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MICEC:Q8KNF2
Contents
Species (Taxon ID) | Micromonospora echinospora (Micromonospora purpurea). (1877) | |
Gene Name(s) | calG1 (ECO:0000313 with EMBL:AAM70336.1) | |
Protein Name(s) | CalG1 (ECO:0000313 with EMBL:AAM70336.1) | |
External Links | ||
UniProt | Q8KNF2 | |
EMBL | AF497482 | |
PDB | 3OTG 3OTH | |
PDBsum | 3OTG 3OTH | |
ProteinModelPortal | Q8KNF2 | |
CAZy | GT1 | |
GO | GO:0030246 GO:0016758 GO:0030259 | |
InterPro | IPR010610 IPR004276 IPR007235 IPR002213 | |
PANTHER | PTHR11926 | |
Pfam | PF06722 PF04101 PF03033 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0016757 |
transferase activity, transferring glycosyl groups |
ECO:0000314 |
F |
CalG1 is a glycosyltransferase in the calicheamicin gene cluster found in the Micromonospora echinospora organism. Its structure is solved by X-ray crystallography, as shown in Fig 2D & 3D. |
complete | |||||
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
GO:0016757 |
transferase activity, transferring glycosyl groups |
ECO:0000314 |
F |
CalG1 is a glycosyltransferase from the calicheamicin gene cluster in the organism, Micromonospora echinospora. Its function is characterized via HPLC and Mass spectrometry (Fig 1). |
complete | |||||
enables |
GO:0016758 |
transferase activity, transferring hexosyl groups |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0030259 |
lipid glycosylation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Chang, A et al. (2011) Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity. Proc. Natl. Acad. Sci. U.S.A. 108 17649-54 PubMed GONUTS page
- ↑ Zhang, C et al. (2006) Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions. Science 313 1291-4 PubMed GONUTS page
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