Ontology | Accession | Term | GO Evidence | Evidence Ontology (ECO) Code | Reference | Comments |
---|---|---|---|---|---|---|
Biological Process | GO:0006006 | glucose metabolic process |
Inferred from Sequence Model
Term mapped from: InterPro:PIRSF000110
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Molecular Function | GO:0050661 | NADP binding |
Inferred from Sequence Model
Term mapped from: InterPro:PIRSF000110
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Molecular Function | GO:0016614 | oxidoreductase activity, acting on CH-OH group of donors |
Inferred from Sequence Model
Term mapped from: InterPro:PIRSF000110
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Molecular Function | GO:0004345 | glucose-6-phosphate dehydrogenase activity |
Inferred from Sequence Model
Term mapped from: InterPro:PF02781
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
|
Database | Xref | Pathway | Version | Evidence | PMID |
---|---|---|---|---|---|
KEGG | paf01120 | Microbial metabolism in diverse environments | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf00480 | Glutathione metabolism | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf01200 | Carbon metabolism | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf01100 | Metabolic pathways | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf01110 | Biosynthesis of secondary metabolites | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf00030 | Pentose phosphate pathway | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
|
KEGG | paf01130 | Biosynthesis of antibiotics | 81.0+/01-23, Jan 17 |
ECO:0000249
sequence similarity evidence used in automatic assertion |
Analysis | Accession | Description | Interpro Accession | Interpro Description | Amino Acid Start | Amino Acid Stop | E-value |
---|---|---|---|---|---|---|---|
PIRSF | PIRSF000110 | G6PD | IPR001282 | Glucose-6-phosphate dehydrogenase | 1 | 488 | 0.0 |
PRINTS | PR00079 | Glucose-6-phosphate dehydrogenase signature | IPR001282 | Glucose-6-phosphate dehydrogenase | 220 | 237 | 6.5E-49 |
PRINTS | PR00079 | Glucose-6-phosphate dehydrogenase signature | IPR001282 | Glucose-6-phosphate dehydrogenase | 144 | 157 | 6.5E-49 |
PANTHER | PTHR23429 | GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD | IPR001282 | Glucose-6-phosphate dehydrogenase | 8 | 485 | 0.0 |
Pfam | PF02781 | Glucose-6-phosphate dehydrogenase, C-terminal domain | IPR022675 | Glucose-6-phosphate dehydrogenase, C-terminal | 190 | 486 | 2.6E-123 |
PRINTS | PR00079 | Glucose-6-phosphate dehydrogenase signature | IPR001282 | Glucose-6-phosphate dehydrogenase | 238 | 254 | 6.5E-49 |
NCBIfam | TIGR00871 | JCVI: glucose-6-phosphate dehydrogenase | IPR001282 | Glucose-6-phosphate dehydrogenase | 9 | 486 | 0.0 |
PRINTS | PR00079 | Glucose-6-phosphate dehydrogenase signature | IPR001282 | Glucose-6-phosphate dehydrogenase | 168 | 196 | 6.5E-49 |
SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains | IPR036291 | NAD(P)-binding domain superfamily | 5 | 191 | 3.74E-53 |
Hamap | MF_00966 | Glucose-6-phosphate 1-dehydrogenase [zwf]. | IPR001282 | Glucose-6-phosphate dehydrogenase | 9 | 488 | 82.590828 |
Pfam | PF00479 | Glucose-6-phosphate dehydrogenase, NAD binding domain | IPR022674 | Glucose-6-phosphate dehydrogenase, NAD-binding | 14 | 188 | 5.2E-54 |
Gene3D | G3DSA:3.40.50.720 | - | - | - | 12 | 436 | 0.0 |
SUPERFAMILY | SSF55347 | Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain | - | - | 178 | 487 | 2.19E-116 |
Gene3D | G3DSA:3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 | - | - | 178 | 476 | 0.0 |
PRINTS | PR00079 | Glucose-6-phosphate dehydrogenase signature | IPR001282 | Glucose-6-phosphate dehydrogenase | 329 | 355 | 6.5E-49 |