ID E2NUZ7_CATMR Unreviewed; 159 AA. AC E2NUZ7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 11-DEC-2019, entry version 48. 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 ECO:0000313|EMBL:EEF92966.1}; GN ORFNames=CATMIT_02428 {ECO:0000313|EMBL:EEF92966.1}; OS Catenibacterium mitsuokai (strain DSM 15897 / JCM 10609 / CIP 106738 / OS RCA14-39). OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium. OX NCBI_TaxID=451640 {ECO:0000313|EMBL:EEF92966.1, ECO:0000313|Proteomes:UP000004579}; RN [1] {ECO:0000313|EMBL:EEF92966.1, ECO:0000313|Proteomes:UP000004579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15897 / JCM 10609 / CIP 106738 / RCA14-39 RC {ECO:0000313|Proteomes:UP000004579}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) 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, ECO:0000256|SAAS:SAAS00395140}. 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:0000256|HAMAP- CC Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00834013}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC 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:SAAS00109038}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00108990}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000256|HAMAP- CC Rule:MF_00151, ECO:0000256|SAAS:SAAS00580827}. 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:EEF92966.1}. 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; ACCK01000415; EEF92966.1; -; Genomic_DNA. DR EnsemblBacteria; EEF92966; EEF92966; CATMIT_02428. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000004579; 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; -; 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, ECO:0000256|SAAS:SAAS00109028}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00151, 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:EEF92966.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:EEF92966.1}. FT DOMAIN 5..132 FT /note="CTP_transf_like" FT /evidence="ECO:0000259|Pfam:PF01467" FT NP_BIND 9..10 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT NP_BIND 88..90 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT NP_BIND 123..129 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 9 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 17 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 41 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 73 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 87 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151" FT BINDING 98 FT /note="ATP" 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 159 AA; 18147 MW; B52D4B38D1FAC441 CRC64; MIKAVYTGTF DPVTNGHLDI IERASKMYDV LYVTIFINPH KTCLFSVEER IEMLREATKQ FPNVVIDESS ALAVEYAREV GAQVLVRGLR ATEDYNYESL MCFTNQYLDE GIETVFLMTR LAYTFVSSSF VKEIVSHNHS VEGLVPACVE EKLIKKYRG //