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 02-NOV-2016, entry version 72.
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_LPWC02000002.1.
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; 18350250; VBIEscCol44059_0644.
DR eggNOG; ENOG4105E4F; Bacteria.
DR eggNOG; COG1169; LUCA.
DR HOGENOM; HOG000028185; -.
DR KO; K02361; -.
DR OMA; MWHLSSR; -.
DR BioCyc; ECOO157:ENTC-MONOMER; -.
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 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}.
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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