ID COAD_SHEB9 Reviewed; 163 AA. AC A9KWX0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 16-JAN-2019, entry version 69. 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=Sbal195_4471; OS Shewanella baltica (strain OS195). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399599; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS195; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., RA Hofle M., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS195."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. 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: CC Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho- CC CoA + 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 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; CP000891; ABX51628.1; -; Genomic_DNA. DR RefSeq; WP_006084735.1; NC_009997.1. DR ProteinModelPortal; A9KWX0; -. DR SMR; A9KWX0; -. DR EnsemblBacteria; ABX51628; ABX51628; Sbal195_4471. DR GeneID; 11774424; -. DR KEGG; sbn:Sbal195_4471; -. DR HOGENOM; HOG000006518; -. DR KO; K00954; -. DR OMA; EFQMALM; -. DR BioCyc; SBAL399599:G1GAL-4669-MONOMER; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000000770; Chromosome. 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; -; 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 PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1. 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; Complete proteome; Cytoplasm; KW Magnesium; Nucleotide-binding; Nucleotidyltransferase; Transferase. FT CHAIN 1 163 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_1000076786. 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 163 AA; 17953 MW; FF4C4BAF173EA412 CRC64; MHTRAIYPGT FDPITNGHAD LIERAAKLFK HVIIGIAANP SKQPRFTLEE RVELVNRVTA HLDNVEVVGF SGLLVDFAKE QKASVLVRGL RAVSDFEYEF QLANMNRRLS PDLESVFLTP AEENSFISST LVKEVALHGG DVSQFVHSEV ATALAAKLKL AKP //