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 26-FEB-2020, entry version 63. 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}; OrderedLocusNames=GM21_2318; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter; unclassified 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., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA 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 pyrophosphate. CC {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-pantetheine 4'-phosphate + 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; 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; CLU_100149_0_1_7; -. 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; Cytoplasm; Magnesium; KW Nucleotide-binding; Nucleotidyltransferase; Transferase. FT CHAIN 1..161 FT /note="Phosphopantetheine adenylyltransferase" FT /id="PRO_1000203423" FT NP_BIND 11..12 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT NP_BIND 90..92 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT NP_BIND 125..131 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 11 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 19 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 43 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 75 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 89 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 100 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT SITE 19 FT /note="Transition state stabilizer" FT /evidence="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 //