ID A0A3A1XUE9_9BIFI Unreviewed; 182 AA. AC A0A3A1XUE9; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 02-OCT-2024, entry version 19. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151}; DE EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00151}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151}; DE Short=PPAT {ECO:0000256|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000256|HAMAP-Rule:MF_00151}; GN ORFNames=CJI49_04495 {ECO:0000313|EMBL:RIY28819.1}; OS Bifidobacteriaceae bacterium NR016. OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae. OX NCBI_TaxID=2026093 {ECO:0000313|EMBL:RIY28819.1, ECO:0000313|Proteomes:UP000266350}; RN [1] {ECO:0000313|EMBL:RIY28819.1, ECO:0000313|Proteomes:UP000266350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NR016 {ECO:0000313|EMBL:RIY28819.1, RC ECO:0000313|Proteomes:UP000266350}; RA Vancuren S.J., Hill J.E.; RT "A comparative genomics approach to explaining the enigmatic role of RT Gardnerella vaginalis in the vaginal microbiome."; RL Submitted (AUG-2017) 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00029346, ECO:0000256|HAMAP- CC Rule:MF_00151}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00151}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000256|HAMAP- CC Rule:MF_00151}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RIY28819.1}. 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; NQOQ01000002; RIY28819.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3A1XUE9; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000266350; Unassembled WGS sequence. 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 NCBIfam; TIGR01510; coaD_prev_kdtB; 1. DR NCBIfam; TIGR00125; cyt_tran_rel; 1. 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00151}; KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP- KW Rule:MF_00151}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00151}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00151}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00151}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000313|EMBL:RIY28819.1}. FT DOMAIN 5..141 FT /note="Cytidyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF01467" FT BINDING 9..10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 9 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 98..100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 132..138 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT SITE 17 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" SQ SEQUENCE 182 AA; 19600 MW; DA100B39B03D40C7 CRC64; MTIAVCPGSY DPVTAGHLDV IQRCTHLFDE VHVLVAVNAA KTPLFSESER VKIIQEAINN LPQSQNSFNR DCKIVVTSTA GLITDYCTKV GATVIVKGLR QNGDYEAELG MALVNRKLAG IETLFLPADP VLEHVSSSVV KDVARHGGNV TGMVPDNVIP LLKKLFSEQS LGVDNNSSML NN //