A0A370P3Q0 · A0A370P3Q0_ASPPH
- ProteinPhosphomannomutase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids436 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic activity
- alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Cofactor
Pathway
Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 192 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 192 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 194 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 194 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 201 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 306 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 317 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 324 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 362 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 364 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 398 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 410 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 412 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | metal ion binding | |
Molecular Function | phosphomannomutase activity | |
Biological Process | GDP-mannose biosynthetic process | |
Biological Process | mannose metabolic process | |
Biological Process | protein N-linked glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphomannomutase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus
Accessions
- Primary accessionA0A370P3Q0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MLSSEPCRESLKSHPDRVPVDSPERAART | ||||||
Domain | 1-55 | J | ||||
Sequence: MLSSEPCRESLKSHPDRVPVDSPERAARTRKFQEISDAYYTLSDVSRRREYDAMR | ||||||
Compositional bias | 9-29 | Basic and acidic residues | ||||
Sequence: ESLKSHPDRVPVDSPERAART |
Sequence similarities
Belongs to the eukaryotic PMM family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length436
- Mass (Da)48,940
- Last updated2018-11-07 v1
- Checksum0C33F9E92555E373
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-29 | Basic and acidic residues | ||||
Sequence: ESLKSHPDRVPVDSPERAART |