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ECOLI:ALKH
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | eda (synonyms: hga, kdgA) | |
| Protein Name(s) | KHG/KDPG aldolase
4-hydroxy-2-oxoglutarate aldolase 2-keto-4-hydroxyglutarate aldolase KHG-aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase 2-keto-3-deoxy-6-phosphogluconate aldolase KDPG-aldolase Phospho-2-dehydro-3-deoxygluconate aldolase Phospho-2-keto-3-deoxygluconate aldolase | |
| External Links | ||
| UniProt | P0A955 | |
| EMBL | X68871 M87458 L20897 X63694 U00096 AP009048 | |
| PIR | B42986 | |
| RefSeq | NP_416364.1 YP_490112.1 | |
| PDB | 1EUA 1EUN 1FQ0 1FWR 1WAU 1WBH 2C0A | |
| PDBsum | 1EUA 1EUN 1FQ0 1FWR 1WAU 1WBH 2C0A | |
| ProteinModelPortal | P0A955 | |
| SMR | P0A955 | |
| DIP | DIP-36196N | |
| IntAct | P0A955 | |
| STRING | 511145.b1850 | |
| SWISS-2DPAGE | P0A955 | |
| PaxDb | P0A955 | |
| PRIDE | P0A955 | |
| EnsemblBacteria | AAC74920 BAA15658 | |
| GeneID | 12930159 946367 | |
| KEGG | ecj:Y75_p1826 eco:b1850 | |
| PATRIC | 32119021 | |
| EchoBASE | EB0252 | |
| EcoGene | EG10256 | |
| eggNOG | COG0800 | |
| HOGENOM | HOG000233114 | |
| InParanoid | P0A955 | |
| KO | K01625 | |
| OMA | PKNLIQN | |
| OrthoDB | EOG67DPKT | |
| PhylomeDB | P0A955 | |
| BioCyc | EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER ECOL316407:JW1839-MONOMER MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER | |
| UniPathway | UPA00227 UPA00856 | |
| EvolutionaryTrace | P0A955 | |
| PRO | PR:P0A955 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0A955 | |
| GO | GO:0005829 GO:0016020 GO:0008675 GO:0008700 GO:0042802 | |
| Gene3D | 3.20.20.70 | |
| InterPro | IPR000887 IPR013785 | |
| Pfam | PF01081 | |
| TIGRFAMs | TIGR01182 | |
| PROSITE | PS00159 PS00160 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0009255 |
Entner-Doudoroff pathway |
ECO:0000315 |
P |
See Table 2. The EDA mutants were unable to grow on gluconate, the precursor for the Enter-Doudoroff pathway, as well as several other sugar acids. |
complete | |||||
|
part_of |
GO:0016020 |
membrane |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008700 |
4-hydroxy-2-oxoglutarate aldolase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008675 |
2-dehydro-3-deoxy-phosphogluconate aldolase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0106009 |
(4S)-4-hydroxy-2-oxoglutarate aldolase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016833 |
oxo-acid-lyase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016833 |
oxo-acid-lyase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008948 |
oxaloacetate decarboxylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008675 |
2-dehydro-3-deoxy-phosphogluconate aldolase 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:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0043725 |
2-keto-3-deoxygluconate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008700 |
4-hydroxy-2-oxoglutarate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008675 |
2-dehydro-3-deoxy-phosphogluconate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008152 |
metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Fradkin, JE & Fraenkel, DG (1971) 2-keto-3-deoxygluconate 6-phosphate aldolase mutants of Escherichia coli. J. Bacteriol. 108 1277-83 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
- ↑ Walters, MJ et al. (2008) Characterization and crystal structure of Escherichia coli KDPGal aldolase. Bioorg. Med. Chem. 16 710-20 PubMed GONUTS page
- ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 Nishihara, H & Dekker, EE (1972) Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J. Biol. Chem. 247 5079-87 PubMed GONUTS page
- ↑ Wang, JK et al. (1981) Physical and chemical evidence for the trimeric subunit structure of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli K-12. J. Biol. Chem. 256 1793-800 PubMed GONUTS page
- ↑ Patil, RV & Dekker, EE (1992) Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene. J. Bacteriol. 174 102-7 PubMed GONUTS page
- ↑ Fong, S et al. (2000) Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars. Chem. Biol. 7 873-83 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
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