ENTC_ECOLI
ID ENTC_ECOLI Reviewed; 391 AA.
AC P0AEJ2; P10377; P77099; Q2MBK8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Isochorismate synthase EntC {ECO:0000303|PubMed:2536681};
DE EC=5.4.4.2 {ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795};
DE AltName: Full=Isochorismate mutase {ECO:0000305};
GN Name=entC {ECO:0000303|PubMed:2536681}; OrderedLocusNames=b0593, JW0585;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2536681; DOI=10.1128/jb.171.2.775-783.1989;
RA Ozenberger B.A., Brickman T.J., McIntosh M.A.;
RT "Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC
RT and evolutionary relationship of isochorismate synthetase and other
RT chorismate-utilizing enzymes.";
RL J. Bacteriol. 171:775-783(1989).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=2139473; DOI=10.1016/0022-2836(90)90229-f;
RA Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Regulation of divergent transcription from the iron-responsive fepB-entC
RT promoter-operator regions in Escherichia coli.";
RL J. Mol. Biol. 212:669-682(1990).
RN [7]
RP PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=2139795; DOI=10.1021/bi00458a012;
RA Liu J., Quinn N., Berchtold G.A., Walsh C.T.;
RT "Overexpression, purification, and characterization of isochorismate
RT synthase (EntC), the first enzyme involved in the biosynthesis of
RT enterobactin from chorismate.";
RL Biochemistry 29:1417-1425(1990).
RN [8]
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 [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=8655506; DOI=10.1128/jb.178.11.3252-3259.1996;
RA Kwon O., Hudspeth M.E., Meganathan R.;
RT "Anaerobic biosynthesis of enterobactin Escherichia coli: regulation of
RT entC gene expression and evidence against its involvement in menaquinone
RT (vitamin K2) biosynthesis.";
RL J. Bacteriol. 178:3252-3259(1996).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9795253; DOI=10.1016/s0304-4165(98)00089-0;
RA Dahm C., Muller R., Schulte G., Schmidt K., Leistner E.;
RT "The role of isochorismate hydroxymutase genes entC and menF in
RT enterobactin and menaquinone biosynthesis in Escherichia coli.";
RL Biochim. Biophys. Acta 1425:377-386(1998).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17243787; DOI=10.1021/ja065064+;
RA Jiang M., Guo Z.;
RT "Effects of macromolecular crowding on the intrinsic catalytic efficiency
RT and structure of enterobactin-specific isochorismate synthase.";
RL J. Am. Chem. Soc. 129:730-731(2007).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=22096151; DOI=10.1099/mic.0.054361-0;
RA Orchard S.S., Rostron J.E., Segall A.M.;
RT "Escherichia coli enterobactin synthesis and uptake mutants are
RT hypersensitive to an antimicrobial peptide that limits the availability of
RT iron in addition to blocking Holliday junction resolution.";
RL Microbiology 158:547-559(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ALA-303; PHE-327; ILE-346 AND PHE-359, COFACTOR, SUBUNIT,
RP AND ACTIVE SITE.
RX PubMed=20079748; DOI=10.1016/j.jmb.2010.01.019;
RA Sridharan S., Howard N., Kerbarh O., Blaszczyk M., Abell C., Blundell T.L.;
RT "Crystal structure of Escherichia coli enterobactin-specific isochorismate
RT synthase (EntC) bound to its reaction product isochorismate: implications
RT for the enzyme mechanism and differential activity of chorismate-utilizing
RT enzymes.";
RL J. Mol. Biol. 397:290-300(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine).
CC Catalyzes the reversible conversion of chorismate to isochorismate.
CC {ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748,
CC ECO:0000269|PubMed:2139795, ECO:0000269|PubMed:2536681,
CC ECO:0000269|PubMed:8655506, ECO:0000269|PubMed:9795253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC Evidence={ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748,
CC ECO:0000269|PubMed:2139795};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20079748};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for isochorismate (at pH 7.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2139795};
CC KM=7 uM for chorismate {ECO:0000269|PubMed:20079748};
CC KM=14 uM for chorismate (at pH 7.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2139795};
CC KM=41 uM for chorismate {ECO:0000269|PubMed:17243787};
CC Note=kcat is 290 min(-1) for mutase activity with chorismate. kcat is
CC 173 min(-1) for mutase activity with chorismate (at pH 7.8 and 37
CC degrees Celsius). kcat is 108 min(-1) for mutase activity with
CC isochorismate (at pH 7.8 and 37 degrees Celsius). kcat is 37 min(-1)
CC for mutase activity with chorismate. {ECO:0000269|PubMed:17243787,
CC ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20079748,
CC ECO:0000269|PubMed:2139795}.
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC {ECO:0000269|PubMed:2521621, ECO:0000269|PubMed:8655506}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC enterobactin and are hypersensitive to the antimicrobial peptide
CC wrwycr. {ECO:0000269|PubMed:22096151, ECO:0000269|PubMed:9795253}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40793.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M36700; AAA18491.1; -; Genomic_DNA.
DR EMBL; M24142; AAA16100.1; -; Unassigned_DNA.
DR EMBL; U82598; AAB40793.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73694.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76348.1; -; Genomic_DNA.
DR EMBL; X53274; CAA37371.1; -; Genomic_DNA.
DR PIR; JT0497; SYECIK.
DR RefSeq; NP_415125.1; NC_000913.3.
DR RefSeq; WP_000381303.1; NZ_SSZK01000032.1.
DR PDB; 3HWO; X-ray; 2.30 A; A/B=1-391.
DR PDB; 5JXZ; X-ray; 1.88 A; A/B=1-391.
DR PDB; 5JY4; X-ray; 2.11 A; A/B=1-391.
DR PDB; 5JY8; X-ray; 2.94 A; A/B=1-391.
DR PDB; 5JZD; X-ray; 2.30 A; A/B=1-391.
DR PDBsum; 3HWO; -.
DR PDBsum; 5JXZ; -.
DR PDBsum; 5JY4; -.
DR PDBsum; 5JY8; -.
DR PDBsum; 5JZD; -.
DR AlphaFoldDB; P0AEJ2; -.
DR SMR; P0AEJ2; -.
DR BioGRID; 4260986; 160.
DR DIP; DIP-47970N; -.
DR IntAct; P0AEJ2; 9.
DR STRING; 511145.b0593; -.
DR BindingDB; P0AEJ2; -.
DR ChEMBL; CHEMBL1075176; -.
DR PaxDb; P0AEJ2; -.
DR PRIDE; P0AEJ2; -.
DR EnsemblBacteria; AAC73694; AAC73694; b0593.
DR EnsemblBacteria; BAE76348; BAE76348; BAE76348.
DR GeneID; 945511; -.
DR KEGG; ecj:JW0585; -.
DR KEGG; eco:b0593; -.
DR PATRIC; fig|1411691.4.peg.1676; -.
DR EchoBASE; EB0257; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_6_6; -.
DR InParanoid; P0AEJ2; -.
DR OMA; TMWHLSS; -.
DR PhylomeDB; P0AEJ2; -.
DR BioCyc; EcoCyc:ENTC-MON; -.
DR BioCyc; MetaCyc:ENTC-MON; -.
DR BRENDA; 5.4.4.2; 2026.
DR SABIO-RK; P0AEJ2; -.
DR UniPathway; UPA00017; -.
DR EvolutionaryTrace; P0AEJ2; -.
DR PRO; PR:P0AEJ2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008909; F:isochorismate synthase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR004561; IsoChor_synthase.
DR Pfam; PF00425; Chorismate_bind; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00543; isochor_syn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Enterobactin biosynthesis;
KW Isomerase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..391
FT /note="Isochorismate synthase EntC"
FT /id="PRO_0000154144"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000303|PubMed:20079748"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000303|PubMed:20079748"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20079748"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20079748"
FT MUTAGEN 303
FT /note="A->T: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:20079748"
FT MUTAGEN 304
FT /note="L->A: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:20079748"
FT MUTAGEN 327
FT /note="F->Y: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:20079748"
FT MUTAGEN 346
FT /note="I->L: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:20079748"
FT MUTAGEN 359
FT /note="F->Q: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:20079748"
FT CONFLICT 305..306
FT /note="SG -> TA (in Ref. 1; AAA18491)"
FT /evidence="ECO:0000305"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3HWO"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5JZD"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 146..160
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3HWO"
FT TURN 222..227
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 236..253
FT /evidence="ECO:0007829|PDB:3HWO"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:3HWO"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:3HWO"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3HWO"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:3HWO"
FT HELIX 370..388
FT /evidence="ECO:0007829|PDB:3HWO"
SQ SEQUENCE 391 AA; 42932 MW; 62882569DFC41AC4 CRC64;
MDTSLAEEVQ QTMATLAPNR FFFMSPYRSF TTSGCFARFD EPAVNGDSPD SPFQQKLAAL
FADAKAQGIK NPVMVGAIPF DPRQPSSLYI PESWQSFSRQ EKQASARRFT RSQSLNVVER
QAIPEQTTFE QMVARAAALT ATPQVDKVVL SRLIDITTDA AIDSGVLLER LIAQNPVSYN
FHVPLADGGV LLGASPELLL RKDGERFSSI PLAGSARRQP DEVLDREAGN RLLASEKDRH
EHELVTQAMK EVLRERSSEL HVPSSPQLIT TPTLWHLATP FEGKANSQEN ALTLACLLHP
TPALSGFPHQ AATQVIAELE PFDRELFGGI VGWCDSEGNG EWVVTIRCAK LRENQVRLFA
GAGIVPASSP LGEWRETGVK LSTMLNVFGL H
