(data stored in ACNUC7421 zone)

SWISSPROT: ENTE_ECO57

ID   ENTE_ECO57              Reviewed;         536 AA.
AC   Q8XBV3;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 94.
DE   RecName: Full=Enterobactin synthase component E {ECO:0000250|UniProtKB:P10378};
DE            EC=6.3.2.14 {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=2,3-dihydroxybenzoate-AMP liase {ECO:0000250|UniProtKB:P10378};
DE            Short=DHB-AMP ligase {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=2,3-dihydroxybenzoate-AMP synthase {ECO:0000250|UniProtKB:P10378};
DE            EC=2.7.7.58 {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=Dihydroxybenzoic acid-activating enzyme {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=Enterochelin synthase E {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=S-dihydroxybenzoyltransferase {ECO:0000250|UniProtKB:P10378};
DE            EC=2.5.1.- {ECO:0000250|UniProtKB:P10378};
GN   Name=entE {ECO:0000250|UniProtKB:P10378};
GN   OrderedLocusNames=Z0736, ECs0633;
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 (enterochelin), which is a macrocyclic trimeric
CC       lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone
CC       serves as a scaffolding for the three catechol functionalities
CC       that provide hexadentate coordination for the tightly ligated
CC       iron(2+) atoms. EntE proccesses via a two-step adenylation-
CC       ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it
CC       catalyzes the activation of the carboxylate group of 2,3-
CC       dihydroxy-benzoate (DHB), via a reversible ATP-dependent
CC       pyrophosphate exchange reactions to yield the acyladenylate
CC       intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to
CC       salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-
CC       trihydroxybenzoate. In the second step, DHB is transferred from
CC       2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB
CC       (holo-EntB) to form DHB-holo-EntB. Then this product will serve in
CC       the formation of the amide bond between 2,3-dihydroxybenzoate
CC       (DHB) and L-serine. {ECO:0000250|UniProtKB:P10378}.
CC   -!- CATALYTIC ACTIVITY: 6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine =
CC       enterobactin + 6 AMP + 6 diphosphate.
CC       {ECO:0000250|UniProtKB:P10378}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2,3-dihydroxybenzoate = diphosphate +
CC       (2,3-dihydroxybenzoyl)adenylate. {ECO:0000250|UniProtKB:P10378}.
CC   -!- CATALYTIC ACTIVITY: (2,3-dihydroxybenzoyl)adenylate + holo-entB =
CC       adenosine 5'-monophosphate + aryl-holo-entB.
CC       {ECO:0000250|UniProtKB:P10378}.
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:P10378}.
CC   -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme
CC       complex called enterobactin synthase. Monomer. EntA and EntE
CC       interact together. {ECO:0000250|UniProtKB:P10378}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10378}.
CC   -!- INDUCTION: Under conditions of iron deficiency and by the fur
CC       protein. {ECO:0000250|UniProtKB:P10378}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. EntE subfamily. {ECO:0000250|UniProtKB:P10378}.
DR   EMBL; AE005174; AAG54929.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34056.1; -; Genomic_DNA.
DR   PIR; A99708; A99708.
DR   PIR; E85558; E85558.
DR   RefSeq; NP_308660.1; NC_002695.1.
DR   RefSeq; WP_000026781.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBV3; -.
DR   SMR; Q8XBV3; -.
DR   STRING; 155864.Z0736; -.
DR   PRIDE; Q8XBV3; -.
DR   EnsemblBacteria; AAG54929; AAG54929; Z0736.
DR   EnsemblBacteria; BAB34056; BAB34056; BAB34056.
DR   GeneID; 916992; -.
DR   KEGG; ece:Z0736; -.
DR   KEGG; ecs:ECs0633; -.
DR   PATRIC; fig|386585.9.peg.743; -.
DR   eggNOG; ENOG4108IQC; Bacteria.
DR   eggNOG; COG1021; LUCA.
DR   HOGENOM; HOG000230011; -.
DR   KO; K02363; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; ISS:UniProtKB.
DR   GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR011963; DHB_AMP_lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02275; DHB_AMP_lig; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XBV3.
DR   SWISS-2DPAGE; Q8XBV3.
KW   Acyltransferase; ATP-binding; Complete proteome;
KW   Enterobactin biosynthesis; Ligase; Membrane; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    536       Enterobactin synthase component E.
FT                                /FTId=PRO_0000193076.
FT   REGION      438    439       Phosphopantetheine binding.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     235    235       Substrate.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     240    240       Substrate.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     309    309       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     331    331       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     335    335       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     415    415       Substrate.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     432    432       Substrate.
FT                                {ECO:0000250|UniProtKB:P10378}.
FT   BINDING     441    441       Substrate.
FT                                {ECO:0000250|UniProtKB:P10378}.
SQ   SEQUENCE   536 AA;  59040 MW;  ABC8E0B3209940A5 CRC64;
     MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS YRELNQAADN
     LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP VLALFSHQRS ELNAYASQIE
     PALLIADRQH ALFSGDDFLN TFVAEHSSIR VVQLLNDSGE HNLQDAINHP ADGFTATPSP
     ADEVVYFQLS GGTTGTPKLI PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS
     PGSLGVFLAG GTVVLAADPS ATLCFPLIEK HQINVTALVP PAVSLWLQAL TEGESRAQLA
     SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK IIHTQGYPMC
     PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH NASAFDANGF YCSGDLISID
     PEGYITVQGR EKDQINRGGE KIAAEEIENL LLRHPAVIYA ALVSMEDELM GEKSCAYLVV
     KEPLRAVQVR RFLREQGIAE FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
//

If you have problems or comments...

PBIL Back to PBIL home page