ENTC_ECO57
ID ENTC_ECO57 Reviewed; 391 AA.
AC P0AEJ3; P10377; P77099;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Isochorismate synthase EntC {ECO:0000250|UniProtKB:P0AEJ2};
DE EC=5.4.4.2 {ECO:0000250|UniProtKB:P0AEJ2};
DE AltName: Full=Isochorismate mutase {ECO:0000250|UniProtKB:P0AEJ2};
GN Name=entC {ECO:0000250|UniProtKB:P0AEJ2}; OrderedLocusNames=Z0735, ECs0632;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:P0AEJ2}.
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:0000250|UniProtKB:P0AEJ2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AEJ2};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P0AEJ2}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AEJ2}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {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; AE005174; AAG54928.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34055.1; -; Genomic_DNA.
DR PIR; D85558; D85558.
DR PIR; H90707; H90707.
DR RefSeq; NP_308659.1; NC_002695.1.
DR RefSeq; WP_000381303.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEJ3; -.
DR SMR; P0AEJ3; -.
DR STRING; 155864.EDL933_0663; -.
DR EnsemblBacteria; AAG54928; AAG54928; Z0735.
DR EnsemblBacteria; BAB34055; BAB34055; ECs_0632.
DR GeneID; 916991; -.
DR KEGG; ece:Z0735; -.
DR KEGG; ecs:ECs_0632; -.
DR PATRIC; fig|386585.9.peg.742; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_6_6; -.
DR OMA; TMWHLSS; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008909; F:isochorismate synthase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
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 3: Inferred from homology;
KW Enterobactin biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..391
FT /note="Isochorismate synthase EntC"
FT /id="PRO_0000154145"
FT REGION 214..215
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ2"
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
