A0A286R6V2 · A0A286R6V2_TRIUA
- ProteinGlucose-1-phosphate adenylyltransferase
- GeneAgp1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids473 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Catalytic activity
- alpha-D-glucose 1-phosphate + ATP + H+ = ADP-alpha-D-glucose + diphosphate
Pathway
Glycan biosynthesis; starch biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | amyloplast | |
Cellular Component | chloroplast | |
Molecular Function | ATP binding | |
Molecular Function | glucose-1-phosphate adenylyltransferase activity | |
Biological Process | glycogen biosynthetic process | |
Biological Process | starch biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucose-1-phosphate adenylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Triticinae > Triticum
Accessions
- Primary accessionA0A286R6V2
Subcellular Location
Interaction
Subunit
Heterotetramer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MDVPLASKTFPSPSPSKREQCNIDGHKSSSKHADLN | ||||||
Compositional bias | 20-34 | Basic and acidic residues | ||||
Sequence: QCNIDGHKSSSKHAD | ||||||
Domain | 45-318 | Nucleotidyl transferase | ||||
Sequence: GIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYGSNIGGYKNEGFVEVLAAQQSPDNPDWFQGTADAVRQYLWLFEEHNVMEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEERATAFGLMKIDEEGRIIEFAEKPKGEQLKAMMVDTTILGLDDARAKEMPYIASMGIYVISKHVMLQLLREQFPGANDFGSEVIPGATSTGMRVQAYLYDGYWEDIGTIEAFYNANLGITK |
Sequence similarities
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)52,075
- Last updated2017-11-22 v1
- Checksum92950731919BA0DF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 20-34 | Basic and acidic residues | ||||
Sequence: QCNIDGHKSSSKHAD |