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 10-MAY-2017, entry version 64. 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; Proteobacteria; 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 CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000255|HAMAP-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 CC (R)-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. CC {ECO:0000255|HAMAP-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 ProteinModelPortal; B5YWD2; -. DR SMR; B5YWD2; -. DR EnsemblBacteria; ACI34683; ACI34683; ECH74115_5004. DR KEGG; ecf:ECH74115_5004; -. DR PATRIC; 18370573; VBIEscCol74651_4900. DR HOGENOM; HOG000006518; -. DR KO; K00954; -. 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-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd02163; PPAT; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium; KW Nucleotide-binding; Nucleotidyltransferase; Transferase. FT CHAIN 1 159 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_1000096789. FT NP_BIND 10 11 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT NP_BIND 89 91 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT NP_BIND 124 130 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 10 10 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 18 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 42 42 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 74 74 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 88 88 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 99 99 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT SITE 18 18 Transition state stabilizer. FT {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 //