITSLKQLQGHIWRIGFQKKELQGVVFEDVPVALKNWHASGIKVYIYSSGSREAQRLLFGNTTYGDLRKFLCGYFDTTTGNKRETRSYFEISQSLGVDSPSQILFITDVFQEAIAAKNAGFEVIISIRPGNAPLPDNHGFRTIKSFSEI |
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-242 | Methylthioribulose-1-phosphate dehydratase | ||||
Sequence: MACSGCSCEAAVGAMASEAYLEGAPVREARELVAELCRHFYAQGWVTGTGGSITVKVNDPTVPLADRLIVMSPSGVQKERMVAEDMYVMAADGKVLSAPVAKPWPNKPPKCTDCAPLFMKAYLMRGAGAVIHSHGIETCIATMLIPGAKEFRVTHMEMIKGIKGHGYHDELVIPIIENTPYEYELTDSLSEAIAAYPKATAVLVRNHGIYVWGESWINAKTQAECYHYLLDACIKLYQLGID | ||||||
Region | 278-517 | Enolase-phosphatase E1 | ||||
Sequence: VVLDIEGTTTPISFVTDVMFPYARDNVRKHLTSTFDFEETKEDIKLLRIQIEDDLQNGVAGAVPVPPDEGGKEEVINSLVANVESMIKADRKITSLKQLQGHIWRIGFQKKELQGVVFEDVPVALKNWHASGIKVYIYSSGSREAQRLLFGNTTYGDLRKFLCGYFDTTTGNKRETRSYFEISQSLGVDSPSQILFITDVFQEAIAAKNAGFEVIISIRPGNAPLPDNHGFRTIKSFSEI |
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 statusComplete
- Length517
- Mass (Da)56,970
- Last updated2008-09-23 v1
- ChecksumC23101545CF82A4F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A804NLJ4 | A0A804NLJ4_MAIZE | 100282341 | 498 | ||
A0A804NLJ5 | A0A804NLJ5_MAIZE | 100282341 | 447 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 61 | in Ref. 2; ACG32666 | ||||
Sequence: T → A | ||||||
Sequence conflict | 333 | in Ref. 2; ACG32666 | ||||
Sequence: Q → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BT042841 EMBL· GenBank· DDBJ | ACF87846.1 EMBL· GenBank· DDBJ | mRNA | ||
EU960548 EMBL· GenBank· DDBJ | ACG32666.1 EMBL· GenBank· DDBJ | mRNA |