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ECOLI:AROB

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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

PMID:6386050[1]

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
CACAO 4424

enables

GO:0003856

3-dehydroquinate synthase activity

PMID:6386050[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009073

aromatic amino acid family biosynthetic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000472619
UniProtKB:P9WPX9

P

Seeded From UniProt

complete

enables

GO:0003856

3-dehydroquinate synthase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10074
PANTHER:PTN000472585
UniProtKB:P9WPX9

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:6386050[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003856

3-dehydroquinate synthase activity

PMID:6386050[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:2514789[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:2514789[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003856

3-dehydroquinate synthase activity

PMID:353051[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003856

3-dehydroquinate synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016037

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016037

C

Seeded From UniProt

complete

involved_in

GO:0009073

aromatic amino acid family biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016037
InterPro:IPR030963

P

Seeded From UniProt

complete

enables

GO:0016838

carbon-oxygen lyase activity, acting on phosphates

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030963

F

Seeded From UniProt

complete

enables

GO:0003856

3-dehydroquinate synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.3.4

F

Seeded From UniProt

complete

involved_in

GO:0009073

aromatic amino acid family biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001254

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

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

GO_REF:0000104

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

PMID:6386050[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0009073

aromatic amino acid family biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0057

P

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0009423

chorismate biosynthetic process

GO_REF:0000041

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. 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. 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. 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
  4. 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