GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
ECOLI:GLDA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | gldA | |
| Protein Name(s) | Glycerol dehydrogenase
GDH GLDH | |
| External Links | ||
| UniProt | P0A9S5 | |
| EMBL | U00006 U00096 AP009048 | |
| PIR | D65201 | |
| RefSeq | NP_418380.4 YP_491506.1 | |
| ProteinModelPortal | P0A9S5 | |
| SMR | P0A9S5 | |
| BioGrid | 852737 | |
| DIP | DIP-47916N | |
| IntAct | P0A9S5 | |
| STRING | 511145.b3945 | |
| PaxDb | P0A9S5 | |
| PRIDE | P0A9S5 | |
| EnsemblBacteria | AAC76927 BAE77365 | |
| GeneID | 12933659 948440 | |
| KEGG | ecj:Y75_p3242 eco:b3945 | |
| PATRIC | 32123413 | |
| EchoBASE | EB1849 | |
| EcoGene | EG11904 | |
| eggNOG | COG0371 | |
| HOGENOM | HOG000031784 | |
| InParanoid | P0A9S5 | |
| KO | K00005 | |
| OMA | FQSPSKY | |
| OrthoDB | EOG67432X | |
| PhylomeDB | P0A9S5 | |
| BioCyc | EcoCyc:GLYCDEH-MONOMER ECOL316407:JW5556-MONOMER MetaCyc:GLYCDEH-MONOMER | |
| SABIO-RK | P0A9S5 | |
| UniPathway | UPA00617 | |
| PRO | PR:P0A9S5 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0A9S5 | |
| GO | GO:0019147 GO:0008888 GO:0042802 GO:0046872 GO:0019588 GO:0051596 | |
| InterPro | IPR001670 IPR018211 IPR016205 | |
| Pfam | PF00465 | |
| PIRSF | PIRSF000112 | |
| PROSITE | PS00913 PS00060 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0008888 |
glycerol dehydrogenase activity |
ECO:0000314 |
F |
Tables 2 & 4 |
complete | |||||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11904 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008888 |
glycerol dehydrogenase [NAD+] activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051596 |
methylglyoxal catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019588 |
anaerobic glycerol catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0019147 |
(R)-aminopropanol dehydrogenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008888 |
glycerol dehydrogenase [NAD+] activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016614 |
oxidoreductase activity, acting on CH-OH group of donors |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008888 |
glycerol dehydrogenase [NAD+] activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006071 |
glycerol metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019588 |
anaerobic glycerol catabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00617 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Truniger, V & Boos, W (1994) Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase. J. Bacteriol. 176 1796-800 PubMed GONUTS page
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 3.0 3.1 Gonzalez, R et al. (2008) A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli. Metab. Eng. 10 234-45 PubMed GONUTS page
- ↑ Kelley, JJ & Dekker, EE (1984) D-1-amino-2-propanol:NAD+ oxidoreductase. Purification and general properties of the large molecular form of the enzyme from Escherichia coli K12. J. Biol. Chem. 259 2124-9 PubMed GONUTS page
- ↑ Campbell, RL et al. (1978) Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD+ oxidoreductase activity from extracts of Escherichia coli K-12. J. Biol. Chem. 253 7282-8 PubMed GONUTS page
- ↑ Tang, CT et al. (1979) Purification and properties of a nicotinamide adenine dinucleotide-linked dehydrogenase that serves an Escherichia coli mutant for glycerol catabolism. J. Bacteriol. 140 182-7 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
