ID   ENTD_SALAS              Reviewed;         232 AA.
AC   Q53636;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Enterobactin synthase component D {ECO:0000250|UniProtKB:P19925};
DE   AltName: Full=4'-phosphopantetheinyl transferase EntD {ECO:0000250|UniProtKB:P19925};
DE            EC=2.7.8.- {ECO:0000250|UniProtKB:P19925};
DE   AltName: Full=Enterochelin synthase D {ECO:0000250|UniProtKB:P19925};
GN   Name=entD {ECO:0000250|UniProtKB:P19925};
OS   Salmonella austin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=47066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Johansen K.A.;
RT   "entD enterobactin biosynthesis genes of enteric bacteria.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC       (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-
CC       dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding
CC       for the three catechol functionalities that provide hexadentate
CC       coordination for the tightly ligated iron(2+) atoms. Plays an essential
CC       role in the assembly of the enterobactin by catalyzing the transfer of
CC       the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-
CC       domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their
CC       holo-forms which make them competent for the activation of 2,3-
CC       dihydroxybenzoate (DHB) and L-serine, respectively.
CC       {ECO:0000250|UniProtKB:P19925}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[aryl-carrier protein] + CoA = adenosine 3',5'-
CC         bisphosphate + H(+) + holo-[aryl-carrier protein];
CC         Xref=Rhea:RHEA:48404, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17557,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC         Evidence={ECO:0000250|UniProtKB:P19925};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[peptidyl-carrier protein] + CoA = adenosine 3',5'-
CC         bisphosphate + H(+) + holo-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:46228, Rhea:RHEA-COMP:11479, Rhea:RHEA-COMP:11480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC         Evidence={ECO:0000250|UniProtKB:P19925};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P24224};
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:P19925}.
CC   -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex called
CC       enterobactin synthase. {ECO:0000250|UniProtKB:P19925}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19925}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family.
CC       {ECO:0000250|UniProtKB:P19925}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97935.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U52685; AAA97935.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q53636; -.
DR   SMR; Q53636; -.
DR   UniPathway; UPA00017; -.
DR   GO; GO:0009366; C:enterobactin synthetase complex; ISS:UniProtKB.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.90.470.20; -; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR041354; 4PPT_N.
DR   InterPro; IPR003542; Enbac_synth_compD-like.
DR   PANTHER; PTHR38096; PTHR38096; 1.
DR   Pfam; PF17837; 4PPT_N; 1.
DR   Pfam; PF01648; ACPS; 1.
DR   PRINTS; PR01399; ENTSNTHTASED.
DR   SUPFAM; SSF56214; SSF56214; 1.
PE   3: Inferred from homology;
KW   Enterobactin biosynthesis; Magnesium; Membrane; Metal-binding; Transferase.
FT   CHAIN           1..232
FT                   /note="Enterobactin synthase component D"
FT                   /id="PRO_0000206071"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   232 AA;  25556 MW;  E5F6EDB5FE61BF68 CRC64;
     MLTSHFPLSF AGHRLHIVDF DASSFHEHDL LWLPHHDRLR SAGRKRKAEH LAGRIAAVHA
     LRRWASGVPG IGDKRQPLWP DDLFGSISHC ASTALAVISR QRVGVDIEKI MSQHTATELA
     VIIDSDEPQI LQASSLPFPL ALTLAFSAKE SVYKAFSDRV SLPGFDSAKV TSLTATHISL
     HLLPAFAATM AERTVRTEWF QRGNSVITLV SALTRWPHDR SAPASILSAI PR