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ECOLI:ASNB
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | asnB | |
| Protein Name(s) | Asparagine synthetase B [glutamine-hydrolyzing]
AS-B | |
| External Links | ||
| UniProt | P22106 | |
| EMBL | J05554 U00096 AP009048 | |
| PIR | A36616 | |
| RefSeq | NP_415200.1 YP_488954.1 | |
| PDB | 1CT9 | |
| PDBsum | 1CT9 | |
| ProteinModelPortal | P22106 | |
| SMR | P22106 | |
| DIP | DIP-9177N | |
| IntAct | P22106 | |
| MINT | MINT-1306603 | |
| STRING | 511145.b0674 | |
| MEROPS | C44.976 | |
| PaxDb | P22106 | |
| PRIDE | P22106 | |
| EnsemblBacteria | AAC73768 BAA35317 | |
| GeneID | 12932818 945281 | |
| KEGG | ecj:Y75_p0653 eco:b0674 | |
| PATRIC | 32116529 | |
| EchoBASE | EB0090 | |
| EcoGene | EG10092 | |
| eggNOG | COG0367 | |
| HOGENOM | HOG000027493 | |
| InParanoid | P22106 | |
| KO | K01953 | |
| OMA | DWSGIYS | |
| OrthoDB | EOG6J48H7 | |
| PhylomeDB | P22106 | |
| BioCyc | EcoCyc:ASNSYNB-MONOMER ECOL316407:JW0660-MONOMER MetaCyc:ASNSYNB-MONOMER | |
| UniPathway | UPA00134 | |
| EvolutionaryTrace | P22106 | |
| PRO | PR:P22106 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P22106 | |
| GO | GO:0005737 GO:0016597 GO:0004066 GO:0004071 GO:0005524 GO:0042802 GO:0006529 GO:0008652 GO:0009063 GO:0006541 GO:0070981 | |
| Gene3D | 3.40.50.620 3.60.20.10 | |
| InterPro | IPR006426 IPR001962 IPR017932 IPR000583 IPR029055 IPR014729 | |
| Pfam | PF00733 PF13537 | |
| PIRSF | PIRSF001589 | |
| SUPFAM | SSF56235 | |
| TIGRFAMs | TIGR01536 | |
| PROSITE | PS51278 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004066 |
asparagine synthase (glutamine-hydrolyzing) activity |
ECO:0000270 |
F |
Tables VI and VII show that when the gene was activated, it produced asparagine, and when it was inhibited, it stopped the production of Asparagine. Therefore, they concluded that Asparagine synthase was resonsible for the production of Asparagine. |
complete | |||||
|
enables |
GO:0016597 |
amino acid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006529 |
asparagine biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004071 |
aspartate-ammonia ligase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004066 |
asparagine synthase (glutamine-hydrolyzing) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10092 |
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:0016597 |
amino acid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009063 |
cellular amino acid catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0008652 |
cellular amino acid biosynthetic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006541 |
glutamine metabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006529 |
asparagine biosynthetic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004066 |
asparagine synthase (glutamine-hydrolyzing) activity |
ECO:0000315 |
mutant phenotype 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:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004066 |
asparagine synthase (glutamine-hydrolyzing) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006529 |
asparagine biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004066 |
asparagine synthase (glutamine-hydrolyzing) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006541 |
glutamine metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016874 |
ligase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006529 |
asparagine biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0070981 |
L-asparagine biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00134 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Cedar, H & Schwartz, JH (1969) The asparagine synthetase of Escherhic coli. I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products. J. Biol. Chem. 244 4112-21 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Boehlein, SK et al. (1994) Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. J. Biol. Chem. 269 7450-7 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
- ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
- ↑ Rajagopala, SV et al. (2012) Studying protein complexes by the yeast two-hybrid system. Methods 58 392-9 PubMed GONUTS page
- ↑ 6.0 6.1 Parr, IB et al. (1996) Mapping the aspartic acid binding site of Escherichia coli asparagine synthetase B using substrate analogs. J. Med. Chem. 39 2367-78 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 Humbert, R & Simoni, RD (1980) Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli. J. Bacteriol. 142 212-20 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
- ↑ Boehlein, SK et al. (1998) Kinetic mechanism of Escherichia coli asparagine synthetase B. Biochemistry 37 13230-8 PubMed GONUTS page
a
- GO:0016597 ! amino acid binding
- GO:0008652 ! amino acid biosynthetic process
- GO:0009063 ! amino acid catabolic process
- GO:0006529 ! asparagine biosynthetic process
- GO:0004066 ! asparagine synthase (glutamine-hydrolyzing) activity
- GO:0004071 ! aspartate-ammonia ligase activity
- GO:0005524 ! ATP binding
b
