(data stored in ACNUC7421 zone)

SWISSPROT: ENTB_ECO57

ID   ENTB_ECO57              Reviewed;         285 AA.
AC   P0ADI5; P15048;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Enterobactin synthase component B {ECO:0000250|UniProtKB:P0ADI4};
DE            EC=6.3.2.14 {ECO:0000250|UniProtKB:P0ADI4};
DE   AltName: Full=Enterobactin biosynthesis bifunctional protein EntB {ECO:0000250|UniProtKB:P0ADI4};
DE   AltName: Full=Enterochelin synthase B {ECO:0000250|UniProtKB:P0ADI4};
DE   Includes:
DE     RecName: Full=Isochorismatase {ECO:0000250|UniProtKB:P0ADI4};
DE              EC=3.3.2.1 {ECO:0000250|UniProtKB:P0ADI4};
DE     AltName: Full=2,3-dihydro-2,3-dihydroxybenzoat synthase {ECO:0000250|UniProtKB:P0ADI4};
DE     AltName: Full=Isochorismate lyase {ECO:0000250|UniProtKB:P0ADI4};
DE   Includes:
DE     RecName: Full=Aryl carrier protein {ECO:0000250|UniProtKB:P0ADI4};
DE              Short=ArCP {ECO:0000250|UniProtKB:P0ADI4};
GN   Name=entB {ECO:0000250|UniProtKB:P0ADI4};
GN   OrderedLocusNames=Z0737, ECs0634;
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. EntB is a bifunctional protein that serves as an
CC       isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes
CC       the conversion of isochorismate to 2,3-dihydro-2,3-
CC       dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-
CC       dihydroxybenzoate (DHB). In the enterobactin assembly, EntB
CC       functions as an aryl carrier protein phosphopantetheinylated near
CC       the C terminus by EntD to yield holo-EntB, which is then acylated
CC       by EntE with 2,3-dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then
CC       this product will serve in the formation of the amide bond between
CC       2,3-dihydroxybenzoate (DHB) and L-serine.
CC       {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- CATALYTIC ACTIVITY: 6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine =
CC       enterobactin + 6 AMP + 6 diphosphate.
CC       {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- CATALYTIC ACTIVITY: Isochorismate + H(2)O = (2S,3S)-2,3-dihydroxy-
CC       2,3-dihydrobenzoate + pyruvate. {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0ADI4};
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme
CC       complex called enterobactin synthase. Dimer.
CC       {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- INDUCTION: Under conditions of iron deficiency and by the fur
CC       protein. {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
CC       serine of apo-EntB by EntD. Holo-EntB so formed is then acylated
CC       with 2,3-dihydroxybenzoate in a reaction catalyzed by EntE.
CC       {ECO:0000250|UniProtKB:P0ADI4}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       isochorismatase family. {ECO:0000250|UniProtKB:P0ADI4}.
DR   EMBL; AE005174; AAG54930.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34057.1; -; Genomic_DNA.
DR   PIR; B90708; B90708.
DR   PIR; F85558; F85558.
DR   RefSeq; NP_308661.1; NC_002695.1.
DR   RefSeq; WP_001007138.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; P0ADI5; -.
DR   SMR; P0ADI5; -.
DR   STRING; 155864.Z0737; -.
DR   EnsemblBacteria; AAG54930; AAG54930; Z0737.
DR   EnsemblBacteria; BAB34057; BAB34057; BAB34057.
DR   GeneID; 916993; -.
DR   KEGG; ece:Z0737; -.
DR   KEGG; ecs:ECs0634; -.
DR   PATRIC; fig|386585.9.peg.744; -.
DR   eggNOG; ENOG4105WQI; Bacteria.
DR   eggNOG; COG1535; LUCA.
DR   eggNOG; COG3433; LUCA.
DR   HOGENOM; HOG000078667; -.
DR   KO; K01252; -.
DR   UniPathway; UPA00017; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; ISS:UniProtKB.
DR   GO; GO:0008908; F:isochorismatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR016291; Isochorismatase.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43540:SF3; PTHR43540:SF3; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001111; Isochorismatase; 1.
DR   PRINTS; PR01398; ISCHRISMTASE.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52499; SSF52499; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0ADI5.
DR   SWISS-2DPAGE; P0ADI5.
KW   Complete proteome; Cytoplasm; Enterobactin biosynthesis; Hydrolase;
KW   Ligase; Magnesium; Metal-binding; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P0ADI4}.
FT   CHAIN         2    285       Enterobactin synthase component B.
FT                                /FTId=PRO_0000201823.
FT   DOMAIN      209    284       Carrier. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   REGION        2    213       Isochorismatase.
FT                                {ECO:0000250|UniProtKB:P0ADI4}.
FT   METAL       227    227       Magnesium.
FT                                {ECO:0000250|UniProtKB:P0ADI4}.
FT   METAL       242    242       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0ADI4}.
FT   METAL       244    244       Magnesium.
FT                                {ECO:0000250|UniProtKB:P0ADI4}.
FT   MOD_RES     245    245       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   285 AA;  32554 MW;  E98C62D5ED23BAB1 CRC64;
     MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC PMMEQVIANI
     AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT RSPEQQKVVD RLTPDADDTV
     LVKWRYSAFH RSPLEQMLKE SGRNQLIITG VYAHIGCMTT ATDAFMRDIK PFMVADALAD
     FSRDEHLMSL KYVAGRSGRV VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID
     YGLDSVRMMA LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
//

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