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ECOLI:ENTE

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) entE
Protein Name(s) Enterobactin synthase component E

Enterochelin synthase E 2,3-dihydroxybenzoate-AMP ligase Dihydroxybenzoic acid-activating enzyme S-dihydroxybenzoyltransferase

External Links
UniProt P10378
EMBL X15058
U82598
U00096
AP009048
M24148
M36700
PIR H64792
RefSeq NP_415126.1
YP_488883.1
PDB 3RG2
4IZ6
PDBsum 3RG2
4IZ6
ProteinModelPortal P10378
SMR P10378
DIP DIP-9515N
IntAct P10378
MINT MINT-1228110
STRING 511145.b0594
BindingDB P10378
ChEMBL CHEMBL4856
PaxDb P10378
PRIDE P10378
EnsemblBacteria AAC73695
BAE76349
GeneID 12930911
947426
KEGG ecj:Y75_p0583
eco:b0594
PATRIC 32116364
EchoBASE EB0259
EcoGene EG10263
eggNOG COG1021
HOGENOM HOG000230011
InParanoid P10378
KO K02363
OMA GEKSCAW
OrthoDB EOG600DJW
PhylomeDB P10378
BioCyc EcoCyc:ENTE-MONOMER
ECOL316407:JW0586-MONOMER
MetaCyc:ENTE-MONOMER
UniPathway UPA00017
PRO PR:P10378
Proteomes UP000000318
UP000000625
Genevestigator P10378
GO GO:0008668
GO:0005524
GO:0016874
GO:0016746
GO:0009239
InterPro IPR025110
IPR020845
IPR000873
IPR011963
Pfam PF00501
PF13193
TIGRFAMs TIGR02275
PROSITE PS00455

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

Contributes to

GO:0016874

ligase activity

PMID:20359185[1]

ECO:0000314

F

Figure 1: Show that entE in E. coli has some kind of kinetic mechanism

complete

Contributes to

GO:0016874

ligase activity

PMID:20359185[1]

ECO:0000314

F

Figure 3: Shows that DHB binds to entE before it binds to ATP

complete

Contributes to

GO:0016874

ligase activity

PMID:20359185[1]

ECO:0000314

F

Figure 5: Shows that entE is associated with some type of inhibition

complete

enables

GO:0047527

2,3-dihydroxybenzoate-serine ligase activity

PMID:9485415[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009239

enterobactin biosynthetic process

PMID:4939766[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008668

(2,3-dihydroxybenzoyl)adenylate synthase activity

PMID:2531000[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000873

F

Seeded From UniProt

complete

enables

GO:0008668

(2,3-dihydroxybenzoyl)adenylate synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011963

F

Seeded From UniProt

complete

involved_in

GO:0019290

siderophore biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011963

P

Seeded From UniProt

complete

enables

GO:0047527

2,3-dihydroxybenzoate-serine ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.3.2.14

F

Seeded From UniProt

complete

enables

GO:0008668

(2,3-dihydroxybenzoyl)adenylate synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.58

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472
UniProtKB-SubCell:SL-0162

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0009239

enterobactin biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0259
UniPathway:UPA00017

P

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

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

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Sikora, AL et al. (2010) Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli. Biochemistry 49 3648-57 PubMed GONUTS page
  2. Gehring, AM et al. (1998) Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 37 2648-59 PubMed GONUTS page
  3. Luke, RK & Gibson, F (1971) Location of three genes concerned with the conversion of 2,3-dihydroxybenzoate into enterochelin in Escherichia coli K-12. J. Bacteriol. 107 557-62 PubMed GONUTS page
  4. Rusnak, F et al. (1989) Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. Biochemistry 28 6827-35 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page