A0A6C1SPT9 · A0A6C1SPT9_9PROT
- ProteinAlpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- GeneglgE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids700 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Catalytic activity
- alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl](n) = [(1->4)-alpha-D-glucosyl](n+2) + phosphate
CHEBI:63576 + [(1→4)-α-D-glucosyl](n) RHEA-COMP:9584 = [(1→4)-α-D-glucosyl](n+2) RHEA-COMP:10183 + CHEBI:43474
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 295 | alpha-maltose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 355 | alpha-maltose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 390 | alpha-maltose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 426 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 427 | alpha-maltose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 455 | Proton donor | ||||
Sequence: E | ||||||
Site | 513 | Transition state stabilizer | ||||
Sequence: D | ||||||
Binding site | 566-567 | alpha-maltose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: KY |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hexosyltransferase activity | |
Molecular Function | hydrolase activity, hydrolyzing O-glycosyl compounds | |
Biological Process | alpha-glucan biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- EC number
- Short namesGMPMT
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales
Accessions
- Primary accessionA0A6C1SPT9
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Disordered | ||||
Sequence: MPPKDEAASPPATPSQPAADDDAAPHRHHKDESARGRA | ||||||
Compositional bias | 21-38 | Basic and acidic residues | ||||
Sequence: DDAAPHRHHKDESARGRA | ||||||
Domain | 243-591 | Glycosyl hydrolase family 13 catalytic | ||||
Sequence: AAWYEMFPRSQGQIPGRSATFADCEARLPEVRRMGFDVVYFVPIHPIGRTFRKGRNNTLNAGPDDPGSPYAIGGPEGGHTAIHPELGTLEDFRRFVAACHAQGMEVALDFAVQCSPDHPWIKDHPEWFLFRADGSIKYAENPPKKYQDIVNVDFYCTDWQSLWEELLFVVNFWVDQGVKIFRVDNPHTKPVPFWEWLIREVQEKHPDVIFLAEAFTRPPMLKMMAKIGFGQSYTYFTWRHGKQELTEYLTELTQTDVKEYLRPNFFTNTPDINPPYLQTGGRPAHQIRLVLAATLSSVYGMYNGFELCEATPIPGKEEYLNSEKYEYKVWDWDQPGNIKDYITRINQIR |
Sequence similarities
Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length700
- Mass (Da)80,571
- Last updated2020-06-17 v1
- ChecksumC55A045F90564902
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 21-38 | Basic and acidic residues | ||||
Sequence: DDAAPHRHHKDESARGRA |