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 02-NOV-2016, entry version 89.
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};
GN 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=10.1016/0378-1097(90)90120-F;
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;
RA Ozenberger B.A., Brickman T.J., McIntosh M.A.;
RT "Nucleotide sequence of Escherichia coli isochorismate synthetase gene
RT entC and evolutionary relationship of isochorismate synthetase and
RT other 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.,
RA Mau B., 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
RT MG1655 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-
RT entC 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,
RP BIOPHYSICOCHEMICAL 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;
RA Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Nucleotide sequence and transcriptional organization of the
RT Escherichia coli enterobactin biosynthesis cistrons entB and entA.";
RL J. Bacteriol. 171:784-790(1989).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=8655506;
RA Kwon O., Hudspeth M.E., Meganathan R.;
RT "Anaerobic biosynthesis of enterobactin Escherichia coli: regulation
RT of entC gene expression and evidence against its involvement in
RT menaquinone (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
RT efficiency and structure of enterobactin-specific isochorismate
RT 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
RT availability of iron in addition to blocking Holliday junction
RT 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
RP PROPERTIES, MUTAGENESIS OF ALA-303; PHE-327; ILE-346 AND PHE-359,
RP COFACTOR, SUBUNIT, 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.,
RA Blundell T.L.;
RT "Crystal structure of Escherichia coli enterobactin-specific
RT isochorismate synthase (EntC) bound to its reaction product
RT isochorismate: implications for the enzyme mechanism and differential
RT activity of chorismate-utilizing enzymes.";
RL J. Mol. Biol. 397:290-300(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore
CC enterobactin (macrocyclic trimeric lactone of N-(2,3-
CC dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of
CC chorismate to isochorismate. {ECO:0000269|PubMed:17243787,
CC ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795,
CC ECO:0000269|PubMed:2536681, ECO:0000269|PubMed:8655506,
CC ECO:0000269|PubMed:9795253}.
CC -!- CATALYTIC ACTIVITY: Chorismate = isochorismate.
CC {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.
CC Kcat is 173 min(-1) for mutase activity with chorismate (at pH
CC 7.8 and 37 degrees Celsius). Kcat is 108 min(-1) for mutase
CC activity with isochorismate (at pH 7.8 and 37 degrees Celsius).
CC Kcat is 37 min(-1) for mutase activity with chorismate.
CC {ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748,
CC 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
CC protein. {ECO:0000269|PubMed:2521621, ECO:0000269|PubMed:8655506}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to
CC produce enterobactin and are hypersensitive to the antimicrobial
CC peptide wrwycr. {ECO:0000269|PubMed:22096151,
CC 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
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_LN832404.1.
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 ProteinModelPortal; P0AEJ2; -.
DR SMR; P0AEJ2; -.
DR BioGrid; 4260986; 156.
DR DIP; DIP-47970N; -.
DR IntAct; P0AEJ2; 9.
DR MINT; MINT-1300552; -.
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; 32116362; VBIEscCol129921_0621.
DR EchoBASE; EB0257; -.
DR EcoGene; EG10261; entC.
DR eggNOG; ENOG4105E4F; Bacteria.
DR eggNOG; COG1169; LUCA.
DR HOGENOM; HOG000028185; -.
DR InParanoid; P0AEJ2; -.
DR KO; K02361; -.
DR OMA; MWHLSSR; -.
DR PhylomeDB; P0AEJ2; -.
DR BioCyc; EcoCyc:ENTC-MONOMER; -.
DR BioCyc; ECOL316407:JW0585-MONOMER; -.
DR BioCyc; MetaCyc:ENTC-MONOMER; -.
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:0005737; C:cytoplasm; IBA:GO_Central.
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 GO; GO:0009697; P:salicylic acid biosynthetic process; IBA:GO_Central.
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; Complete proteome; Direct protein sequencing;
KW Enterobactin biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1 391 Isochorismate synthase EntC.
FT /FTId=PRO_0000154144.
FT REGION 214 215 Substrate. {ECO:0000269|PubMed:20079748}.
FT ACT_SITE 147 147 Proton acceptor.
FT {ECO:0000303|PubMed:20079748}.
FT ACT_SITE 197 197 Proton donor.
FT {ECO:0000303|PubMed:20079748}.
FT METAL 140 140 Magnesium; via carbonyl oxygen.
FT {ECO:0000269|PubMed:20079748}.
FT METAL 142 142 Magnesium; via carbonyl oxygen.
FT {ECO:0000269|PubMed:20079748}.
FT METAL 145 145 Magnesium; via carbonyl oxygen.
FT {ECO:0000269|PubMed:20079748}.
FT METAL 146 146 Magnesium. {ECO:0000269|PubMed:20079748}.
FT METAL 241 241 Magnesium. {ECO:0000269|PubMed:20079748}.
FT METAL 376 376 Magnesium. {ECO:0000269|PubMed:20079748}.
FT BINDING 241 241 Substrate. {ECO:0000269|PubMed:20079748}.
FT BINDING 303 303 Substrate; via carbonyl oxygen.
FT {ECO:0000269|PubMed:20079748}.
FT BINDING 347 347 Substrate. {ECO:0000269|PubMed:20079748}.
FT BINDING 361 361 Substrate; via amide nitrogen.
FT {ECO:0000269|PubMed:20079748}.
FT MUTAGEN 303 303 A->T: Loss of mutase activity.
FT {ECO:0000269|PubMed:20079748}.
FT MUTAGEN 304 304 L->A: Loss of mutase activity.
FT {ECO:0000269|PubMed:20079748}.
FT MUTAGEN 327 327 F->Y: Loss of mutase activity.
FT {ECO:0000269|PubMed:20079748}.
FT MUTAGEN 346 346 I->L: Loss of mutase activity.
FT {ECO:0000269|PubMed:20079748}.
FT MUTAGEN 359 359 F->Q: Loss of mutase activity.
FT {ECO:0000269|PubMed:20079748}.
FT CONFLICT 305 306 SG -> TA (in Ref. 1; AAA18491).
FT {ECO:0000305}.
FT STRAND 22 24 {ECO:0000244|PDB:3HWO}.
FT STRAND 30 34 {ECO:0000244|PDB:3HWO}.
FT STRAND 36 39 {ECO:0000244|PDB:3HWO}.
FT TURN 44 47 {ECO:0000244|PDB:5JZD}.
FT HELIX 52 66 {ECO:0000244|PDB:3HWO}.
FT STRAND 73 78 {ECO:0000244|PDB:3HWO}.
FT STRAND 87 90 {ECO:0000244|PDB:3HWO}.
FT STRAND 92 96 {ECO:0000244|PDB:3HWO}.
FT HELIX 99 108 {ECO:0000244|PDB:3HWO}.
FT STRAND 117 124 {ECO:0000244|PDB:3HWO}.
FT HELIX 126 141 {ECO:0000244|PDB:3HWO}.
FT STRAND 142 144 {ECO:0000244|PDB:3HWO}.
FT STRAND 146 160 {ECO:0000244|PDB:3HWO}.
FT HELIX 164 174 {ECO:0000244|PDB:3HWO}.
FT STRAND 176 184 {ECO:0000244|PDB:3HWO}.
FT STRAND 186 188 {ECO:0000244|PDB:3HWO}.
FT STRAND 190 195 {ECO:0000244|PDB:3HWO}.
FT STRAND 198 203 {ECO:0000244|PDB:3HWO}.
FT STRAND 206 210 {ECO:0000244|PDB:3HWO}.
FT STRAND 212 217 {ECO:0000244|PDB:3HWO}.
FT TURN 222 227 {ECO:0000244|PDB:3HWO}.
FT HELIX 228 234 {ECO:0000244|PDB:3HWO}.
FT HELIX 236 253 {ECO:0000244|PDB:3HWO}.
FT TURN 254 256 {ECO:0000244|PDB:3HWO}.
FT STRAND 257 261 {ECO:0000244|PDB:3HWO}.
FT STRAND 267 270 {ECO:0000244|PDB:3HWO}.
FT STRAND 272 278 {ECO:0000244|PDB:3HWO}.
FT STRAND 281 285 {ECO:0000244|PDB:3HWO}.
FT HELIX 291 298 {ECO:0000244|PDB:3HWO}.
FT TURN 302 304 {ECO:0000244|PDB:3HWO}.
FT STRAND 305 308 {ECO:0000244|PDB:3HWO}.
FT HELIX 309 319 {ECO:0000244|PDB:3HWO}.
FT TURN 325 328 {ECO:0000244|PDB:3HWO}.
FT STRAND 329 335 {ECO:0000244|PDB:3HWO}.
FT STRAND 340 344 {ECO:0000244|PDB:3HWO}.
FT STRAND 347 352 {ECO:0000244|PDB:3HWO}.
FT STRAND 355 364 {ECO:0000244|PDB:3HWO}.
FT HELIX 370 388 {ECO:0000244|PDB:3HWO}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 126 380 ipfam:Chorismate_bind [T]
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
//
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