ID A0A3A1XUE9_9BIFI Unreviewed; 182 AA. AC A0A3A1XUE9; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 16-JAN-2019, entry version 2. 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; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae. OX NCBI_TaxID=2026093 {ECO:0000313|EMBL:RIY28819.1}; RN [1] {ECO:0000313|EMBL:RIY28819.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NR016 {ECO:0000313|EMBL:RIY28819.1}; 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 CC pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00109030}. 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:0000256|HAMAP- CC Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00151, ECO:0000256|SAAS:SAAS00834013}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00108991}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00395173}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00395134}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00580827}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 RefSeq; WP_012913867.1; NZ_NQOQ01000002.1. DR GeneID; 29692155; -. DR UniPathway; UPA00241; UER00355. 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 {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109018}; KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109017}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109028}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00834014}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109023}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109019, ECO:0000313|EMBL:RIY28819.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:RIY28819.1}. FT DOMAIN 6 141 CTP_transf_like. {ECO:0000259|Pfam: FT PF01467}. FT NP_BIND 9 10 ATP. {ECO:0000256|HAMAP-Rule:MF_00151}. FT NP_BIND 98 100 ATP. {ECO:0000256|HAMAP-Rule:MF_00151}. FT NP_BIND 132 138 ATP. {ECO:0000256|HAMAP-Rule:MF_00151}. FT BINDING 9 9 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00151}. FT BINDING 17 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00151}. FT BINDING 41 41 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00151}. FT BINDING 83 83 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00151}. FT BINDING 97 97 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00151}. FT BINDING 108 108 ATP. {ECO:0000256|HAMAP-Rule:MF_00151}. FT SITE 17 17 Transition state stabilizer. FT {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 //