ID S5R0Y9_9PROT Unreviewed; 222 AA. AC S5R0Y9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 02-JUN-2021, entry version 39. DE RecName: Full=4'-phosphopantetheinyl transferase EntD {ECO:0000256|ARBA:ARBA00015433}; DE AltName: Full=Enterobactin synthase component D {ECO:0000256|ARBA:ARBA00019087}; DE AltName: Full=Enterochelin synthase D {ECO:0000256|ARBA:ARBA00019296}; GN Name=dipB {ECO:0000313|EMBL:AGS06837.1}; GN ORFNames=SSDC_00720 {ECO:0000313|EMBL:AGS06837.1}; OS Candidatus Profftella armatura. OC Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Profftella. OX NCBI_TaxID=669502 {ECO:0000313|EMBL:AGS06837.1, ECO:0000313|Proteomes:UP000015216}; RN [1] {ECO:0000313|EMBL:AGS06837.1, ECO:0000313|Proteomes:UP000015216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC {ECO:0000313|EMBL:AGS06837.1, RC ECO:0000313|Proteomes:UP000015216}; RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027; RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M., RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H., RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.; RT "Defensive bacteriome symbiont with a drastically reduced genome."; RL Curr. Biol. 23:1478-1484(2013). 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:0000256|ARBA:ARBA00003937}. CC -!- CATALYTIC ACTIVITY: CC Reaction=apo-[EntB isochorismatase/aryl-carrier protein] + CoA = CC adenosine 3',5'-bisphosphate + H(+) + holo-[EntB CC isochorismatase/aryl-carrier protein]; Xref=Rhea:RHEA:48404, CC Rhea:RHEA-COMP:12097, Rhea:RHEA-COMP:12099, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:64479; Evidence={ECO:0000256|ARBA:ARBA00001061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=apo-[EntF peptidyl-carrier protein] + CoA = adenosine 3',5'- CC bisphosphate + H(+) + holo-[EntF peptidyl-carrier protein]; CC Xref=Rhea:RHEA:48408, Rhea:RHEA-COMP:12098, Rhea:RHEA-COMP:12100, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; CC Evidence={ECO:0000256|ARBA:ARBA00000844}; CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}. CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. CC {ECO:0000256|ARBA:ARBA00004993}. CC -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex called CC enterobactin synthase. {ECO:0000256|ARBA:ARBA00011503}. CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family. CC {ECO:0000256|ARBA:ARBA00008342}. 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; CP003468; AGS06837.1; -; Genomic_DNA. DR RefSeq; WP_020915412.1; NZ_CP012591.1. DR STRING; 669502.SSDC_00720; -. DR KEGG; ssdc:SSDC_00720; -. DR eggNOG; COG2977; Bacteria. DR HOGENOM; CLU_1243455_0_0_4; -. DR OrthoDB; 1542506at2; -. DR BioCyc; CPRO669502:G1HJE-149-MONOMER; -. DR UniPathway; UPA00017; -. DR Proteomes; UP000015216; Chromosome. DR GO; GO:0009366; C:enterobactin synthetase complex; IEA:InterPro. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0009239; P:enterobactin biosynthetic process; IEA:UniProtKB-UniPathway. 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 {ECO:0000256|ARBA:ARBA00023191}; KW Reference proteome {ECO:0000313|Proteomes:UP000015216}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGS06837.1}. FT DOMAIN 39..105 FT /note="4PPT_N" FT /evidence="ECO:0000259|Pfam:PF17837" FT DOMAIN 115..195 FT /note="ACPS" FT /evidence="ECO:0000259|Pfam:PF01648" SQ SEQUENCE 222 AA; 25958 MW; 504F3211C21F045F CRC64; MNIKEDKIIA NINNILYKWF PKKTFIETAK IDNYPILPEE KKLVINAVSK RKKEFSTGRW LSRKGLKYFG FPETEILTGY LKNPIWPDKI NGSISHDNKL CTVVIMKKIP FLTNIGIDII YFPKYSNKLK YLESMFVINK NEIDIMDKFG LNIDSSTILF SVKESIIKAI SSEINNFIDM RDIKIFYENK KIQFIIQNKK PNVDIFAGIS YNYLITAVKI YN //