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ECOLI:AROG
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | aroG | |
| Protein Name(s) | Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase DAHP synthase Phospho-2-keto-3-deoxyheptonate aldolase | |
| External Links | ||
| UniProt | P0AB91 | |
| EMBL | J01591 U00096 AP009048 | |
| PIR | A01106 | |
| RefSeq | NP_415275.1 YP_489027.1 | |
| PDB | 1GG1 1KFL 1N8F 1QR7 | |
| PDBsum | 1GG1 1KFL 1N8F 1QR7 | |
| ProteinModelPortal | P0AB91 | |
| SMR | P0AB91 | |
| DIP | DIP-35898N | |
| IntAct | P0AB91 | |
| STRING | 511145.b0754 | |
| BindingDB | P0AB91 | |
| SWISS-2DPAGE | P0AB91 | |
| PaxDb | P0AB91 | |
| PRIDE | P0AB91 | |
| EnsemblBacteria | AAC73841 BAA35416 | |
| GeneID | 12932715 945605 | |
| KEGG | ecj:Y75_p0727 eco:b0754 | |
| PATRIC | 32116707 | |
| EchoBASE | EB0077 | |
| EcoGene | EG10079 | |
| eggNOG | COG0722 | |
| HOGENOM | HOG000220501 | |
| InParanoid | P0AB91 | |
| KO | K01626 | |
| OMA | GNIKIAT | |
| OrthoDB | EOG63JR9W | |
| PhylomeDB | P0AB91 | |
| BioCyc | EcoCyc:AROG-MONOMER ECOL316407:JW0737-MONOMER MetaCyc:AROG-MONOMER RETL1328306-WGS:GSTH-2382-MONOMER | |
| BRENDA | 2.5.1.54 | |
| SABIO-RK | P0AB91 | |
| UniPathway | UPA00053 | |
| EvolutionaryTrace | P0AB91 | |
| PRO | PR:P0AB91 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0AB91 | |
| GO | GO:0003849 GO:0042802 GO:0009073 GO:0009423 | |
| Gene3D | 3.20.20.70 | |
| InterPro | IPR013785 IPR006218 IPR006219 | |
| PANTHER | PTHR21225 | |
| Pfam | PF00793 | |
| PIRSF | PIRSF001361 | |
| TIGRFAMs | TIGR00034 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0009073 |
aromatic amino acid family biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10078 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10080 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003849 |
3-deoxy-7-phosphoheptulonate synthase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10078 |
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: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: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:0003849 |
3-deoxy-7-phosphoheptulonate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
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:0003849 |
3-deoxy-7-phosphoheptulonate synthase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009058 |
biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009073 |
aromatic amino acid family biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003849 |
3-deoxy-7-phosphoheptulonate synthase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009073 |
aromatic amino acid family biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008652 |
cellular amino acid biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009423 |
chorismate biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00053 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 2.0 2.1 McCandliss, RJ et al. (1978) 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli. J. Biol. Chem. 253 4259-65 PubMed GONUTS page
- ↑ Shumilin, IA et al. (1999) Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure 7 865-75 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
- ↑ Simpson, RJ & Davidson, BE (1976) Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe)from Escherichia coli K12. 2. Kinetic properties. Eur. J. Biochem. 70 501-7 PubMed GONUTS page
