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ECOLI:AROB
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | aroB | |
Protein Name(s) | 3-dehydroquinate synthase | |
External Links | ||
UniProt | P07639 | |
EMBL | X03867 Z19601 U18997 U00096 AP009048 X15162 | |
PIR | A24863 | |
RefSeq | NP_417848.1 YP_492043.1 | |
ProteinModelPortal | P07639 | |
SMR | P07639 | |
DIP | DIP-9150N | |
IntAct | P07639 | |
MINT | MINT-1261041 | |
STRING | 511145.b3389 | |
BindingDB | P07639 | |
ChEMBL | CHEMBL3554 | |
PaxDb | P07639 | |
PRIDE | P07639 | |
EnsemblBacteria | AAC76414 BAE77902 | |
GeneID | 12930302 947927 | |
KEGG | ecj:Y75_p3787 eco:b3389 | |
PATRIC | 32122210 | |
EchoBASE | EB0072 | |
EcoGene | EG10074 | |
eggNOG | COG0337 | |
HOGENOM | HOG000007970 | |
InParanoid | P07639 | |
KO | K01735 | |
OMA | IERSCAA | |
OrthoDB | EOG6SJJGD | |
PhylomeDB | P07639 | |
BioCyc | EcoCyc:AROB-MONOMER ECOL316407:JW3352-MONOMER MetaCyc:AROB-MONOMER | |
BRENDA | 4.2.3.4 | |
UniPathway | UPA00053 | |
PRO | PR:P07639 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P07639 | |
GO | GO:0005737 GO:0003856 GO:0070403 GO:0008270 GO:0009073 GO:0009423 | |
HAMAP | MF_00110 | |
InterPro | IPR016037 | |
PIRSF | PIRSF001455 | |
TIGRFAMs | TIGR01357 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000315 |
F |
By comparing table II and III, E. coli transformants show more dehydroquinate synthase activity than wild-type E. coli. Based on table IV, aroB gene was inserted behind the tac promoter and increase dehydroquinate synthase activity even more. |
complete | |||||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009073 |
aromatic amino acid family biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000472619 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10074 |
F |
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:0003856 |
3-dehydroquinate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0070403 |
NAD+ binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
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:0016838 |
carbon-oxygen lyase activity, acting on phosphates |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
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 |
UniRule:UR000001254 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001254 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0003856 |
3-dehydroquinate synthase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001254 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0009073 |
aromatic amino acid family biosynthetic process |
ECO:0000304 |
author statement supported by traceable reference used in manual 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 | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
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 | |||
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 1.3 1.4 Frost, JW et al. (1984) Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme. Biochemistry 23 4470-5 PubMed GONUTS page
- ↑ 2.0 2.1 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 Bender, SL et al. (1989) Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28 7555-60 PubMed GONUTS page
- ↑ Maitra, US & Sprinson, DB (1978) 5-Dehydro-3-deoxy-D-arabino-heptulosonic acid 7-phosphate. An intermediate in the 3-dehydroquinate synthase reaction. J. Biol. Chem. 253 5426-30 PubMed GONUTS page