O27819 · O27819_METTH
- Proteinglucose-1-phosphate thymidylyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids292 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- alpha-D-glucose 1-phosphate + dTTP + H+ = diphosphate + dTDP-alpha-D-glucose
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | dTDP 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 8 | dTDP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 8 | dTDP 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 23 | dTDP 3 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 23 | dTDP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 23 | dTDP 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 80 | dTDP 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 80 | dTDP 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 85 | dTDP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 85 | dTDP 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 85 | dTDP 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 108 | dTDP 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 108 | dTDP 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 113 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 114 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 115 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 116 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 117 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 249 | dTDP 4 (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glucose-1-phosphate thymidylyltransferase activity | |
Biological Process | extracellular polysaccharide biosynthetic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameglucose-1-phosphate thymidylyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanothermobacter
Accessions
- Primary accessionO27819
Proteomes
PTM/Processing
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-238 | Nucleotidyl transferase | ||||
Sequence: KGIVLAGGSGTRLYPITRAVSKQLLPIYDKPMIYYPLSVLMLAGIRDILIISTPRDLPLYRDLLGDGSQFGVRFSYRVQEEPRGIADAFIVGKDFIGDSKVALVLGDNVFYGHRFSEILRRAASLEDGAVIFGYYVRDPRPFGVVEFDSEGRVISIEEKPSRPKSNYVVPGLYFYDNQVVEIARRIEPSDRGELEITSVNEEYLRMGKLRVELMGRGMAWLDTGTHDGLLEASSFIE |
Sequence similarities
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length292
- Mass (Da)33,061
- Last updated1998-01-01 v1
- Checksum65D961F5DB10B13E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000666 EMBL· GenBank· DDBJ | AAB86257.1 EMBL· GenBank· DDBJ | Genomic DNA |