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 22-FEB-2023, entry version 70. 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. 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=(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; CP001661; ACT18366.1; -; Genomic_DNA. DR RefSeq; WP_015837599.1; NC_012918.1. DR AlphaFoldDB; C6DZ58; -. DR SMR; C6DZ58; -. DR STRING; 443144.GM21_2318; -. DR EnsemblBacteria; ACT18366; ACT18366; GM21_2318. DR KEGG; gem:GM21_2318; -. DR eggNOG; COG0669; Bacteria. DR HOGENOM; CLU_100149_0_1_7; -. DR OMA; EFQMALM; -. DR OrthoDB; 9806661at2; -. 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 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. 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 BINDING 11..12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 90..92 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151" FT BINDING 125..131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 //