Isochorismatase (P0ADI4)

Identification
Name:Isochorismatase
Synonyms:
  • 2,3 dihydro-2,3 dihydroxybenzoate synthase
  • Enterobactin synthase component B
  • Enterochelin synthase B
  • Isochorismate lyase
Gene Name:entB
Enzyme Class:
Biological Properties
General Function:Involved in isochorismatase activity
Specific Function:Required for production of 2,3-DHB. Also serves as an aryl carrier protein and plays a role in enterobactin assembly
Cellular Location:Cytoplasmic
SMPDB Pathways:
  • 2,3-dihydroxybenzoate biosynthesis PW000751
  • Biosynthesis of siderophore group nonribosomal peptides PW000760
  • Enterobactin Biosynthesis PW002048
KEGG Pathways:
  • Biosynthesis of siderophore group nonribosomal peptides ec01053
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0Isochorismate ↔ 1.0(2S,3S)-2,3-Dihydro-2,3-dihydroxybenzoate + 1.0Pyruvic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0isochorismate+1.0Thumb → 1.0Thumb+1.02,3-dihydroxy-2,3-dihydrobenzoate
1.0Water + 1.0isochorismate + 1.0Isochorismate → 1.0Pyruvic acid + 1.02,3-dihydroxy-2,3-dihydrobenzoate
ReactionCard
6.0Thumb+3.0L-Serine+3.0Thumb+3.0Thumb → 6.0Thumb+1.0enterobactin+6.0Pyrophosphate+3.0Thumb
6.0Adenosine triphosphate + 3.0L-Serine + 3.02,3-Dihydroxybenzoic acid + 3.0L-Serine → 6.0Adenosine monophosphate + 1.0enterobactin + 6.0Pyrophosphate + 3.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Thumb
1.0Adenosine triphosphate + 1.02,3-Dihydroxybenzoic acid → 1.0Pyrophosphate + 1.0(2,3-Dihydroxybenzoyl)adenylic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Pyrophosphate
1.0Adenosine triphosphate + 1.02,3-Dihydroxybenzoic acid ↔ 1.0(2,3-Dihydroxybenzoyl)adenylic acid + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0Isochorismate ↔ 1.0(2S,3S)-2,3-Dihydro-2,3-dihydroxybenzoate + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04053(2,3-Dihydroxybenzoyl)adenylic acidMetaboCard
ECMDB20009(2S,3S)-2,3-Dihydro-2,3-dihydroxybenzoateMetaboCard
ECMDB040552,3-Dihydro-2,3-dihydroxybenzoic acidMetaboCard
ECMDB241842,3-Dihydroxybenzoic acidMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20162IsochorismateMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
acyl carrier activity
binding
catalytic activity
cofactor binding
ether hydrolase activity
hydrolase activity
hydrolase activity, acting on ether bonds
isochorismatase activity
leukotriene-A4 hydrolase activity
substrate-specific transporter activity
transporter activity
Process
metabolic process
Gene Properties
Blattner:b0595
Gene OrientationClockwise
Centisome Percentage:13.51
Left Sequence End626917
Right Sequence End627774
Gene Sequence:
>858 bp
TTGCTGAAGTATCGCCTGATATCTGCTTTTGTGTTAATACCCGTCGTCATCGCGGCGTTG
TTTCTGTTGCCGCCGGTGGGGTTCGCCATTGTAACGCTGGTGGTCTGCATGCTGGCAGCG
TGGGAATGGGGACAGCTTAGCGGTTTTACCACTCGTTCGCAGCGAGTATGGTTGGCGGTG
TTATGCGGGTTATTGTTGGCGCTGATGCTTTTTCTGTTGCCGGAATATCACCGAAATATT
CATCAACCGCTGGTTGAAATCTCACTTTGGGCTTCGCTGGGTTGGTGGATTGTCGCGCTA
TTGCTGGTGCTGTTTTACCCAGGTTCCGCAGCAATCTGGCGTAACTCTAAAACATTGCGC
CTTATTTTTGGCGTGCTAACCATTGTTCCCTTCTTCTGGGGCATGCTGGCGTTACGGGCC
TGGCACTATGACGAGAATCATTACAGTGGCGCAATATGGCTGCTCTATGTCATGATCCTG
GTATGGGGCGCTGACTCCGGCGCATATATGTTTGGCAAATTGTTTGGTAAACATAAGCTG
GCACCGAAGGTTTCTCCGGGTAAAACCTGGCAAGGCTTTATCGGTGGACTCGCTACTGCA
GCGGTAATCTCATGGGGTTATGGCATGTGGGCGAATCTCGACGTCGCTCCCGTCACCTTA
CTCATTTGCTCTATTGTCGCAGCGTTAGCCTCAGTGCTCGGCGATCTGACCGAGAGTATG
TTTAAGCGTGAAGCAGGAATTAAGGACAGCGGTCATTTAATTCCAGGACACGGTGGTATT
TTAGATCGTATTGATAGCCTGACGGCTGCGGTACCGGTCTTTGCTTGCTTGTTGTTACTG
GTATTCAGGACGCTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:285
Protein Molecular Weight:32554
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Isochorismatase
MAIPKLQAYALPESHDIPQNKVDWAFEPQRAALLIHDMQDYFVSFWGENCPMMEQVIANI
AALRDYCKQHNIPVYYTAQPKEQSDEDRALLNDMWGPGLTRSPEQQKVVDRLTPDADDTV
LVKWRYSAFHRSPLEQMLKESGRNQLIITGVYAHIGCMTTATDAFMRDIKPFMVADALAD
FSRDEHLMSLKYVAGRSGRVVMTEELLPAPIPASKAALREVILPLLDESDEPFDDDNLID
YGLDSVRMMALAARWRKVHGDIDFVMLAKNPTIDAWWKLLSREVK
References
External Links:
ResourceLink
Uniprot ID:P0ADI4
Uniprot Name:ENTB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674368
Ecogene ID:EG10260
Ecocyc:EG10260
ColiBase:b0595
Kegg Gene:b0595
EchoBASE ID:EB0256
CCDB:ENTB_ECOLI
BacMap:16128578
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Gehring, A. M., Bradley, K. A., Walsh, C. T. (1997). "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate." Biochemistry 36:8495-8503. Pubmed: 9214294
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Liu, J., Duncan, K., Walsh, C. T. (1989). "Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase." J Bacteriol 171:791-798. Pubmed: 2521622
  • Nahlik, M. S., Brickman, T. J., Ozenberger, B. A., McIntosh, M. A. (1989). "Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA." J Bacteriol 171:784-790. Pubmed: 2521621