ENTD_SALTY
ID ENTD_SALTY Reviewed; 234 AA.
AC Q56064;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
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}; OrderedLocusNames=STM0584;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Johansen K.A.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U52686; AAA97937.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19535.1; -; Genomic_DNA.
DR RefSeq; NP_459576.1; NC_003197.2.
DR RefSeq; WP_000958064.1; NC_003197.2.
DR AlphaFoldDB; Q56064; -.
DR SMR; Q56064; -.
DR STRING; 99287.STM0584; -.
DR PaxDb; Q56064; -.
DR EnsemblBacteria; AAL19535; AAL19535; STM0584.
DR GeneID; 1252104; -.
DR KEGG; stm:STM0584; -.
DR PATRIC; fig|99287.12.peg.616; -.
DR HOGENOM; CLU_075076_1_0_6; -.
DR OMA; WFGSISH; -.
DR PhylomeDB; Q56064; -.
DR BioCyc; SENT99287:STM0584-MON; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000001014; Chromosome.
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 GO; GO:0009237; P:siderophore metabolic process; IBA:GO_Central.
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;
KW Reference proteome; Transferase.
FT CHAIN 1..234
FT /note="Enterobactin synthase component D"
FT /id="PRO_0000206073"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 63..68
FT /note="EVGVRT -> RWASG (in Ref. 1; AAA97937)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="M -> I (in Ref. 1; AAA97937)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="PS -> V (in Ref. 1; AAA97937)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..130
FT /note="ER -> DA (in Ref. 1; AAA97937)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..185
FT /note="SDRVTLPGFNSAKVTSLTATHISLHLL -> QTASRSRDSIAQKLPRLPPRT
FT SRYICW (in Ref. 1; AAA97937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 25826 MW; CDDE500DDB92E416 CRC64;
MLTSHFPLPF AGHRLHIVDF DASSFREHDL LWLPHHDRLR SAGRKRKAEH LAGRIAAVHA
LREVGVRTVP GMGDKRQPLW PDGLFGSISH CATTALAVIS RQRIGIDIEK IMSQHTATEL
APSIIDSDER QILQASLLPF PLALTLAFSA KESVYKAFSD RVTLPGFNSA KVTSLTATHI
SLHLLPAFAA TMAERTVRTE WFQRDNSVIT LVSAITRVPH DRSAPASILS AIPR
