ID COAD_ECO5E Reviewed; 159 AA. AC B5YWD2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 08-NOV-2023, entry version 87. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; GN OrderedLocusNames=ECH74115_5004; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RX PubMed=22135463; DOI=10.1073/pnas.1107176108; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. CC {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, CC ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00151}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00151}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP- CC Rule:MF_00151}. 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; CP001164; ACI34683.1; -; Genomic_DNA. DR RefSeq; WP_001171866.1; NC_011353.1. DR AlphaFoldDB; B5YWD2; -. DR SMR; B5YWD2; -. DR GeneID; 82264242; -. DR KEGG; ecf:ECH74115_5004; -. DR HOGENOM; CLU_100149_0_1_6; -. DR OMA; EFQMALM; -. DR UniPathway; UPA00241; UER00355. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02163; PPAT; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; PPAT. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR01510; coaD_prev_kdtB; 1. DR NCBIfam; TIGR00125; cyt_tran_rel; 1. DR PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1. DR PANTHER; PTHR21342:SF1; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium; KW Nucleotide-binding; Nucleotidyltransferase; Transferase. FT CHAIN 1..159 FT /note="Phosphopantetheine adenylyltransferase" FT /id="PRO_1000096789" FT BINDING 10..11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 10 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 89..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 99 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 124..130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT SITE 18 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" SQ SEQUENCE 159 AA; 17837 MW; C4D7B8715A061B91 CRC64; MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE RVALAQQATA HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM QLAHMNRHLM PELESVFLMP SKEWSFISSS LVKEVARHQG DVTHFLPENV HQALMAKLA //