ID COAD_GEOSM Reviewed; 161 AA. AC C6DZ58; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 08-MAY-2019, entry version 60. 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=GM21_2318; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Lovley D.; RT "Complete sequence of Geobacter sp. M21."; RL Submitted (JUL-2009) 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; CP001661; ACT18366.1; -; Genomic_DNA. DR RefSeq; WP_015837599.1; NC_012918.1. DR SMR; C6DZ58; -. DR STRING; 443144.GM21_2318; -. DR EnsemblBacteria; ACT18366; ACT18366; GM21_2318. DR KEGG; gem:GM21_2318; -. DR eggNOG; ENOG4108ZEF; Bacteria. DR eggNOG; COG0669; LUCA. DR HOGENOM; HOG000006518; -. DR KO; K00954; -. DR OMA; EFQMALM; -. DR BioCyc; GSP443144:G1GFA-2347-MONOMER; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000002380; 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 1 161 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_1000203423. FT NP_BIND 11 12 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT NP_BIND 90 92 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT NP_BIND 125 131 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 11 11 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 19 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 43 43 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 75 75 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00151}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00151}. FT BINDING 100 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00151}. FT SITE 19 19 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00151}. SQ SEQUENCE 161 AA; 18058 MW; A5F79047E03C69E5 CRC64; MPLKMAVYPG SFDPVTYGHL DIIDRGLKIF DGVIVAVARN SEKNALFSVQ ERIELLTEIL KDRPEARVET FDGLLVDYVR RVGASVIIRG LRAVSDFEFE FQLAQMNRNI TRDVETLFMM TSVPYSYLSS SIVKEVSCLN GPVDKLVPPL VKSALDAKFR G //