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ECOLI:ALDA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | aldA (synonyms: ald) | |
| Protein Name(s) | Lactaldehyde dehydrogenase
Aldehyde dehydrogenase A Glycolaldehyde dehydrogenase | |
| External Links | ||
| UniProt | P25553 | |
| EMBL | M64541 U00096 AP009048 | |
| PIR | A38165 | |
| RefSeq | NP_415933.1 YP_489682.1 | |
| PDB | 2HG2 2ILU 2IMP 2OPX | |
| PDBsum | 2HG2 2ILU 2IMP 2OPX | |
| ProteinModelPortal | P25553 | |
| SMR | P25553 | |
| BioGrid | 850044 | |
| DIP | DIP-9081N | |
| IntAct | P25553 | |
| MINT | MINT-1313045 | |
| STRING | 511145.b1415 | |
| SWISS-2DPAGE | P25553 | |
| PaxDb | P25553 | |
| PRIDE | P25553 | |
| EnsemblBacteria | AAC74497 BAA15032 | |
| GeneID | 12931179 945672 | |
| KEGG | ecj:Y75_p1391 eco:b1415 | |
| PATRIC | 32118116 | |
| EchoBASE | EB0034 | |
| EcoGene | EG10035 | |
| eggNOG | COG1012 | |
| HOGENOM | HOG000271509 | |
| InParanoid | P25553 | |
| KO | K07248 | |
| OMA | LANIMIR | |
| OrthoDB | EOG6BS8QW | |
| PhylomeDB | P25553 | |
| BioCyc | EcoCyc:LACTALDDEHYDROG-MONOMER ECOL316407:JW1412-MONOMER MetaCyc:LACTALDDEHYDROG-MONOMER | |
| BRENDA | 1.2.1.22 | |
| SABIO-RK | P25553 | |
| EvolutionaryTrace | P25553 | |
| PRO | PR:P25553 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P25553 | |
| GO | GO:0050569 GO:0008911 GO:0004777 GO:0042355 GO:0019301 | |
| Gene3D | 3.40.309.10 3.40.605.10 | |
| InterPro | IPR016161 IPR016163 IPR016160 IPR029510 IPR016162 IPR015590 | |
| Pfam | PF00171 | |
| SUPFAM | SSF53720 | |
| PROSITE | PS00070 PS00687 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0009013 |
succinate-semialdehyde dehydrogenase [NAD(P)+] activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11329 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004777 |
succinate-semialdehyde dehydrogenase (NAD+) activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11329 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008911 |
lactaldehyde dehydrogenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051289 |
protein homotetramerization |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0050569 |
glycolaldehyde dehydrogenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
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:0042355 |
L-fucose catabolic process |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019301 |
rhamnose catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008911 |
lactaldehyde dehydrogenase 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 | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004777 |
succinate-semialdehyde dehydrogenase (NAD+) activity |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
F |
Seeded From UniProt |
Missing: with/from | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR015590 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016620 |
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
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 |
InterPro:IPR015590 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0050569 |
glycolaldehyde dehydrogenase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008911 |
lactaldehyde dehydrogenase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Sridhara, S & Wu, TT (1969) Purification and properties of lactaldehyde dehydrogenase from Escherichia coli. J. Biol. Chem. 244 5233-8 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Baldomà, L & Aguilar, J (1987) Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12. J. Biol. Chem. 262 13991-6 PubMed GONUTS page
- ↑ Hacking, AJ & Lin, EC (1976) Disruption of the fucose pathway as a consequence of genetic adaptation to propanediol as a carbon source in Escherichia coli. J. Bacteriol. 126 1166-72 PubMed GONUTS page
- ↑ Chen, YM et al. (1987) NAD-linked aldehyde dehydrogenase for aerobic utilization of L-fucose and L-rhamnose by Escherichia coli. J. Bacteriol. 169 3289-94 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 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
- ↑ Reed, JL et al. (2003) An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR). Genome Biol. 4 R54 PubMed GONUTS page
