ENTD_SHIFL
ID ENTD_SHIFL Reviewed; 206 AA.
AC P0A3C0; Q54153; Q8XBW8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=SF0495, S0501;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAA97936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN42145.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP16017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U52684; AAA97936.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE005674; AAN42145.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP16017.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_706438.2; NC_004337.2.
DR RefSeq; WP_001506608.1; NZ_WPGW01000132.1.
DR AlphaFoldDB; P0A3C0; -.
DR SMR; P0A3C0; -.
DR STRING; 198214.SF0495; -.
DR EnsemblBacteria; AAN42145; AAN42145; SF0495.
DR EnsemblBacteria; AAP16017; AAP16017; S0501.
DR GeneID; 1023411; -.
DR GeneID; 58391511; -.
DR KEGG; sfl:SF0495; -.
DR KEGG; sfx:S0501; -.
DR PATRIC; fig|198214.7.peg.573; -.
DR HOGENOM; CLU_075076_1_0_6; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 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..206
FT /note="Enterobactin synthase component D"
FT /id="PRO_0000206074"
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 27..28
FT /note="EQ -> DE (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..50
FT /note="TEH -> AED (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="V -> I (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> T (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="A -> G (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> E (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="T -> I (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="D -> Y (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="C -> S (in Ref. 1; AAA97936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23131 MW; 68005CD6E9C6AE0C CRC64;
MKTTHTSLPF AGHTLHFVEF DPANFCEQDL LWLPHYAQLQ HAGRKRKTEH LAGRIAAVYA
LREYGYKCVP AIGELRQPVW PAEVYGSISH CGATALAVVS RQPIGVDIEE IFSAQTATEL
TDNIITPAEH ERLADCGLAF SLALTLAFSA KESAFKASEI QTDAGFLDYQ IISWNKQQVI
IHRENEMFAV HWQIKEKIVI TLCQHD
