ENTD_ECOLI
ID ENTD_ECOLI Reviewed; 206 AA.
AC P19925; P77092;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Enterobactin synthase component D {ECO:0000303|PubMed:9485415};
DE AltName: Full=4'-phosphopantetheinyl transferase EntD {ECO:0000303|PubMed:9485415};
DE EC=2.7.8.- {ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
DE AltName: Full=Enterochelin synthase D {ECO:0000303|PubMed:9485415};
GN Name=entD {ECO:0000303|PubMed:2533240}; OrderedLocusNames=b0583, JW5085;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2533240; DOI=10.1099/00221287-136-8-1667;
RA Coderre P.E., Earhart C.F.;
RT "The entD gene of the Escherichia coli K12 enterobactin gene cluster.";
RL J. Gen. Microbiol. 135:3043-3055(1989).
RN [2]
RP ERRATUM OF PUBMED:2533240.
RA Coderre P.E., Earhart C.F.;
RL J. Gen. Microbiol. 136:1667-1667(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=2526281; DOI=10.1111/j.1365-2958.1989.tb00224.x;
RA Armstrong S.K., Pettis G.S., Forrester L.J., McIntosh M.A.;
RT "The Escherichia coli enterobactin biosynthesis gene, entD: nucleotide
RT sequence and membrane localization of its protein product.";
RL Mol. Microbiol. 3:757-766(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP FUNCTION.
RX PubMed=8939709; DOI=10.1016/s1074-5521(96)90181-7;
RA Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
RA Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
RT "A new enzyme superfamily -- the phosphopantetheinyl transferases.";
RL Chem. Biol. 3:923-936(1996).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=BL21-DE3;
RX PubMed=9214294; DOI=10.1021/bi970453p;
RA Gehring A.M., Bradley K.A., Walsh C.T.;
RT "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB)
RT is a bifunctional enzyme that is phosphopantetheinylated by EntD and then
RT acylated by EntE using ATP and 2,3-dihydroxybenzoate.";
RL Biochemistry 36:8495-8503(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9485415; DOI=10.1021/bi9726584;
RA Gehring A.M., Mori I., Walsh C.T.;
RT "Reconstitution and characterization of the Escherichia coli enterobactin
RT synthetase from EntB, EntE, and EntF.";
RL Biochemistry 37:2648-2659(1998).
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:0000269|PubMed:8939709, ECO:0000269|PubMed:9214294,
CC ECO:0000269|PubMed:9485415}.
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:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
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:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P24224};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 uM for EntB (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9214294};
CC Note=kcat is 5.1 min(-1) for transferase activity with EntB as
CC substrate (at pH 7.5 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:9214294};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000305|PubMed:9214294}.
CC -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex called
CC enterobactin synthase. {ECO:0000269|PubMed:9485415}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2526281}.
CC -!- MISCELLANEOUS: Deletion of the C-terminal 25 residues of EntB results
CC in very strong decrease of the catalytic efficiency of EntD.
CC {ECO:0000269|PubMed:9214294}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40782.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA35224.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB57861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17426; CAB57861.1; ALT_INIT; Genomic_DNA.
DR EMBL; U82598; AAB40782.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73684.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35224.2; ALT_INIT; Genomic_DNA.
DR PIR; E64791; E64791.
DR RefSeq; NP_415115.2; NC_000913.3.
DR RefSeq; WP_001749708.1; NZ_STEB01000047.1.
DR AlphaFoldDB; P19925; -.
DR SMR; P19925; -.
DR BioGRID; 4260709; 77.
DR BioGRID; 849580; 1.
DR IntAct; P19925; 1.
DR STRING; 511145.b0583; -.
DR PaxDb; P19925; -.
DR PRIDE; P19925; -.
DR EnsemblBacteria; AAC73684; AAC73684; b0583.
DR EnsemblBacteria; BAA35224; BAA35224; BAA35224.
DR GeneID; 945194; -.
DR KEGG; ecj:JW5085; -.
DR KEGG; eco:b0583; -.
DR PATRIC; fig|511145.12.peg.608; -.
DR EchoBASE; EB0258; -.
DR eggNOG; COG2977; Bacteria.
DR HOGENOM; CLU_075076_1_0_6; -.
DR InParanoid; P19925; -.
DR PhylomeDB; P19925; -.
DR BioCyc; EcoCyc:ENTD-MON; -.
DR BioCyc; MetaCyc:ENTD-MON; -.
DR BRENDA; 2.7.8.7; 2026.
DR UniPathway; UPA00017; -.
DR PRO; PR:P19925; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009366; C:enterobactin synthetase complex; IDA:EcoCyc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Enterobactin biosynthesis; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..206
FT /note="Enterobactin synthase component D"
FT /id="PRO_0000206069"
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 74..75
FT /note="EL -> DV (in Ref. 3; CAB57861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23259 MW; F2ED3F858A0C5DDF CRC64;
MKTTHTSLPF AGHTLHFVEF DPANFCEQDL LWLPHYAQLQ HAGRKRKTEH LAGRIAAVYA
LREYGYKCVP AIGELRQPVW PAEVYGSISH CGTTALAVVS RQPIGIDIEE IFSVQTAREL
TDNIITPAEH ERLADCGLAF SLALTLAFSA KESAFKASEI QTDAGFLDYQ IISWNKQQVI
IHRENEMFAV HWQIKEKIVI TLCQHD
