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Protein

Enterobactin synthase component B

Gene

entB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron2+ atoms. EntB is a bifunctional protein that serves as an isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-dihydroxybenzoate (DHB). In the enterobactin assembly, EntB functions as an aryl carrier protein phosphopantetheinylated near the C terminus by EntD to yield holo-EntB, which is then acylated by EntE with 2,3-dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine.8 Publications

Catalytic activityi

6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.4 Publications
Isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate.4 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by 3-[(carboxyethenyl)oxy]-6-hydroxy-1-benzoic acid and 3-[(carboxyethenyl)oxy]benzoic acid.1 Publication

Kineticsi

Kcat is 600 min(-1) for isochorismatase activity with isochorismate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 540 min(-1) for isochorismatase activity with 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as substrate (at pH 7 and 37 degrees Celsius). Kcat is 310 min(-1) for isochorismatase activity with 4,5-dihydroisochorismate as substrate (at pH 7 and 37 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=14.7 µM for isochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  2. KM=23 µM for 4,5-dihydroisochorismate (at pH 7 and 37 degrees Celsius)1 Publication
  3. KM=86 µM for 3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  4. KM=120 µM for 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate (at pH 7 and 37 degrees Celsius)1 Publication
  5. KM=280 µM for cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic acid (at pH 7 and 37 degrees Celsius)1 Publication
  1. Vmax=18.5 µmol/min/mg enzyme (at pH 7 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 6.5 and 7.5. At pH 5.5, EntB retains 50% of isochorismatase activity.1 Publication

Pathwayi: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi227Magnesium1 Publication1
Metal bindingi242Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi244Magnesium1 Publication1

GO - Molecular functioni

  • 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
  • isochorismatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphopantetheine binding Source: UniProtKB
  • transferase activity, transferring alkyl or aryl (other than methyl) groups Source: EcoliWiki

GO - Biological processi

  • enterobactin biosynthetic process Source: UniProtKB
  • phenazine biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase

Keywords - Biological processi

Enterobactin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENTB-MONOMER.
ECOL316407:JW0587-MONOMER.
MetaCyc:ENTB-MONOMER.
BRENDAi3.3.2.1. 2026.
6.3.2.14. 2026.
SABIO-RKP0ADI4.
UniPathwayiUPA00017.

Names & Taxonomyi

Protein namesi
Recommended name:
Enterobactin synthase component B1 Publication (EC:6.3.2.144 Publications)
Alternative name(s):
Enterobactin biosynthesis bifunctional protein EntB1 Publication
Enterochelin synthase B1 Publication
Including the following 2 domains:
Isochorismatase1 Publication (EC:3.3.2.14 Publications)
Alternative name(s):
2,3-dihydro-2,3-dihydroxybenzoate synthase1 Publication
Isochorismate lyase1 Publication
Aryl carrier protein1 Publication
Short name:
ArCP1 Publication
Gene namesi
Name:entB1 Publication
Synonyms:entG1 Publication
Ordered Locus Names:b0595, JW0587
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10260. entB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are hypersensitive to the antimicrobial peptide wrwycr.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi240D → R: The catalytic efficiency slightly increases, but a 8-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication1
Mutagenesisi242G → A: Not efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi244D → A: Efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi244D → R: Not efficiently phosphopantetheinylated by EntD. 1 Publication1
Mutagenesisi249M → A: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication1
Mutagenesisi263D → R: The catalytic efficiency is the same as the wild-type, but a 3-fold decrease of the affinity for the S-dihydroxybenzoyltransferase EntE is observed. 1 Publication1
Mutagenesisi264F → E: The affinity for EntE and catalytic efficiency of the S-dihydroxybenzoyltransferase EntE are below that of the wild-type. 2 Publications1
Mutagenesisi268A → Q: Unable to recognize EntE and EntF. Exhibits a decrease in the enterobactin production compared to the wild-type. Still able to be phosphopantetheinylated. 1 Publication1
Mutagenesisi269K → A: Behaves similarly to the wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002018222 – 285Enterobactin synthase component BAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei245O-(pantetheine 4'-phosphoryl)serine1 Publication1

Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-dihydroxybenzoate in a reaction catalyzed by EntE.1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

EPDiP0ADI4.
PaxDbiP0ADI4.
PRIDEiP0ADI4.

2D gel databases

SWISS-2DPAGEP0ADI4.

Expressioni

Inductioni

Under conditions of iron deficiency and by the fur protein.1 Publication

Interactioni

Subunit structurei

Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Dimer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-547993,EBI-547993
entHP0A8Y83EBI-547993,EBI-1118982

Protein-protein interaction databases

BioGridi4260905. 198 interactors.
DIPiDIP-9512N.
IntActiP0ADI4. 29 interactors.
MINTiMINT-1241343.
STRINGi511145.b0595.

Structurei

Secondary structure

1285
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 16Combined sources3
Helixi28 – 30Combined sources3
Beta strandi31 – 36Combined sources6
Helixi40 – 43Combined sources4
Helixi51 – 69Combined sources19
Beta strandi74 – 78Combined sources5
Helixi85 – 88Combined sources4
Helixi91 – 95Combined sources5
Helixi98 – 101Combined sources4
Helixi103 – 105Combined sources3
Helixi110 – 112Combined sources3
Beta strandi118 – 122Combined sources5
Beta strandi125 – 127Combined sources3
Turni128 – 131Combined sources4
Helixi134 – 140Combined sources7
Beta strandi145 – 151Combined sources7
Turni153 – 155Combined sources3
Helixi156 – 166Combined sources11
Beta strandi170 – 179Combined sources10
Helixi183 – 196Combined sources14
Beta strandi199 – 201Combined sources3
Helixi203 – 206Combined sources4
Beta strandi207 – 209Combined sources3
Helixi215 – 222Combined sources8
Helixi223 – 225Combined sources3
Helixi239 – 241Combined sources3
Helixi247 – 255Combined sources9
Turni256 – 258Combined sources3
Helixi264 – 268Combined sources5
Helixi273 – 281Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FQ1X-ray2.30A/B1-285[»]
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J209-285[»]
ProteinModelPortaliP0ADI4.
SMRiP0ADI4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADI4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini214 – 281Acyl carrierPROSITE-ProRule annotationAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 213Isochorismatase1 PublicationAdd BLAST212

Sequence similaritiesi

In the N-terminal section; belongs to the isochorismatase family.Curated
Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105WQI. Bacteria.
COG1535. LUCA.
COG3433. LUCA.
HOGENOMiHOG000078667.
InParanoidiP0ADI4.
KOiK01252.
OMAiRDIKPFF.
PhylomeDBiP0ADI4.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.850. 1 hit.
InterProiIPR016291. Isochorismatase.
IPR000868. Isochorismatase-like.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001111. Isochorismatase. 1 hit.
PRINTSiPR01398. ISCHRISMTASE.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52499. SSF52499. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC
60 70 80 90 100
PMMEQVIANI AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT
110 120 130 140 150
RSPEQQKVVD RLTPDADDTV LVKWRYSAFH RSPLEQMLKE SGRNQLIITG
160 170 180 190 200
VYAHIGCMTT ATDAFMRDIK PFMVADALAD FSRDEHLMSL KYVAGRSGRV
210 220 230 240 250
VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID YGLDSVRMMA
260 270 280
LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
Length:285
Mass (Da):32,554
Last modified:December 6, 2005 - v1
Checksum:iE98C62D5ED23BAB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24148 Unassigned DNA. Translation: AAA16102.1.
M24143 Genomic DNA. Translation: AAA76835.1.
U82598 Genomic DNA. Translation: AAB40795.1.
U00096 Genomic DNA. Translation: AAC73696.1.
AP009048 Genomic DNA. Translation: BAE76350.1.
PIRiC91904. YXECIC.
RefSeqiNP_415127.1. NC_000913.3.
WP_001007138.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73696; AAC73696; b0595.
BAE76350; BAE76350; BAE76350.
GeneIDi946178.
KEGGiecj:JW0587.
eco:b0595.
PATRICi32116366. VBIEscCol129921_0623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24148 Unassigned DNA. Translation: AAA16102.1.
M24143 Genomic DNA. Translation: AAA76835.1.
U82598 Genomic DNA. Translation: AAB40795.1.
U00096 Genomic DNA. Translation: AAC73696.1.
AP009048 Genomic DNA. Translation: BAE76350.1.
PIRiC91904. YXECIC.
RefSeqiNP_415127.1. NC_000913.3.
WP_001007138.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FQ1X-ray2.30A/B1-285[»]
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J209-285[»]
ProteinModelPortaliP0ADI4.
SMRiP0ADI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260905. 198 interactors.
DIPiDIP-9512N.
IntActiP0ADI4. 29 interactors.
MINTiMINT-1241343.
STRINGi511145.b0595.

2D gel databases

SWISS-2DPAGEP0ADI4.

Proteomic databases

EPDiP0ADI4.
PaxDbiP0ADI4.
PRIDEiP0ADI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73696; AAC73696; b0595.
BAE76350; BAE76350; BAE76350.
GeneIDi946178.
KEGGiecj:JW0587.
eco:b0595.
PATRICi32116366. VBIEscCol129921_0623.

Organism-specific databases

EchoBASEiEB0256.
EcoGeneiEG10260. entB.

Phylogenomic databases

eggNOGiENOG4105WQI. Bacteria.
COG1535. LUCA.
COG3433. LUCA.
HOGENOMiHOG000078667.
InParanoidiP0ADI4.
KOiK01252.
OMAiRDIKPFF.
PhylomeDBiP0ADI4.

Enzyme and pathway databases

UniPathwayiUPA00017.
BioCyciEcoCyc:ENTB-MONOMER.
ECOL316407:JW0587-MONOMER.
MetaCyc:ENTB-MONOMER.
BRENDAi3.3.2.1. 2026.
6.3.2.14. 2026.
SABIO-RKP0ADI4.

Miscellaneous databases

EvolutionaryTraceiP0ADI4.
PROiP0ADI4.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.850. 1 hit.
InterProiIPR016291. Isochorismatase.
IPR000868. Isochorismatase-like.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001111. Isochorismatase. 1 hit.
PRINTSiPR01398. ISCHRISMTASE.
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52499. SSF52499. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENTB_ECOLI
AccessioniPrimary (citable) accession number: P0ADI4
Secondary accession number(s): P15048, Q2MBK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.