K5B7Z4 · K5B7Z4_MYCHD
- ProteinGlucosyl-3-phosphoglycerate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids314 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- (2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + UDP + H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 49 | UDP (UniProtKB | ChEBI) | |||
Binding site | 49 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 51 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 51 | UDP (UniProtKB | ChEBI) | |||
Binding site | 51 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 78 | UDP (UniProtKB | ChEBI) | |||
Binding site | 78 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 110 | UDP (UniProtKB | ChEBI) | |||
Binding site | 110 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 111 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 131 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 132 | UDP (UniProtKB | ChEBI) | |||
Binding site | 132 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 133 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 178 | (R)-malate 2 (UniProtKB | ChEBI) | |||
Binding site | 178 | (S)-malate (UniProtKB | ChEBI) | |||
Binding site | 180 | (R)-malate 2 (UniProtKB | ChEBI) | |||
Binding site | 180 | (R)-malate 1 (UniProtKB | ChEBI) | |||
Binding site | 180 | (S)-malate (UniProtKB | ChEBI) | |||
Binding site | 181 | (R)-malate 1 (UniProtKB | ChEBI) | |||
Binding site | 181 | (R)-malate 2 (UniProtKB | ChEBI) | |||
Binding site | 181 | (S)-malate (UniProtKB | ChEBI) | |||
Binding site | 223 | UDP (UniProtKB | ChEBI) | |||
Binding site | 223 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 226 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
Binding site | 253 | (S)-malate (UniProtKB | ChEBI) | |||
Binding site | 255 | (R)-malate 2 (UniProtKB | ChEBI) | |||
Binding site | 255 | (R)-malate 1 (UniProtKB | ChEBI) | |||
Binding site | 255 | UDP (UniProtKB | ChEBI) | |||
Binding site | 255 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glycosyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucosyl-3-phosphoglycerate synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionK5B7Z4
Proteomes
Interaction
Protein-protein interaction databases
Sequence
- Sequence statusComplete
- Length314
- Mass (Da)33,592
- Last updated2013-01-09 v1
- MD5 Checksum7C8AE0572C42001DE73503653B4BD7E7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AMRA01000093 EMBL· GenBank· DDBJ | EKF22803.1 EMBL· GenBank· DDBJ | Genomic DNA |