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ECOLI:AAT
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | aspC | |
Protein Name(s) | Aspartate aminotransferase
AspAT Transaminase A | |
External Links | ||
UniProt | P00509 | |
EMBL | X03629 X05904 U00096 AP009048 | |
PIR | A00598 | |
RefSeq | NP_415448.1 YP_489200.1 | |
PDB | 1AAM 1AAW 1AHE 1AHF 1AHG 1AHX 1AHY 1AIA 1AIB 1AIC 1AMQ 1AMR 1AMS 1ARG 1ARH 1ARI 1ARS 1ART 1ASA 1ASB 1ASC 1ASD 1ASE 1ASF 1ASG 1ASL 1ASM 1ASN 1B4X 1BQA 1BQD 1C9C 1CQ6 1CQ7 1CQ8 1CZC 1CZE 1G4V 1G4X 1G7W 1G7X 1IX6 1IX7 1IX8 1QIR 1QIS 1QIT 1SPA 1TOE 1TOG 1TOI 1TOJ 1TOK 1X28 1X29 1X2A 1YOO 2AAT 2D5Y 2D61 2D63 2D64 2D65 2D66 2D7Y 2D7Z 2Q7W 2QA3 2QB2 2QB3 2QBT 3AAT 3QN6 3QPG 3ZZJ 3ZZK 4A00 4DBC 4F5F 4F5G 4F5H 4F5I 4F5J 4F5K 4F5L 4F5M 5EAA | |
PDBsum | 1AAM 1AAW 1AHE 1AHF 1AHG 1AHX 1AHY 1AIA 1AIB 1AIC 1AMQ 1AMR 1AMS 1ARG 1ARH 1ARI 1ARS 1ART 1ASA 1ASB 1ASC 1ASD 1ASE 1ASF 1ASG 1ASL 1ASM 1ASN 1B4X 1BQA 1BQD 1C9C 1CQ6 1CQ7 1CQ8 1CZC 1CZE 1G4V 1G4X 1G7W 1G7X 1IX6 1IX7 1IX8 1QIR 1QIS 1QIT 1SPA 1TOE 1TOG 1TOI 1TOJ 1TOK 1X28 1X29 1X2A 1YOO 2AAT 2D5Y 2D61 2D63 2D64 2D65 2D66 2D7Y 2D7Z 2Q7W 2QA3 2QB2 2QB3 2QBT 3AAT 3QN6 3QPG 3ZZJ 3ZZK 4A00 4DBC 4F5F 4F5G 4F5H 4F5I 4F5J 4F5K 4F5L 4F5M 5EAA | |
ProteinModelPortal | P00509 | |
SMR | P00509 | |
DIP | DIP-9181N | |
IntAct | P00509 | |
STRING | 511145.b0928 | |
SWISS-2DPAGE | P00509 | |
PaxDb | P00509 | |
PRIDE | P00509 | |
EnsemblBacteria | AAC74014 BAA35674 | |
GeneID | 12931027 945553 | |
KEGG | ecj:Y75_p0900 eco:b0928 | |
PATRIC | 32117069 | |
EchoBASE | EB0094 | |
EcoGene | EG10096 | |
eggNOG | COG1448 | |
HOGENOM | HOG000185899 | |
InParanoid | P00509 | |
KO | K00813 | |
OMA | KIWISNP | |
OrthoDB | EOG6C2WBK | |
PhylomeDB | P00509 | |
BioCyc | EcoCyc:ASPAMINOTRANS-MONOMER ECOL316407:JW0911-MONOMER MetaCyc:ASPAMINOTRANS-MONOMER | |
BRENDA | 2.6.1.1 | |
SABIO-RK | P00509 | |
EvolutionaryTrace | P00509 | |
PRO | PR:P00509 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P00509 | |
GO | GO:0005737 GO:0005829 GO:0042802 GO:0004069 GO:0080130 GO:0004838 GO:0030170 GO:0009094 GO:0033585 | |
Gene3D | 3.40.640.10 | |
InterPro | IPR004839 IPR000796 IPR004838 IPR015424 IPR015421 | |
PANTHER | PTHR11879 | |
Pfam | PF00155 | |
PRINTS | PR00799 | |
SUPFAM | SSF53383 | |
PROSITE | PS00105 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0047319 |
aspartate-phenylpyruvate transaminase activity |
ECO:0000314 |
F |
Figure 1 shows increasing phenylalanine aminotransferase activity with increasing levels of enzyme. |
complete | |||||
GO:0008483 |
transaminase activity |
ECO:0000315 |
F |
Fig. 2 shows the difference in transamination rates between wild type AspAT and mutant forms. |
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:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0033585 |
L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0030170 |
pyridoxal phosphate binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004838 |
L-tyrosine:2-oxoglutarate aminotransferase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004069 |
L-aspartate:2-oxoglutarate aminotransferase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10096 |
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:0030170 |
pyridoxal phosphate binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009094 |
L-phenylalanine biosynthetic process |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
EcoliWiki:ilvE |
P |
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:0004838 |
L-tyrosine:2-oxoglutarate aminotransferase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004069 |
L-aspartate:2-oxoglutarate aminotransferase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0033585 |
L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
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 | |||
involved_in |
GO:0006520 |
cellular amino acid metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008483 |
transaminase 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 | |||
enables |
GO:0030170 |
pyridoxal phosphate binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004069 |
L-aspartate:2-oxoglutarate aminotransferase 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:0008483 |
transaminase activity |
ECO:0000322 |
imported manually asserted information 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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Powell, JT & Morrison, JF (1978) The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87 391-400 PubMed GONUTS page
- ↑ Birolo, L et al. (1999) Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase. Biochemistry 38 905-13 PubMed GONUTS page
- ↑ 3.0 3.1 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
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 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
- ↑ 6.0 6.1 6.2 6.3 Gelfand, DH & Steinberg, RA (1977) Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J. Bacteriol. 130 429-40 PubMed GONUTS page
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