A0A158NP52 · A0A158NP52_ATTCE
- ProteinEnolase-phosphatase E1
- Gene105622504
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids716 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic activity
- 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Cofactor
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 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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
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 | |
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 nameEnolase-phosphatase E1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Myrmicinae > Atta
Accessions
- Primary accessionA0A158NP52
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 265-468 | Disordered | ||||
Sequence: RQKIETTDDKVDEGTADVSEPMDTSEDVEMSNVSDKKVEKNDAKEVTESIEKECAKDQPSESTSISSGQVEESAIDEKDVSNTEQKITESNVKSEESINEESGSSENAKSDVKDDVTPATKDNDKDIAEKTEENLDTTATEITAADDSMDVSVPESASKSETTITSSEKKIEDSTDVTKDTQAEDVDKTETIKSDEKADNIVPQ | ||||||
Compositional bias | 266-281 | Basic and acidic residues | ||||
Sequence: QKIETTDDKVDEGTAD | ||||||
Compositional bias | 293-322 | Basic and acidic residues | ||||
Sequence: EMSNVSDKKVEKNDAKEVTESIEKECAKDQ | ||||||
Compositional bias | 336-400 | Basic and acidic residues | ||||
Sequence: ESAIDEKDVSNTEQKITESNVKSEESINEESGSSENAKSDVKDDVTPATKDNDKDIAEKTEENLD | ||||||
Compositional bias | 429-461 | Basic and acidic residues | ||||
Sequence: TSSEKKIEDSTDVTKDTQAEDVDKTETIKSDEK | ||||||
Region | 524-687 | Disordered | ||||
Sequence: VTENGEATETATEKTTVSEAVTETEETVTDVRKEATASTEVSAEKSSEIIAESEKADEKVQTMETETTDADKCENETTQQETIKEEETVKEENVVDTKDKTTVDSEKQKLNGTTQNGNTDVPVLDDKLHSNGLNEGPSKETTNEDAAAQNGEPESLSESSAESI | ||||||
Compositional bias | 528-547 | Polar residues | ||||
Sequence: GEATETATEKTTVSEAVTET | ||||||
Compositional bias | 548-562 | Basic and acidic residues | ||||
Sequence: EETVTDVRKEATAST | ||||||
Compositional bias | 570-629 | Basic and acidic residues | ||||
Sequence: SEIIAESEKADEKVQTMETETTDADKCENETTQQETIKEEETVKEENVVDTKDKTTVDSE | ||||||
Compositional bias | 630-644 | Polar residues | ||||
Sequence: KQKLNGTTQNGNTDV | ||||||
Compositional bias | 657-685 | Polar residues | ||||
Sequence: NEGPSKETTNEDAAAQNGEPESLSESSAE |
Sequence similarities
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length716
- Mass (Da)78,749
- Last updated2016-06-08 v1
- ChecksumB9CF916F5078FB3A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 266-281 | Basic and acidic residues | ||||
Sequence: QKIETTDDKVDEGTAD | ||||||
Compositional bias | 293-322 | Basic and acidic residues | ||||
Sequence: EMSNVSDKKVEKNDAKEVTESIEKECAKDQ | ||||||
Compositional bias | 336-400 | Basic and acidic residues | ||||
Sequence: ESAIDEKDVSNTEQKITESNVKSEESINEESGSSENAKSDVKDDVTPATKDNDKDIAEKTEENLD | ||||||
Compositional bias | 429-461 | Basic and acidic residues | ||||
Sequence: TSSEKKIEDSTDVTKDTQAEDVDKTETIKSDEK | ||||||
Compositional bias | 528-547 | Polar residues | ||||
Sequence: GEATETATEKTTVSEAVTET | ||||||
Compositional bias | 548-562 | Basic and acidic residues | ||||
Sequence: EETVTDVRKEATAST | ||||||
Compositional bias | 570-629 | Basic and acidic residues | ||||
Sequence: SEIIAESEKADEKVQTMETETTDADKCENETTQQETIKEEETVKEENVVDTKDKTTVDSE | ||||||
Compositional bias | 630-644 | Polar residues | ||||
Sequence: KQKLNGTTQNGNTDV | ||||||
Compositional bias | 657-685 | Polar residues | ||||
Sequence: NEGPSKETTNEDAAAQNGEPESLSESSAE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADTU01022225 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |