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ECOLI:TYRB
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | tyrB | |
| Protein Name(s) | Aromatic-amino-acid aminotransferase
ARAT AROAT Beta-methylphenylalanine transaminase | |
| External Links | ||
| UniProt | P04693 | |
| EMBL | X03628 M12047 U00006 U00096 AP009048 M17809 | |
| PIR | A30379 | |
| RefSeq | NP_418478.1 YP_492197.1 | |
| PDB | 3FSL 3TAT | |
| PDBsum | 3FSL 3TAT | |
| ProteinModelPortal | P04693 | |
| SMR | P04693 | |
| IntAct | P04693 | |
| STRING | 511145.b4054 | |
| PaxDb | P04693 | |
| PRIDE | P04693 | |
| EnsemblBacteria | AAC77024 BAE78056 | |
| GeneID | 12933673 948563 | |
| KEGG | ecj:Y75_p3941 eco:b4054 | |
| PATRIC | 32123649 | |
| EchoBASE | EB1033 | |
| EcoGene | EG11040 | |
| eggNOG | COG1448 | |
| HOGENOM | HOG000185899 | |
| InParanoid | P04693 | |
| KO | K00832 | |
| OMA | GFSAGME | |
| OrthoDB | EOG6C2WBK | |
| PhylomeDB | P04693 | |
| BioCyc | EcoCyc:TYRB-MONOMER ECOL316407:JW4014-MONOMER MetaCyc:TYRB-MONOMER | |
| UniPathway | UPA00121 UPA00122 | |
| EvolutionaryTrace | P04693 | |
| PRO | PR:P04693 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P04693 | |
| GO | GO:0005737 GO:0008793 GO:0050048 GO:0080130 GO:0004838 GO:0030170 GO:0006532 GO:0033585 GO:0009098 GO:0019292 | |
| 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:0070547 |
L-tyrosine aminotransferase activity |
ECO:0000315 |
F |
"The refined crystallographic structure of the "closed" conformation of chicken mitochondrial aspartate aminotransferase has been used as a template for the construction of models of the two Escherichia coli aminotransferases encoded by the tyrB and aspC genes" |
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:0030170 |
pyridoxal phosphate binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006532 |
aspartate biosynthetic process |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
EcoliWiki:aspC |
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:0050048 |
L-leucine: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:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019292 |
tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009098 |
leucine biosynthetic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008793 |
aromatic-amino-acid:2-oxoglutarate aminotransferase 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:0004838 |
L-tyrosine:2-oxoglutarate aminotransferase 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 | |||
|
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:0080130 |
L-phenylalanine:2-oxoglutarate aminotransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008793 |
aromatic-amino-acid:2-oxoglutarate aminotransferase activity |
ECO:0000501 |
evidence 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:0008483 |
transaminase 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 | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
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:0006571 |
tyrosine biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00122 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0009094 |
L-phenylalanine biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00121 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Seville, M et al. (1988) Modeling the three-dimensional structures of bacterial aminotransferases. Biochemistry 27 8344-9 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 3.0 3.1 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
- ↑ 4.0 4.1 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
- ↑ 5.0 5.1 Powell, JT & Morrison, JF (1978) Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis. J. Bacteriol. 136 1-4 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 6.3 Mavrides, C & Orr, W (1975) Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J. Biol. Chem. 250 4128-33 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
a
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- GO:0009098 ! L-leucine biosynthetic process
- GO:0080130 ! L-phenylalanine-2-oxoglutarate transaminase activity
- GO:0033585 ! L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
- GO:0009094 ! L-phenylalanine biosynthetic process
- GO:0004838 ! L-tyrosine-2-oxoglutarate transaminase activity
- GO:0019292 ! L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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