(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 76.
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};
GN   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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:P0AEJ2}.
CC   -!- CATALYTIC ACTIVITY: Chorismate = isochorismate.
CC       {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}.
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_MWVM01000011.1.
DR   ProteinModelPortal; P0AEJ3; -.
DR   SMR; P0AEJ3; -.
DR   STRING; 155864.Z0735; -.
DR   EnsemblBacteria; AAG54928; AAG54928; Z0735.
DR   EnsemblBacteria; BAB34055; BAB34055; BAB34055.
DR   GeneID; 916991; -.
DR   KEGG; ece:Z0735; -.
DR   KEGG; ecs:ECs0632; -.
DR   PATRIC; fig|386585.9.peg.742; -.
DR   eggNOG; ENOG4105E4F; Bacteria.
DR   eggNOG; COG1169; LUCA.
DR   HOGENOM; HOG000028185; -.
DR   KO; K02361; -.
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;
DR   PRODOM; P0AEJ3.
DR   SWISS-2DPAGE; P0AEJ3.
KW   Complete proteome; Enterobactin biosynthesis; Isomerase; Magnesium;
KW   Metal-binding.
FT   CHAIN         1    391       Isochorismate synthase EntC.
FT                                /FTId=PRO_0000154145.
FT   REGION      214    215       Substrate.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   ACT_SITE    147    147       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   ACT_SITE    197    197       Proton donor.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       140    140       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       142    142       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       145    145       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       146    146       Magnesium.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       241    241       Magnesium.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   METAL       376    376       Magnesium.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   BINDING     241    241       Substrate.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   BINDING     303    303       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   BINDING     347    347       Substrate.
FT                                {ECO:0000250|UniProtKB:P0AEJ2}.
FT   BINDING     361    361       Substrate; via amide nitrogen.
FT                                {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
//

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