ENTE_ECOLI
ID ENTE_ECOLI Reviewed; 536 AA.
AC P10378; P15049; P77773; Q2MBK7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Enterobactin synthase component E {ECO:0000303|PubMed:9485415};
DE EC=6.3.2.14 {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294};
DE AltName: Full=2,3-dihydroxybenzoate-AMP ligase {ECO:0000303|PubMed:2531000};
DE Short=DHB-AMP ligase {ECO:0000303|PubMed:2531000};
DE AltName: Full=2,3-dihydroxybenzoate-AMP synthase {ECO:0000305};
DE EC=6.2.1.71 {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000};
DE AltName: Full=Dihydroxybenzoic acid-activating enzyme {ECO:0000303|PubMed:2531000};
DE AltName: Full=Enterochelin synthase E {ECO:0000303|PubMed:9485415};
GN Name=entE {ECO:0000303|PubMed:2525505}; OrderedLocusNames=b0594, JW0586;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2525505; DOI=10.1016/0378-1097(89)90450-3;
RA Staab J.F., Elkins M.F., Earhart C.F.;
RT "Nucleotide sequence of the Escherichia coli entE gene.";
RL FEMS Microbiol. Lett. 50:15-19(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=K12;
RX PubMed=2110093; DOI=10.1111/j.1574-6968.1990.tb04118.x;
RA Elkins M.F., Earhart C.F.;
RT "Opacity factor from group A streptococci is an apoproteinase.";
RL FEMS Microbiol. Lett. 56:35-39(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-536.
RX PubMed=2521622; DOI=10.1128/jb.171.2.791-798.1989;
RA Liu J., Duncan K., Walsh C.T.;
RT "Nucleotide sequence of a cluster of Escherichia coli enterobactin
RT biosynthesis genes: identification of entA and purification of its product
RT 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
RL J. Bacteriol. 171:791-798(1989).
RN [7]
RP INDUCTION.
RX PubMed=6227609; DOI=10.1128/jb.156.3.1171-1177.1983;
RA Fleming T.P., Nahlik M.S., McIntosh M.A.;
RT "Regulation of enterobactin iron transport in Escherichia coli:
RT characterization of ent::Mu d(Apr lac) operon fusions.";
RL J. Bacteriol. 156:1171-1177(1983).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=2531000; DOI=10.1021/bi00443a008;
RA Rusnak F., Faraci W.S., Walsh C.T.;
RT "Subcloning, expression, and purification of the enterobactin biosynthetic
RT enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound
RT (2,3-dihydroxybenzoyl)adenylate product.";
RL Biochemistry 28:6827-6835(1989).
RN [9]
RP INDUCTION.
RX PubMed=2521621; DOI=10.1128/jb.171.2.784-790.1989;
RA Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Nucleotide sequence and transcriptional organization of the Escherichia
RT coli enterobactin biosynthesis cistrons entB and entA.";
RL J. Bacteriol. 171:784-790(1989).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=9214294; DOI=10.1021/bi970453p;
RA Gehring A.M., Bradley K.A., Walsh C.T.;
RT "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB)
RT is a bifunctional enzyme that is phosphopantetheinylated by EntD and then
RT acylated by EntE using ATP and 2,3-dihydroxybenzoate.";
RL Biochemistry 36:8495-8503(1997).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9485415; DOI=10.1021/bi9726584;
RA Gehring A.M., Mori I., Walsh C.T.;
RT "Reconstitution and characterization of the Escherichia coli enterobactin
RT synthetase from EntB, EntE, and EntF.";
RL Biochemistry 37:2648-2659(1998).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10692387; DOI=10.1128/jb.182.6.1768-1773.2000;
RA Hantash F.M., Earhart C.F.;
RT "Membrane association of the Escherichia coli enterobactin synthase
RT proteins EntB/G, EntE, and EntF.";
RL J. Bacteriol. 182:1768-1773(2000).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=10688898; DOI=10.1073/pnas.040572897;
RA Ehmann D.E., Shaw-Reid C.A., Losey H.C., Walsh C.T.;
RT "The EntF and EntE adenylation domains of Escherichia coli enterobactin
RT synthetase: sequestration and selectivity in acyl-AMP transfers to
RT thiolation domain cosubstrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2509-2514(2000).
RN [14]
RP FUNCTION, MUTAGENESIS OF ARG-437; LYS-473 AND ARG-494, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND REACTION MECHANISM.
RX PubMed=16632253; DOI=10.1016/j.chembiol.2006.02.005;
RA Drake E.J., Nicolai D.A., Gulick A.M.;
RT "Structure of the EntB multidomain nonribosomal peptide synthetase and
RT functional analysis of its interaction with the EntE adenylation domain.";
RL Chem. Biol. 13:409-419(2006).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16567620; DOI=10.1073/pnas.0601038103;
RA Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.;
RT "A protein interaction surface in nonribosomal peptide synthesis mapped by
RT combinatorial mutagenesis and selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5314-5319(2006).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MISCELLANEOUS.
RX PubMed=19852513; DOI=10.1021/bi901680m;
RA Sikora A.L., Cahill S.M., Blanchard J.S.;
RT "Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-
RT tetraphosphate.";
RL Biochemistry 48:10827-10829(2009).
RN [17]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=19699210; DOI=10.1016/j.jmb.2009.08.036;
RA Khalil S., Pawelek P.D.;
RT "Ligand-induced conformational rearrangements promote interaction between
RT the Escherichia coli enterobactin biosynthetic proteins EntE and EntB.";
RL J. Mol. Biol. 393:658-671(2009).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND REACTION MECHANISM.
RX PubMed=20359185; DOI=10.1021/bi100350c;
RA Sikora A.L., Wilson D.J., Aldrich C.C., Blanchard J.S.;
RT "Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from
RT Escherichia coli.";
RL Biochemistry 49:3648-3657(2010).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20845982; DOI=10.1021/bi1012854;
RA Felnagle E.A., Barkei J.J., Park H., Podevels A.M., McMahon M.D.,
RA Drott D.W., Thomas M.G.;
RT "MbtH-like proteins as integral components of bacterial nonribosomal
RT peptide synthetases.";
RL Biochemistry 49:8815-8817(2010).
RN [20]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=21166461; DOI=10.1021/bi101558v;
RA Khalil S., Pawelek P.D.;
RT "Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-
RT protein interaction between Escherichia coli 2,3-dihydro-2,3-
RT dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase
RT (EntE).";
RL Biochemistry 50:533-545(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP PHOSPHOPANTETHEINE, AND SUBUNIT.
RX PubMed=22365602; DOI=10.1016/j.chembiol.2011.11.013;
RA Sundlov J.A., Shi C., Wilson D.J., Aldrich C.C., Gulick A.M.;
RT "Structural and functional investigation of the intermolecular interaction
RT between NRPS adenylation and carrier protein domains.";
RL Chem. Biol. 19:188-198(2012).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF CHIMERIC ENTE-ENTB CONSTRUCT IN
RP COMPLEX WITH SUBSTRATE ANALOG AND PHOSPHOPANTETHEINE, AND SUBUNIT.
RX PubMed=23897471; DOI=10.1107/s0907444913009372;
RA Sundlov J.A., Gulick A.M.;
RT "Structure determination of the functional domain interaction of a chimeric
RT nonribosomal peptide synthetase from a challenging crystal with
RT noncrystallographic translational symmetry.";
RL Acta Crystallogr. D 69:1482-1492(2013).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-
CC dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding
CC for the three catechol functionalities that provide hexadentate
CC coordination for the tightly ligated iron(2+) atoms. EntE proccesses
CC via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong
CC mechanism). First, it catalyzes the activation of the carboxylate group
CC of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent
CC pyrophosphate exchange reactions to yield the acyladenylate
CC intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to
CC salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-
CC trihydroxybenzoate. In the second step, DHB is transferred from 2,3-
CC dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB)
CC to form DHB-holo-EntB. Then this product will serve in the formation of
CC the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can
CC also transfer adenylated salicylate to holo-EntB.
CC {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:19699210,
CC ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:21166461,
CC ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6
CC diphosphate + enterobactin + 4 H(+); Xref=Rhea:RHEA:30571,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805,
CC ChEBI:CHEBI:456215; EC=6.3.2.14;
CC Evidence={ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000,
CC ECO:0000269|PubMed:9214294};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] =
CC 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate;
CC Xref=Rhea:RHEA:61652, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36654,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC EC=6.2.1.71; Evidence={ECO:0000269|PubMed:10688898,
CC ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513,
CC ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982,
CC ECO:0000269|PubMed:2531000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoyl-5'-AMP + holo-[aryl-carrier protein] =
CC 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + H(+);
CC Xref=Rhea:RHEA:48604, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57417, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:9214294,
CC ECO:0000269|PubMed:9485415};
CC -!- ACTIVITY REGULATION: Inhibited by the adenylate analogs, 5'-O-[N-
CC (salicyl)sulfamoyl]adenosine (Sal-AMS) and 5'-O-[N-(2,3-
CC dihydroxybenzoyl)sulfamoyl]adenosine (DHB-AMS). Adenylation of 2,3-
CC dihydroxybenzoate (DHB) is enhanced by a protein-protein interaction
CC between the EntA and EntE. {ECO:0000269|PubMed:20359185,
CC ECO:0000269|PubMed:21166461}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for holo-EntB (at pH 8.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9214294};
CC KM=0.5 uM for holo-EntB {ECO:0000269|PubMed:16567620};
CC KM=2.5 uM for DHB (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=2.7 uM for DHB {ECO:0000269|PubMed:2531000};
CC KM=2.9 uM for DHB {ECO:0000269|PubMed:20845982};
CC KM=2.9 uM for holo-EntB (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=23.3 uM for holo-EntB (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16632253};
CC KM=70 uM for 3-hydroxybenzoate (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=70 uM for salicylate (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=400 uM for 5,5-diadenosine tetraphosphate
CC {ECO:0000269|PubMed:19852513};
CC KM=430 uM for ATP (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=1200 uM for ATP {ECO:0000269|PubMed:2531000};
CC KM=3100 uM for 4-aminosalicylate (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC KM=34.2 mM for D-pantetheine (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20359185};
CC Vmax=3168.2 pmol/min/mg enzyme {ECO:0000269|PubMed:20845982};
CC Note=kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase
CC activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25
CC degrees Celsius). kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP
CC ligase activity with salicylate as substrate (at pH 7.8 and 25
CC degrees Celsius). kcat is 0.9 sec(-1) for S-
CC dihydroxybenzoyltransferase activity with D-pantetheine as substrate
CC (at pH 7.8 and 25 degrees Celsius). kcat is 2.8 sec(-1) for 2,3-
CC dihydroxybenzoate-AMP ligase activity with ATP and DHB as substrates
CC (at pH 7.8 and 25 degrees Celsius). kcat is 2.8 sec(-1) for S-
CC dihydroxybenzoyltransferase activity with holo-EntB as substrate (at
CC pH 7.8 and 25 degrees Celsius). kcat is 4.4 sec(-1) for 2,3-
CC dihydroxybenzoate-AMP ligase activity with 4-aminosalicylate as
CC substrate (at pH 7.8 and 25 degrees Celsius). kcat is 5.94 sec(-1)
CC for S-dihydroxybenzoyltransferase activity with holo-EntB as
CC substrate (at pH 7.8 and 25 degrees Celsius). kcat is 100 min(-1) for
CC S-dihydroxybenzoyltransferase activity with holo-EntB as substrate
CC (at pH 8.8 and 37 degrees Celsius). kcat is 140 min(-1) for S-
CC dihydroxybenzoyltransferase activity with holo-EntB as substrate.
CC {ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:16632253,
CC ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:9214294};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000305|PubMed:9485415}.
CC -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme complex
CC called enterobactin synthase. Monomer. EntA and EntE interact together.
CC {ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:22365602,
CC ECO:0000269|PubMed:23897471, ECO:0000269|PubMed:2531000,
CC ECO:0000269|PubMed:9485415}.
CC -!- INTERACTION:
CC P10378; P15047: entA; NbExp=5; IntAct=EBI-550322, EBI-1118936;
CC P10378; P0ADI4: entB; NbExp=3; IntAct=EBI-550322, EBI-547993;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10692387}.
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC {ECO:0000269|PubMed:2521621, ECO:0000269|PubMed:6227609}.
CC -!- MISCELLANEOUS: In the absence of holo-EntB, EntE can transfer the
CC adenylate moiety of the 2,3-dihydroxybenzoyl-AMP intermediate to ATP,
CC generating the stress signaling molecule Ap4A involved in the
CC regulation of cell division during oxidative stress, and releasing 2,3-
CC dihydroxybenzoate. It seems that the expression of EntE during iron
CC starvation produces Ap(4)A to slow growth until intracellular iron
CC stores can be restored. {ECO:0000269|PubMed:19852513}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC EntE subfamily. {ECO:0000305}.
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DR EMBL; X15058; CAA33158.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40794.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73695.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76349.1; -; Genomic_DNA.
DR EMBL; M24148; AAA16101.1; -; Unassigned_DNA.
DR EMBL; M36700; AAA18492.1; -; Genomic_DNA.
DR PIR; H64792; SYECEB.
DR RefSeq; NP_415126.1; NC_000913.3.
DR RefSeq; WP_000026812.1; NZ_SSZK01000032.1.
DR PDB; 3RG2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-536.
DR PDB; 4IZ6; X-ray; 2.40 A; A/B=1-536.
DR PDB; 6IYK; X-ray; 2.45 A; A/B=1-536.
DR PDB; 6IYL; X-ray; 2.56 A; A/B=1-536.
DR PDBsum; 3RG2; -.
DR PDBsum; 4IZ6; -.
DR PDBsum; 6IYK; -.
DR PDBsum; 6IYL; -.
DR AlphaFoldDB; P10378; -.
DR SMR; P10378; -.
DR BioGRID; 4259905; 320.
DR BioGRID; 851747; 5.
DR ComplexPortal; CPX-5747; entAE 2,3-dihydroxybenzoate-AMP ligase complex.
DR ComplexPortal; CPX-5748; entBE aryl carrier complex.
DR DIP; DIP-9515N; -.
DR IntAct; P10378; 14.
DR STRING; 511145.b0594; -.
DR BindingDB; P10378; -.
DR ChEMBL; CHEMBL4856; -.
DR jPOST; P10378; -.
DR PaxDb; P10378; -.
DR PRIDE; P10378; -.
DR EnsemblBacteria; AAC73695; AAC73695; b0594.
DR EnsemblBacteria; BAE76349; BAE76349; BAE76349.
DR GeneID; 947426; -.
DR KEGG; ecj:JW0586; -.
DR KEGG; eco:b0594; -.
DR PATRIC; fig|1411691.4.peg.1675; -.
DR EchoBASE; EB0259; -.
DR eggNOG; COG1021; Bacteria.
DR HOGENOM; CLU_000022_59_7_6; -.
DR InParanoid; P10378; -.
DR OMA; PNIRFIR; -.
DR PhylomeDB; P10378; -.
DR BioCyc; EcoCyc:ENTE-MON; -.
DR BioCyc; MetaCyc:ENTE-MON; -.
DR BRENDA; 2.7.7.58; 2026.
DR BRENDA; 6.2.1.71; 2026.
DR BRENDA; 6.3.2.14; 2026.
DR UniPathway; UPA00017; -.
DR PRO; PR:P10378; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; IDA:EcoCyc.
DR GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011963; DHB_AMP_lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02275; DHB_AMP_lig; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; ATP-binding; Enterobactin biosynthesis;
KW Ligase; Membrane; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..536
FT /note="Enterobactin synthase component E"
FT /id="PRO_0000193075"
FT REGION 438..439
FT /note="Phosphopantetheine binding"
FT /evidence="ECO:0000269|PubMed:22365602,
FT ECO:0000269|PubMed:23897471"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22365602"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897471"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22365602,
FT ECO:0000269|PubMed:23897471"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22365602,
FT ECO:0000269|PubMed:23897471"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22365602"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22365602,
FT ECO:0000269|PubMed:23897471"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897471"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897471"
FT MUTAGEN 437
FT /note="R->D: Catalyzes the adenylation reaction with 10%
FT reduction of activity compared to the wild-type. 3%
FT reduction of activity compared to the wild-type; when
FT associated with D-473."
FT /evidence="ECO:0000269|PubMed:16632253"
FT MUTAGEN 473
FT /note="K->D: Catalyzes the adenylation reaction with same
FT activity as the wild-type. 3% reduction of activity
FT compared to the wild-type; when associated with D-437."
FT /evidence="ECO:0000269|PubMed:16632253"
FT MUTAGEN 494
FT /note="R->D: Catalyzes the adenylation reaction with same
FT activity as the wild-type."
FT /evidence="ECO:0000269|PubMed:16632253"
FT CONFLICT 369..378
FT /note="DAEGNPLPQG -> ECRRKSTAAR (in Ref. 1; CAA33158)"
FT /evidence="ECO:0000305"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:4IZ6"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6IYK"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:3RG2"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 457..467
FT /evidence="ECO:0007829|PDB:4IZ6"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 471..482
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:4IZ6"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:3RG2"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:4IZ6"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:4IZ6"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:4IZ6"
SQ SEQUENCE 536 AA; 59112 MW; F818942DFDD8DC99 CRC64;
MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS YRELNQAADN
LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP VLALFSHQRS ELNAYASQIE
PALLIADRQH ALFSGDDFLN TFVTEHSSIR VVQLLNDSGE HNLQDAINHP AEDFTATPSP
ADEVAYFQLS GGTTGTPKLI PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS
PGSLGVFLAG GTVVLAADPS ATLCFPLIEK HQVNVTALVP PAVSLWLQAL IEGESRAQLA
SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK IIHTQGYPMC
PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH NASAFDANGF YCSGDLISID
PEGYITVQGR EKDQINRGGE KIAAEEIENL LLRHPAVIYA ALVSMEDELM GEKSCAYLVV
KEPLRAVQVR RFLREQGIAE FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
